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5-phospho-D-ribosyl diphosphate + H2O
?
40.73% activity compared to D-fructose 1,6-bisphosphate
-
-
?
beta-D-glucose 1,6-bisphosphate + H2O
D-glucose 6-phosphate + phosphate
beta-glycerophosphate + H2O
?
-
substrate at pH 9.0, no activity at pH 6.5
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
D-fructose 1,6-diphosphate + H2O
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
D-fructose 1-phosphate + H2O
D-fructose + phosphate
-
-
?
D-fructose 6-phosphate + phosphate
D-fructose 1,6-diphosphate + H2O
D-glucose 1,6-bisphosphate + H2O
D-glucose 6-phosphate + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
23% of the activity found with D-fructose 1,6-bisphosphate
-
?
D-glucose-1-phosphate + H2O
D-glucose + phosphate
-
-
?
glucose 1,6-diphosphate + H2O
?
-
about 10% of maximal activity
-
-
?
glyceraldehyde 3-phosphate + H2O
?
11.43% of the activity compared to D-fructose 1,6-bisphosphate
-
-
?
glycerol-2-phosphate + H2O
glycerol + phosphate
-
-
?
GTP + H2O
?
22.9% of the activity compared to D-fructose 1,6-bisphosphate
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
-
-
?
phosphoribosyl diphosphate + H2O
?
40.73% of the activity compared to D-fructose 1,6-bisphosphate
-
-
?
ribulose 1,5-bisphosphate + H2O
ribulose 5-phosphate + phosphate
15% of activity obtained with D-fructose 1,6-bisphosphate
-
?
ribulose 1,5-diphosphate + H2O
?
sedoheptulose 1,6-diphosphate + H2O
sedoheptulose 6-phosphate + phosphate
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
additional information
?
-
beta-D-glucose 1,6-bisphosphate + H2O
D-glucose 6-phosphate + phosphate
-
-
-
-
?
beta-D-glucose 1,6-bisphosphate + H2O
D-glucose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
E2RAN6
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Fbp plays a key role in gluconeogenesis that supplies cellular building blocks such as hexose and intermediates of the pentose phosphate pathway for cell growth. Fructose-1,6-bisphosphatase increases its abundance by 2.0-2.7fold on various aromatic compounds. Fbp plays a key role in aromatic assimilation by Coryneacterium glutamicum. The Fbp gene is disrupted and the mutant WTDfbp loses the ability to grow on aromatic compounds. Genetic complementation by the Fbp gene restores this ability
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
best substrate
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
enzyme functions with FBPase I in the centarle pathways of carbohydrate metabolism
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
enzyme is a part of Calvin cycle
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is highly specific for D-fructose 1,6-bisphosphate. At 1 mM substrate, activity is only 40% of the activity at 0.06 mM substrate
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
gluconeogenic enzyme
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
the the chloroplastic isozyme plays a key role in the Calvin cycle and the cytoplasmic isozyme plays a key role in the sucrose synthesis in cytoplasm
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
preferred substrate
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
key enzyme of the gluconeogenic pathway
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
the bifunctional, thermostable enzyme (EC 4.1.2.13/EC 3.1.3.11) catalyses two subsequent steps in gluconeogenesis in most archaea and in deeply branching bacterial lineages
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
the bifunctional, thermostable enzyme (EC 4.1.2.13/EC 3.1.3.11) catalyses two subsequent steps in gluconeogenesis. It catalyses a multi-step reaction by remodelling its active site according to the respective catalytic requirements
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
the bifunctional, thermostable enzyme (EC 4.1.2.13/EC 3.1.3.11) catalyses two subsequent steps in gluconeogenesis in most archaea and in deeply branching bacterial lineages
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
the bifunctional, thermostable enzyme (EC 4.1.2.13/EC 3.1.3.11) catalyses two subsequent steps in gluconeogenesis. It catalyses a multi-step reaction by remodelling its active site according to the respective catalytic requirements
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
regulatory enzyme of glyconeogenesis. FBPase participates in some nuclear processes during development and regeneration of skeletal muscle
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
the coregulation of phosphofructo 1-kinase I and fructose 1,6-bisphosphatase are required for the ability of these cells to respond to glucose and induce metabolic and Ca2+ signals that can be important for sperm development and function
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
best substrate
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
the substrate is bound in its linear, open conformation with the cleavable C1-phosphate positioned deep in the active site
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
one of the key enzymes in gluconeogenesis
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
the bifunctional enzyme also shows activity of EC 4.1.2.13. The crystal structures of the enzyme in the two forms reveals that it achieves its bifunctionality by transforming its active-site architecture, through the toggle switch-like motions of the three mobile loop regions
-
-
r
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
the bifunctional enzyme also shows activity of EC 4.1.2.13. The crystal structures of the enzyme in the two forms reveals that it achieves its bifunctionality by transforming its active-site architecture, through the toggle switch-like motions of the three mobile loop regions
-
-
r
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
r
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
FBPase contributes to the partitioning of the fixed carbon for ribulose-1,5-bisphosphate regeneration or starch synthesis
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
best substrate
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Thermosynechococcus vestitus
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
the enzyme plays a key role in the Calvin cycle
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
key regulatory enzyme in the control of the Emden-Meyerhof pathway
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
key regulatory enzyme in the control of the Emden-Meyerhof pathway
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
constitutive enzyme
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
the enzyme is involved in the futile cycling of fructose 6-phosphate and fructose 1,6-diphosphate in flight muscle, the net result of which is the hydrolysis of ATP
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
enzyme in gluconeogenic pathway
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
enzyme plays a key regulatory role in the futile cycle of fructose 1,6-diphosphate synthesis and degradation
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
the alkaline isoenzyme may have an important role in vivo in the regulation and control of glycolysis and glyconeogenesis
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
gluconeogenic enzyme
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
regulatory enzyme in gluconeogenesis
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
enzyme is involved in photosynthetic process
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
isoenzyme A is present when the organism is grown under autotrophic conditions but is not synthesized during heterotrophic growth. Isoenzyme B is detected in both autothrophically and heterotrophically grown organisms
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
the enzyme may be involved in the regulation of the Calvin-Bassham carbon reduction cycle
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
key regulatory enzyme in carbohydrate synthesis in both gluconeogenesis and photosynthesis
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
r
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
r
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is a part of Calvin cycle
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 6-phosphate + phosphate
D-fructose 1,6-diphosphate + H2O
-
-
-
r
D-fructose 6-phosphate + phosphate
D-fructose 1,6-diphosphate + H2O
-
-
-
-
r
ribulose 1,5-diphosphate + H2O
?
-
-
-
-
?
ribulose 1,5-diphosphate + H2O
?
-
intestinal and muscle enzyme
-
-
?
ribulose 1,5-diphosphate + H2O
?
-
-
-
-
?
ribulose 1,5-diphosphate + H2O
?
-
23% of the activity with fructose 1,6-diphosphate
-
-
?
ribulose 1,5-diphosphate + H2O
?
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
no activity
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
intestinal and muscle enzyme
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
81% of the activity with fructose 1,6-diphosphate
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
at 22.4% of the activity with fructose 1,6-diphosphate
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
about 5% of maximal activity
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
no activity
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
-
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
activity with isoenzyme F-1, no activity with isoenzyme F-II
-
-
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
no activity
-
-
?
additional information
?
-
-
role as a key enzyme in CO2 assimilation and also in coordinating carbon and nitrogen metabolism
-
-
?
additional information
?
-
-
bifunctional fructose 1,6-bisphosphate, FBP, aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity
-
-
?
additional information
?
-
I3DTM3
the chromosome-encoded isoform is the major fructose 1,6-bisphosphatase of Bacillus methanolicus
-
-
?
additional information
?
-
the chromosome-encoded isoform is the major fructose 1,6-bisphosphatase of Bacillus methanolicus
-
-
?
additional information
?
-
-
the chromosome-encoded isoform is the major fructose 1,6-bisphosphatase of Bacillus methanolicus
-
-
?
additional information
?
-
I3DTM3
the chromosome-encoded isoform is the major fructose 1,6-bisphosphatase of Bacillus methanolicus
-
-
?
additional information
?
-
the chromosome-encoded isoform is the major fructose 1,6-bisphosphatase of Bacillus methanolicus
-
-
?
additional information
?
-
-
bifunctional fructose 1,6-bisphosphate, FBP, aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity
-
-
?
additional information
?
-
-
enzyme together with phosphofructokinase plays a crucial role in metabolism of pancreatic islet cells
-
-
?
additional information
?
-
-
the FBP active site works by stabilizing the FBPase, and the allosteric site impairs the activity of FBPase through its binding of a nonsubstrate molecule. Competitive inhibition of AMP, fructose 1,6-bisphosphate, or fructose 6-phosphate binding to FBPase with fluorescent AMP analogue, 2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate (TNP-AMP)-binding FBPase
-
-
?
additional information
?
-
-
bifunctional fructose 1,6-bisphosphate, FBP, aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity
-
-
?
additional information
?
-
the higher Km for D-fructose 1,6-bisphosphate of LmFBPase compared to the Escherichia coli enzyme may be explained by a sequence difference at the active site, with Tyr221 replaced by Asn221 resulting in the loss of a direct hydrogen bond with substrate D-fructose 1,6-bisphosphate. Binding structure analysis of substrate and product, overview
-
-
?
additional information
?
-
-
the higher Km for D-fructose 1,6-bisphosphate of LmFBPase compared to the Escherichia coli enzyme may be explained by a sequence difference at the active site, with Tyr221 replaced by Asn221 resulting in the loss of a direct hydrogen bond with substrate D-fructose 1,6-bisphosphate. Binding structure analysis of substrate and product, overview
-
-
?
additional information
?
-
-
no substrate: D-glucose 1-phosphate, D-glucose 6-phosphate, sorbitol 6-phosphate, phosphoenolpyruvate, D-fructose 6-phosphate, 3-glycerate phosphate, dihydroxyacetone
-
-
?
additional information
?
-
substrate binding analysis of wild-type and mutant enzymes by surface plasmon resonance method, substrate affinities, overview
-
-
?
additional information
?
-
substrate binding analysis of wild-type and mutant enzymes by surface plasmon resonance method, substrate affinities, overview
-
-
?
additional information
?
-
substrate binding analysis of wild-type and mutant enzymes by surface plasmon resonance method, substrate affinities, overview
-
-
?
additional information
?
-
purified recombinant Pcal_0111 catalyzes both phosphatase and aldolase reactions with specific activity values of 4 U and 1.3 U, respectively. Although the enzyme can utilize several substrates for dephosphorylation, no phosphatase activity is detected with AMP, UTP, NADP, glucose 6-phosphate, ribose 5-phosphate, riboflavin 5-monophosphate, and pyridoxal 5-phosphate. Varying amounts of phosphatase activity are found when ATP, GTP, ADP, CTP, glyceraldehyde 3-phosphate, fructose 6-phosphate, fructose 1,6-bisphosphate, and phosphoribosyl diphosphate are used as substrates. The highest phosphatase activity is found with fructose 1,6-bisphosphate followed by phosphoribosyl diphosphate. Spectrophotometric coupled enzyme assay as discontinuous assay method, or product phosphate detection by malachite green assay method. Substrate binding residues include Tyr229, Lys232, and Tyr358
-
-
?
additional information
?
-
no phosphatase activity could be detected with AMP, UTP, NADP, glucose 6-phosphate, ribose 5-phosphate, riboflavin 5-monophosphate, and pyridoxal 5-phosphate
-
-
-
additional information
?
-
-
enzyme together with phosphofructokinase plays a crucial role in metabolism of pancreatic islet cells
-
-
?
additional information
?
-
-
enzyme influences the connection between DNA damage, aging and oxidative stress
-
-
?
additional information
?
-
purified YK23 exhibits high phosphatase activity against fructose 1,6-bisphosphate, significant hydrolytic activity toward fructose 1-phosphate, and detectable activity with glyceraldehyde 3-phosphate, erythrose 4-phosphate, and ribulose 1,5-diphosphate
-
-
?
additional information
?
-
-
purified YK23 exhibits high phosphatase activity against fructose 1,6-bisphosphate, significant hydrolytic activity toward fructose 1-phosphate, and detectable activity with glyceraldehyde 3-phosphate, erythrose 4-phosphate, and ribulose 1,5-diphosphate
-
-
?
additional information
?
-
-
binding of the first substrate molecule, in one dimer of the enzyme, produces a conformational change at the other dimer, reducing the substrate affinity and catalytic activity of its subunits
-
-
?
additional information
?
-
not: D-fructose 1-phosphate, D-fructose 6-phosphate, D-fructose 2,6-bisphosphate, glycerol 3-phosphate, glycerol 1-phosphate
-
?
additional information
?
-
-
not: D-fructose 1-phosphate, D-fructose 6-phosphate, D-fructose 2,6-bisphosphate, glycerol 3-phosphate, glycerol 1-phosphate
-
?
additional information
?
-
-
the enzyme TNA1-Fbp has broad substrate specificities for D-fructose-1,6-bisphosphate and its analogues including D-fructose 1-bisphosphate, D-fructose 6-phosphate, D-glucose 1-phosphate, D-glucose 6-phosphate, glycerol 2-phosphate, and phosphoenolpyruvate, as well as AMP, ADP ATP, substrate specificity, overview
-
-
?
additional information
?
-
Thermosynechococcus vestitus
a dual-function fructose-1,6/sedoheptulose-1,7-bisphosphatase (FBP/SBPase) exhibiting activity of EC 3.1.3.37, sedoheptulose 1,7-diphosphatase, and 3.1.3.11, fructose 1,6-bisphosphatase
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
D-fructose 1,6-diphosphate + H2O
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
additional information
?
-
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
E2RAN6
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Fbp plays a key role in gluconeogenesis that supplies cellular building blocks such as hexose and intermediates of the pentose phosphate pathway for cell growth. Fructose-1,6-bisphosphatase increases its abundance by 2.0-2.7fold on various aromatic compounds. Fbp plays a key role in aromatic assimilation by Coryneacterium glutamicum. The Fbp gene is disrupted and the mutant WTDfbp loses the ability to grow on aromatic compounds. Genetic complementation by the Fbp gene restores this ability
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
enzyme functions with FBPase I in the centarle pathways of carbohydrate metabolism
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
enzyme is a part of Calvin cycle
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
gluconeogenic enzyme
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
the the chloroplastic isozyme plays a key role in the Calvin cycle and the cytoplasmic isozyme plays a key role in the sucrose synthesis in cytoplasm
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
key enzyme of the gluconeogenic pathway
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
the bifunctional, thermostable enzyme (EC 4.1.2.13/EC 3.1.3.11) catalyses two subsequent steps in gluconeogenesis in most archaea and in deeply branching bacterial lineages
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
the bifunctional, thermostable enzyme (EC 4.1.2.13/EC 3.1.3.11) catalyses two subsequent steps in gluconeogenesis in most archaea and in deeply branching bacterial lineages
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
regulatory enzyme of glyconeogenesis. FBPase participates in some nuclear processes during development and regeneration of skeletal muscle
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
the coregulation of phosphofructo 1-kinase I and fructose 1,6-bisphosphatase are required for the ability of these cells to respond to glucose and induce metabolic and Ca2+ signals that can be important for sperm development and function
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
best substrate
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
one of the key enzymes in gluconeogenesis
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
r
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
FBPase contributes to the partitioning of the fixed carbon for ribulose-1,5-bisphosphate regeneration or starch synthesis
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Thermosynechococcus vestitus
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
the enzyme plays a key role in the Calvin cycle
-
?
D-fructose 1,6-diphosphate + H2O
?
-
key regulatory enzyme in the control of the Emden-Meyerhof pathway
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
key regulatory enzyme in the control of the Emden-Meyerhof pathway
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
constitutive enzyme
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
the enzyme is involved in the futile cycling of fructose 6-phosphate and fructose 1,6-diphosphate in flight muscle, the net result of which is the hydrolysis of ATP
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
enzyme in gluconeogenic pathway
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
enzyme plays a key regulatory role in the futile cycle of fructose 1,6-diphosphate synthesis and degradation
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
the alkaline isoenzyme may have an important role in vivo in the regulation and control of glycolysis and glyconeogenesis
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
gluconeogenic enzyme
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
regulatory enzyme in gluconeogenesis
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
enzyme is involved in photosynthetic process
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
isoenzyme A is present when the organism is grown under autotrophic conditions but is not synthesized during heterotrophic growth. Isoenzyme B is detected in both autothrophically and heterotrophically grown organisms
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
the enzyme may be involved in the regulation of the Calvin-Bassham carbon reduction cycle
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
key regulatory enzyme in carbohydrate synthesis in both gluconeogenesis and photosynthesis
-
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
enzyme is a part of Calvin cycle
-
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
-
?
additional information
?
-
-
role as a key enzyme in CO2 assimilation and also in coordinating carbon and nitrogen metabolism
-
-
?
additional information
?
-
-
bifunctional fructose 1,6-bisphosphate, FBP, aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity
-
-
?
additional information
?
-
-
bifunctional fructose 1,6-bisphosphate, FBP, aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity
-
-
?
additional information
?
-
-
enzyme together with phosphofructokinase plays a crucial role in metabolism of pancreatic islet cells
-
-
?
additional information
?
-
-
bifunctional fructose 1,6-bisphosphate, FBP, aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity
-
-
?
additional information
?
-
-
enzyme together with phosphofructokinase plays a crucial role in metabolism of pancreatic islet cells
-
-
?
additional information
?
-
-
enzyme influences the connection between DNA damage, aging and oxidative stress
-
-
?
additional information
?
-
Thermosynechococcus vestitus
a dual-function fructose-1,6/sedoheptulose-1,7-bisphosphatase (FBP/SBPase) exhibiting activity of EC 3.1.3.37, sedoheptulose 1,7-diphosphatase, and 3.1.3.11, fructose 1,6-bisphosphatase
-
-
?
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(1H-indol-1-yl)(4-(trifluoromethyl)phenyl)methanone
-
-
(2,3-diethoxy-7,8,9,10-tetrahydro-6H-cyclohepta[b]quinolin-11-yl)[3-(2-methylthiazol-4-yl)phenyl]amine
-
-
(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-7-yl)methyl dihydrogen phosphate
-
(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-7-yl)phosphonic acid
-
(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl)methyl dihydrogen phosphate
-
(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl)phosphonic acid
-
(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-9-yl)methyl dihydrogen phosphate
-
(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-9-yl)phosphonic acid
-
(2-amino-5,6-dihydro-4H-benzo[6,7]cyclohepta[1,2-d][1,3]thiazol-9-yl)methyl dihydrogen phosphate
-
(2-amino-5,6-dihydro-4H-benzo[6,7]cyclohepta[1,2-d][1,3]thiazol-9-yl)phosphonic acid
-
(2-amino-8H-indeno[1,2-d][1,3]thiazol-4-yl)methyl dihydrogen phosphate
-
(2-amino-8H-indeno[1,2-d][1,3]thiazol-4-yl)phosphonic acid
-
(2-amino-8H-indeno[1,2-d][1,3]thiazol-5-yl)methyl dihydrogen phosphate
-
(2-amino-8H-indeno[1,2-d][1,3]thiazol-5-yl)phosphonic acid
-
(2-amino-8H-indeno[1,2-d][1,3]thiazol-6-yl)methyl dihydrogen phosphate
-
(2-amino-8H-indeno[1,2-d][1,3]thiazol-6-yl)phosphonic acid
-
(2-aminomethyl-6,7-diethoxy-2,3-dihydro-1H-cyclopenta[b]quinolin-9-yl)[3-(2-methylthiazol-4-yl)phenyl]-amine
-
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-[(3-methylbut-2-en-1-yl)oxy]phenyl]prop-2-en-1-one
(3-Bromo-phenyl)-(6,7-diethoxy-quinazolin-4-yl)-amine
-
IC50: 0.0017 mM
(3-Bromo-phenyl)-(6,7-dimethoxy-2-methyl-quinazolin-4-yl)-amine
-
IC50: 0.0045 mM
(3-Bromo-phenyl)-(6,7-dimethoxy-quinazolin-4-yl)-amine
-
IC50: 0.001 mM
(3-Bromo-phenyl)-(7-ethoxy-6-nitro-quinazolin-4-yl)-amine
-
IC50: 0.0039 mM
(3-Bromo-phenyl)-[6-(2-methoxy-ethoxy)-quinazolin-4-yl]-amine
-
IC50: 0.0029 mM
(3-Bromo-phenyl)-[7-methoxy-6-(2-methoxy-ethoxy)-quinazolin-4-yl]-amine
-
IC50: 0.0055 mM
(3-Chloro-4-fluoro-phenyl)-(6,7-diethoxy-quinazolin-4-yl)-amine
-
IC50: 0.00053 mM
(3-Chloro-phenyl)-(6,7-diethoxy-quinazolin-4-yl)-amine
-
IC50: 0.0016 mM
(3-Chloro-phenyl)-(6,7-dimethoxy-quinazolin-4-yl)-amine
-
IC50: 0.0013 mM
(4-[3-(6,7-diethoxy-quinazolin-4-ylamino)-phenyl]-thiazol-2-yl)-methanol
(5-[2-amino-5-[(propylsulfanyl)carbonyl]-1,3-thiazol-4-yl]furan-2-yl)phosphonic acid
-
-
(5-[4-amino-7-[3-(dimethylamino)propyl]-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl)phosphonic acid
(6,7-diethoxy-1,2,3,4-tetrahydroacridin-9-yl)[3-(2-methylthiazol-4-yl)phenyl]amine
-
-
(6,7-diethoxy-2,3-dihydro-1H-cyclopenta[b]quinolin-9-yl)[3-(2-methylthiazol-4-yl)phenyl]amine
-
-
(6,7-Diethoxy-quinazolin-4-yl)-(3-ethynyl-phenyl)-amine
-
IC50: 0.0024 mM
(6,7-Diethoxy-quinazolin-4-yl)-(3-fluoro-phenyl)-amine
-
IC50: 0.0092 mM
(6,7-Diethoxy-quinazolin-4-yl)-(3-iodo-phenyl)-amine
-
IC50: 0.0021 mM
(6,7-Dimethoxy-quinazolin-4-yl)-(3-ethynyl-phenyl)-amine
-
IC50: 0.0009 mM
1-(cyclopropyl)methyl-3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
-
1-benzyl-3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
-
1-Fluoro-2,4-dinitrobenzene
-
up to 90% inhibition at pH 6.5-7.0, slight increase at pH 9.0 when Mg2+ is the metal cofactor. 3fold increase of activity at alkaline pH, less activation at neutral pH when Mn2+ is the metal cofactor
2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate
2,5-anhydromannitol 1,6-diphosphate
-
-
2,5-dichloro-N-(4-methyl-1,3-benzoxazol-2-yl)benzenesulfonamide
-
-
2,5-dichloro-N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
2,5-dichloro-N-(5-methyl-1,3-benzoxazol-2-yl)benzenesulfonamide
-
-
2,5-dichloro-N-(6-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
-
-
2,5-dichloro-N-(6-methoxy-1,3-benzoxazol-2-yl)benzenesulfonamide
-
-
2,5-dichloro-N-(6-methyl-1,3-benzoxazol-2-yl)benzenesulfonamide
-
-
2,5-dichloro-N-[5-(3-furyl)-1,3-benzoxazol-2-yl]benzenesulfonamide
-
-
2,5-dichloro-N-[5-methoxy-7-(4-methoxypyridin-3-yl)-1,3-benzoxazol-2-yl]benzenesulfonamide
-
-
2,5-dichloro-N-[7-(3-hydroxyphenyl)-5-methoxy-1,3-benzoxazol-2-yl]benzenesulfonamide
-
-
2,5-dichloro-N-[7-(4-hydroxyphenyl)-5-methoxy-1,3-benzoxazol-2-yl]benzenesulfonamide
-
-
2-(2-(phenylamino)thiazol-4-yl)phenol
-
2-(2-aminoethyl)-6,7-diethoxy-N-[3-(2-methyl-1,3-thiazol-4-yl)phenyl]quinazolin-4-amine
-
uncompetitive
2-(2-thienyl)-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-(3-pyridyl)-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-(4-(4-hydroxyphenyl)thiazol-2-ylamino)phenol
-
2-(4-phenylthiazol-2-ylamino)phenol
-
2-acetamido-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-7-yl dihydrogen phosphate
-
2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl dihydrogen phosphate
-
2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-9-yl dihydrogen phosphate
-
2-amino-4-[1-(3-phosphono)phenyl]thiazole
-
-
2-amino-4-[2-(5-(1-(3-bromophenyl)-1,3-propyl)phosphono)-furanyl]-5-isobutyl-thiazole
-
-
2-amino-4-[2-(5-(O-phenyl)-(N-((S)-1-ethoxycarbonyl)ethyl)-phosphonamido)-furanyl]-5-isobutylthiazole
-
-
2-amino-4-[2-(5-bis(p-acetoxybenzyl)phosphono)furanyl]-5-isobutylthiazole
-
-
2-amino-4-[2-(5-diphenylphosphono)furanyl]-5-isobutylthiazole
-
-
2-amino-4-[2-(5-monophenyl-monoamino-phosphono)furanyl]-5-isobutylthiazole
-
-
2-amino-4-[2-(5-monophenylphosphono)furanyl]-5-isobutylthiazole
-
-
2-amino-4-[2-(5-N,N'-bis((S)-1-(1-ethoxycarbonyl)ethyl)phosphonoamido)furanyl]-5-isobutylthiazole
-
optimization of the diamide prodrugs of phosphonic acid leads to the identification of a new diamide, the first reported orally efficacious FBPase inhibitor
2-amino-4-[2-(5-phosphono)furanyl]-5-ethoxycarbonylthiazole
2-amino-4-[2-(5-phosphono)furanyl]-5-isobutylthiazole
2-amino-4-[2-(5-phosphono)furanyl]-5-phenylthiazole
2-amino-4-[2-(5-phosphono)furanyl]-5-propylsulfanylthiazole
2-amino-4-[2-(6-phosphono)pyridyl]thiazole
-
-
2-amino-4-[2-[5-(1-(4-pyridyl)-1,3-propyl)phosphono]furanyl]-5-isobutylthiazole
-
-
2-amino-4-[2-[5-bis(1-(1-ethoxycarbonyloxy)ethyl)phosphono]-furanyl]-5-isobutyl-thiazole
-
-
2-amino-4-[2-[5-bis(ethoxycarbonyloxymethyl)phosphono]-furanyl]-5-isobutyl-thiazole
-
-
2-amino-4-[2-[5-bis(phenoxycarbonyloxymethyl)phosphono]-furanyl]-5-isobutyl-thiazole
-
-
2-amino-5,6-dihydro-4H-benzo[6,7]cyclohepta[1,2-d][1,3]thiazol-9-yl dihydrogen phosphate
-
2-amino-5-(2,2,2-trifluoroethyl)-4-[2-(5-phosphono)furanyl]-thiazole
-
-
2-amino-5-(2-furanyl)-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-(2-methoxyphenyl)-4-[2-(5-phosphono)furanyl]-thiazole
-
-
2-amino-5-(2-naphthyl)-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-(2-thienyl)-4-[(N-phosphonomethyl)carbamoyl]-thiazole
-
-
2-amino-5-(2-thienyl)-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-(3-methoxyphenyl)-4-[2-(5-phosphono)furanyl]-thiazole
-
-
2-amino-5-(4-acetylphenyl)-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-(4-chlorophenyl)-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-(4-fluorophenyl)-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-(4-methanesulfonyl)-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-(4-methoxycarbonylphenyl)-4-[2-(5-phosphono)-furanyl]thiazole
-
-
2-amino-5-(4-methoxyphenyl)-4-[2-(5-phosphono)furanyl]-thiazole
-
-
2-amino-5-(4-methylthiophenyl)-4-[2-(5-phosphono)furanyl]-thiazole
-
-
2-amino-5-(4-phenylphenyl)-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-(4-tert-butylphenyl)-4-[2-(5-phosphono)furanyl]-thiazole
-
-
2-amino-5-(N-morpholinyl)-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-benzyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-benzyloxycarbonyl-4-[2-(5-phosphono)furanyl]-thiazole
-
-
2-amino-5-bromo-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-chloro-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-cyclobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-cyclohexyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-cyclohexylmethyl-4-[2-(5-phosphono)furanyl]-thiazole
-
-
2-amino-5-cyclopentyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-cyclopentylmethyl-4-[2-(5-phosphono)furanyl]-thiazole
-
-
2-amino-5-cyclopropylmethyl-4-[2-(5-phosphono)furanyl]-thiazole
-
-
2-amino-5-ethylthio-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-hydroxymethyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-iodo-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
2-amino-5-isopropyl- 4-[1-(4-methoxy-3-phosphono)phenyl]-thiazole
-
-
2-amino-5-isopropyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-isopropylthio-4-[2-(5-phosphono)furanyl]thiazole hydrobromide
-
-
2-amino-5-methyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-methylsulfanyl-4-[2-(5-diethylphosphono)furanyl]thiazole
2-amino-5-neopentyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-phenyl- 4-[1-(4-fluoro-3-phosphono)phenyl]thiazole
-
-
2-amino-5-phenyl-4-[2-(5-methyl-4-phosphono)oxazolyl]-thiazole
-
-
2-amino-5-phenyl-4-[3-(1-phosphono)pyrrolyl]thiazole
-
-
2-amino-5-phenylthio-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-propyl- 4-[1-(4-methyl-3-phosphono)phenyl]thiazole
-
-
2-amino-5-propyl-4-phosphonomethoxycarbonylthiazole
-
-
2-amino-5-propyl-4-[1-(3-phosphono)phenyl]thiazole
-
-
2-amino-5-propyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-tert-butylthio-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-[(4-morpholinyl)methyl]-4-[2-(5-phosphono)furanyl]-thiazole dihydrobromide
-
-
2-amino-5-[(N,N-dimethyl)carbamoyl]-4-[2-(5-phosphono)-furanyl]thiazole
-
-
2-amino-8H-indeno[1,2-d][1,3]thiazol-4-yl dihydrogen phosphate
-
2-amino-8H-indeno[1,2-d][1,3]thiazol-5-yl dihydrogen phosphate
-
2-amino-8H-indeno[1,2-d][1,3]thiazol-6-yl dihydrogen phosphate
-
2-bromo-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-bromo-N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
-
-
2-carbamoyl-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-chloro-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-cyano-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-deoxyribose-5-phosphate
-
-
2-ethyl-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-hydroxymethyl-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-methyl-5-isobutyl-4-[2-(5-phosphono)furanyl]-thiazole
-
-
2-methylamino-5-isobutyl-4-[2-(5-hosphono)furanyl]thiazole
-
-
2-methylthio-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-phenyl-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-thiocarbamoyl-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-vinyl-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-[(3S,11aS)-3-(4-hydroxybenzyl)-1,4-dioxo-1,3,4,6,11,11a-hexahydro-2H-pyrazino[1,2-b]isoquinolin-2-yl]-N-[2-(4-hydroxyphenyl)ethyl]pentanamide
-
uncompetitive
2-[3-methyl-5-([[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]sulfamoyl)thiophen-2-yl]ethyl acetate
2-[5-([[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]sulfamoyl)-3-methylthiophen-2-yl]ethyl acetate
3,4-dihydroxy-N'-[(E)-[4-oxo-6-(propan-2-yl)-4H-chromen-3-yl]methylidene]benzohydrazide
compound potently inhibits both fructose-1,6-bisphoshate aldolase and fructose-1,6-bisphosphatase with IC50 values below 30 microM
3,5-diphenyl-1-(3-(trifluoromethyl) phenyl)-1H-pyrazole
-
-
3-(2-(ethoxycarbonyl)-7-nitro-1H-indol-3-yl)propanoic acid
-
3-(2-carboxyethyl)-4,6-dichloro-1H-indole-2-carboxylic acid
3-(2-carboxyethyl)-4-(2-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-4-(2-methylpropyl)-7-nitro-1H-indole-2-carboxylic acid
-
-
3-(2-carboxyethyl)-4-(3-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-4-(3-methoxyanilino)-7-nitro-1H-indole-2-carboxylic acid
-
-
3-(2-carboxyethyl)-4-(3-methoxyphenyl)-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-4-(4-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-4-(4-methoxyanilino)-7-nitro-1H-indole-2-carboxylic acid
-
-
3-(2-carboxyethyl)-4-(4-methoxyphenyl)-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-4-chloro-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-4-ethyl-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-4-isobutyl-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-5-(2-methylpropyl)-7-nitro-1H-indole-2-carboxylic acid
-
-
3-(2-carboxyethyl)-5-bromo-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-5-chloro-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-5-ethyl-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-5-ethyl-7-nitro-1H-indole-2-carboxylicacid
-
3-(2-carboxyethyl)-5-isobutyl-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-5-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-5-phenylamino-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-7-nitro-4-(3-methoxyphenylamino)-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-7-nitro-4-(3-nitrophenyl)-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-7-nitro-4-(4-methoxyphenylamino)-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-7-nitro-4-(4-nitrophenyl)-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-7-nitro-4-phenyl-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-7-nitro-4-phenylamino-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-7-nitro-5-phenyl-1H-indole-2-carboxylic acid
-
3-(4-(4-hydroxyphenyl)thiazol-2-ylamino)benzenesulfonamide
-
3-(4-(4-hydroxyphenyl)thiazol-2-ylamino)phenol
-
3-(4-phenylthiazol-2-ylamino)benzenesulfonamide
-
3-(4-phenylthiazol-2-ylamino)phenol
-
3-chloro-N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
-
-
3-chloro-N-[(3,5-dichlorophenyl)carbamoyl]benzenesulfonamide
3-ethyl-5-isobutyl-7-nitro-1H-indole-2-carboxylic acid
-
molecular modeling of binding mode. The key hydrogen bonding interactions are observed between the carboxylate and residues Thr 27, Lys 112 and Arg 140, which are also recognized by the phosphate group in AMP. This hydrogen bonding network may make crucial contributions to the binding affinity. The indole ring is situated in a hydrophobic pocket involved in residues Leu30 and Leu34. The 7-nitro group interacted with the hydroxyl group of Thr31 via a hydrogen bond
4-(2-(2-hydroxyphenylamino)thiazol-4-yl)benzene-1,3-diol
-
4-(2-(3-hydroxyphenylamino)thiazol-4-yl)benzene-1,3-diol
-
4-(2-(3-nitrophenylamino)thiazol-4-yl)phenol
-
4-(2-(4-hydroxyphenylamino)thiazol-4-yl)benzene-1,3-diol
-
4-(2-(4-nitrophenylamino)thiazol-4-yl)phenol
-
4-(2-(phenylamino)thiazol-4-yl)benzene-1,3-diol
-
4-(4-(2,4-dihydroxyphenyl)thiazol-2-ylamino)benzenesulfonamide
-
4-(4-(4-hydroxyphenyl)thiazol-2-ylamino)benzenesulfonamide
-
4-(4-(4-hydroxyphenyl)thiazol-2-ylamino)phenol
-
4-(4-phenylthiazol-2-ylamino)benzenesulfonamide
-
4-(4-phenylthiazol-2-ylamino)phenol
-
4-anilino-3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
-
-
4-anilinoquinazoline
-
low molecular weight inhibitors of enzyme that are not substrate mimics or AMP analogues
4-chloromercuribenzoate
-
-
4-tert-butyl-N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
-
-
4-[[(2R,4S)-4-(3-chlorophenyl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazole
-
-
4-[[(2R,4S)-4-(3-methoxyphenyl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazole
-
-
4-[[(2R,4S)-4-(4-chlorophenyl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazole
-
-
4-[[(2S,4S)-4-(3-chlorophenyl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazole
-
-
4-[[(2S,4S)-4-(3-methoxyphenyl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazole
-
-
4-[[(2S,4S)-4-(4-chlorophenyl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazole
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
up to 90% inhibition at pH 6.5-7.0, slight increase at pH 9.0 when Mg2+ is the metal cofactor. 3fold increase of activity at alkaline pH, less activation at neutral pH when Mn2+ is the metal cofactor
5-(1H-tetrazol-5-yl)-N-(3-(5-p-tolyl-1,3,4-oxadiazol-2-yl)phenyl)pentanamide
-
-
5-(2-hydroxyethyl)-4-methyl-N-[[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
5-(2-methoxyethyl)-4-methyl-N-([6-[(methylcarbamoyl)amino]-4-(methylsulfanyl)pyridin-2-yl]carbamoyl)thiophene-2-sulfonamide
5-(2-methoxyethyl)-4-methyl-N-[[4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
5-(2-methoxyethyl)-4-methyl-N-[[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
5-(2-methoxyethyl)-N-([4-methoxy-6-[(methylcarbamoyl)amino]pyridin-2-yl]carbamoyl)-4-methylthiophene-2-sulfonamide
5-anilino-3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
-
-
5-bromo-3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
-
-
5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
6,7-diethoxy-N-[3-(2-methyl-1,3-thiazol-4-yl)phenyl]quinazolin-4-amine
-
-
6,7-dimethyl-4-[[(2R,4S)-2-oxido-4-(pyridin-2-yl)-1,3,2-dioxaphosphinan-2-yl]methoxy]-8H-indeno[1,2-d][1,3]thiazole
-
-
6,7-dimethyl-4-[[(2R,4S)-2-oxido-4-(pyridin-3-yl)-1,3,2-dioxaphosphinan-2-yl]methoxy]-8H-indeno[1,2-d][1,3]thiazole
-
-
6,7-dimethyl-4-[[(2R,4S)-2-oxido-4-(pyridin-4-yl)-1,3,2-dioxaphosphinan-2-yl]methoxy]-8H-indeno[1,2-d][1,3]thiazole
-
-
6,7-dimethyl-4-[[(2R,4S)-4-(2-methylpyridin-3-yl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-8H-indeno[1,2-d][1,3]thiazole
-
-
6,7-dimethyl-4-[[(2R,4S)-4-(6-methylpyridin-3-yl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-8H-indeno[1,2-d][1,3]thiazole
-
-
6-hydroxy-N-(3-(5-p-tolyl-1,3,4-oxadiazol-2-yl)phenyl)hexanamide
-
-
6-oxo-6-(3-(5-p-tolyl-1,3,4-oxadiazol-2-yl)phenylamino)hexanoic acid
-
-
7-amino-3-(2-carboxyethyl)-1H-indole-2-carboxylic acid
-
aminoimidazole carboxamide ribotide
-
inhibition of fructose-1,6-bisphosphatase by aminoimidazole carboxamide ribotide prevents growth of Salmonella enterica purH mutants on glycerol
ammonium sulfate
-
10 mM, 127% of initial activity, 50 mM, no residual activity
D-fructose 1,6-bisphosphate
D-fructose 2,6-bisphosphate
D-fructose 6-phosphate
-
mixed-type. AMP, D-fructose 6-phosphate, D-fructose 1,6-bisphosphate interact in a synergistic way to inhibit the enzyme activity
D-fructose-1-phosphate
-
-
D-fructose-2,6-bisphosphate
dehydroascorbate
-
deactivates the enzyme activated by reduced thioredoxin f
diethyl (5-[4-amino-1-[(1R,2R)-bicyclo[2.2.1]hept-2-ylamino]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
diethyl (5-[4-amino-1-[3-(thiophen-3-ylmethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
diethyl (5-[4-amino-1-[4-(furan-3-ylmethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
diethyl (5-[4-amino-1-[4-(trifluoromethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
diethyl [5-(4-amino-1-benzyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
diethyl [5-(4-amino-1-ethyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
diethyl [5-(4-amino-1-methyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
diethyl [5-(4-amino-1-propyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
diethyl [5-[4-amino-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
diethyl [5-[4-amino-1-(3-hydroxybenzyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
diethyl [5-[4-amino-1-(4-tert-butylbenzyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
diethyl [5-[4-amino-1-(biphenyl-4-ylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
diethyl [5-[4-amino-1-(cyclobutylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
diethyl [5-[4-amino-1-(cycloheptylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
diethyl [5-[4-amino-1-(cyclohexylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
diethyl [5-[4-amino-1-(cyclopentylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
diethyl [5-[4-amino-1-(cyclopropylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
diphenyl [5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]phosphonate
-
non-competitive
ethyl (2S,6S)-4-[5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]-2,6-dimethyl-7-oxo-8-oxa-3,5-diaza-4-phosphadecan-1-oate 4-oxide
-
-
ethyl (2S,6S)-4-[[(6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazol-4-yl)oxy]methyl]-2,6-dimethyl-7-oxo-8-oxa-3,5-diaza-4-phosphadecan-1-oate 4-oxide
-
-
ethyl 2-[((5-[2-amino-5-(2,2-dimethylpropanoyl)-1,3-thiazol-4-yl]furan-2-yl)[(1-ethoxy-2-methyl-1-oxopropan-2-yl)amino]phosphoryl)amino]-2-methylpropanoate
MB07803
ethyl 3,3,3-trifluoro-2-hydroxy-2-(1-methyl-1H-indol-3-yl)propanoate
-
-
ethyl 3-(3,5-dimethyl-1H-pyrrol-2-yl)-4,4,4-trifluoro-3-hydroxybutanoate
-
-
ethyl 4-[5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]-2,2,6,6-tetramethyl-7-oxo-8-oxa-3,5-diaza-4-phosphadecan-1-oate 4-oxide (non-preferred name)
-
-
ethyl 4-[5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]-2,6-dimethyl-7-oxo-8-oxa-3,5-diaza-4-phosphadecan-1-oate 4-oxide (non-preferred name)
-
-
ethyl 4-[5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]-7-oxo-8-oxa-3,5-diaza-4-phosphadecan-1-oate 4-oxide (non-preferred name)
-
-
fructose 2,6-bisphosphate
fructose 6-phosphate
-
product inhibitor
fructose-1,6-bisphosphate
at higher concentrations
fructose-2,6-bisphosphate
Hg2+
-
0.1 mM, no residual activity
L-alanine, N,N'-[[5-[2-amino-5-(2-methylpropyl)-4-thiazolyl]-2-furanyl] phosphinylidene]bis-, diethyl ester
-
effect of gluconeogenesis inhibition on postprandial hyperglycemia is investigated using the inhibitor CS-917 in meal-loaded diabetic Goto-Kakizaki rats. CS-917 suppresses plasma glucose elevation after meal loading in a dose-dependent manner at doses ranging from 10 to 40 mg/kg. In an overnight-fasted state, CS-917 decreases the plasma glucose levels dose-dependently at doses ranging from 2.5 to 40 mg/kg. Glucose-lowering is associated with an accumulation of hepatic D-fructose 1,6-bisphosphate and a reduction in hepatic D-fructose 6-phosphate. Chronic treatment of CS-917 decreases plasma glucose significantly, and no significant increase in plasma lactate and no profound elevation in plasma triglycerides are observed by both acute and chronic treatment of CS-917 in Goto-Kakizaki rats
N'-[(E)-(6-ethyl-4-oxo-4H-chromen-3-yl)methylidene]-3,4-dihydroxybenzohydrazide
compound potently inhibits both fructose-1,6-bisphoshate aldolase and fructose-1,6-bisphosphatase with IC50 values below 30 microM
N'-[(E)-(6-tert-butyl-4-oxo-4H-chromen-3-yl)methylidene]-3,4-dihydroxybenzohydrazide
compound potently inhibits both fructose-1,6-bisphoshate aldolase and fructose-1,6-bisphosphatase with IC50 values below 30 microM
N,4-diphenylthiazol-2-amine
-
N,N'-bis(6,7-diethoxy-2,3-dihydro-1H-cyclopenta[b]quinolin-9-yl)pentane-1,5-diamine
-
uncompetitive
N,N'-bis-(6,7-diethoxy-2,3-dihydro-1H-cyclopenta[b]quinolin-9-yl)butan-1,4-diamine
-
0.03 mM, 20% inhibition
N,N'-bis-(6,7-diethoxy-2,3-dihydro-1H-cyclopenta[b]quinolin-9-yl)hexan-1,6-diamine
-
-
N,N'-bis-(6,7-diethoxy-2,3-dihydro-1H-cyclopenta[b]quinolin-9-yl)pentan-1,5-diamine
-
-
N,N'-bis-(6,7-diethoxy-2,3-dihydro-1H-cyclopenta[b]quinolin-9-yl)propan-1,3-diamine
-
-
N-(5-bromo-1,3-benzoxazol-2-yl)-2,5-dichlorobenzenesulfonamide
-
-
N-(5-chloro-1,3-benzoxazol-2-yl)-1-methyl-1H-imidazole-4-sulfonamide
-
-
N-(5-chloro-1,3-benzoxazol-2-yl)-2-(1H-imidazol-1-yl)benzenesulfonamide
-
-
N-(5-chloro-1,3-benzoxazol-2-yl)-2-cyanobenzenesulfonamide
-
-
N-(5-chloro-1,3-benzoxazol-2-yl)-3-nitrobenzenesulfonamide
-
-
N-(5-chloro-1,3-benzoxazol-2-yl)-4-(3-furyl)benzenesulfonamide
-
-
N-(5-chloro-1,3-benzoxazol-2-yl)-4-(trifluoromethoxy)benzenesulfonamide
-
-
N-(5-chloro-1,3-benzoxazol-2-yl)-4-fluorobenzenesulfonamide
-
-
N-(5-chloro-1,3-benzoxazol-2-yl)-4-methylbenzenesulfonamide
-
-
N-(5-chloro-1,3-benzoxazol-2-yl)anthracene-2-sulfonamide
-
-
N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
-
-
N-(5-chloro-1,3-benzoxazol-2-yl)biphenyl-2-sulfonamide
-
-
N-(5-chloro-1,3-benzoxazol-2-yl)biphenyl-3-sulfonamide
-
-
N-(5-chloro-1,3-benzoxazol-2-yl)biphenyl-4-sulfonamide
-
-
N-(5-chloro-1,3-benzoxazol-2-yl)naphthalene-2-sulfamide
-
excellent bioavailability and a good pharmacokinetic profile in rats
N-(5-chloro-1,3-benzoxazol-2-yl)naphthalene-2-sulfonamide
N-(5-chloro-1,3-benzoxazol-2-yl)thiophene-2-sulfonamide
-
-
N-(5-tert-butyl-1,3-benzoxazol-2-yl)-2,5-dichlorobenzenesulfonamide
-
-
N-(6,7-diethoxy-9-[3-(2-methylthiazol-4-yl)phenylamino]-2,3-dihydro-1H-cyclopenta[b]quinolin-1-yl)-acetamide
-
-
N-(6,7-diethoxy-9-[3-(2-methylthiazol-4-yl)phenylamino]-2,3-dihydro-1H-cyclopenta[b]quinolin-2-yl)acetamide
-
-
N-([4-bromo-6-[(2,2,2-trifluoroethyl)amino]pyridin-2-yl]carbamoyl)-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
N-([4-bromo-6-[(methylcarbamoyl)amino]pyridin-2-yl]carbamoyl)-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
N-[(5-bromo-1,3-thiazol-2-yl)carbamoyl]-3-chlorobenzenesulfonamide
N-[(6-amino-4-bromopyridin-2-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
N-[(6-amino-4-methoxypyridin-2-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
N-[(6-bromo-1H-indazol-4-yl)carbamoyl]-3-chlorobenzenesulfonamide
N-[(6-bromo-1H-indazol-4-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
N-[(6-bromo-1H-indol-4-yl)carbamoyl]-3-chlorobenzenesulfonamide
N-[(7-bromoimidazo[1,2-a]pyridin-5-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
N-[4-[[(5-chloro-1,3-benzoxazol-2-yl)amino]sulfonyl]phenyl]butanamide
-
-
N-[6-(4-aminophenyl)-5-methoxy-1,3-benzoxazol-2-yl]-2,5-dichlorobenzenesulfonamide
-
non-competitive
N-[7-(3-aminophenyl)-5-methoxy-1,3-benzoxazol-2-yl]-2,5-dichlorobenzenesulfonamide
-
-
N-[7-(4-aminophenyl)-5-methoxy-1,3-benzoxazol-2-yl]-2,5-dichlorobenzenesulfonamide
-
-
N-[7-[3-(aminomethyl)phenyl]-5-methoxy-1,3-benzoxazol-2-yl]-2,5-dichlorobenzenesulfonamide
-
-
N-[[6-amino-4-(methylsulfanyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
N-[[6-amino-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
N-[[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-hydroxyethyl)-4-methylthiophene-2-sulfonamide
N-[[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
N4-(3-Bromo-phenyl)-7-chloro-quinazoline-4,6-diamine
-
IC50: 0.0119 mM
NaCl
-
in vivo: The presence of 100 mM NaCl in the growth medium only marginally alters the cytosolic and chloroplastic enzyme activities of salt-tolerant varieties whereas both the activities decline appreciably in salt-sensitive varieties tested. in vitro: comparison of inhibition of chloroplastic enzyme in a salt-sensitive and a salt-tolerant enzyme, protection against inhibition in salt-sensitve rice by mannitol, inositol, pinitol, sorbitol, trehalose, sucrose and proline
NADH
-
20% inhibition of isoenzyme A, 83% inhibition of isoenzyme B
nagarse
-
stimulates 2fold to 3fold at pH 9.0, loss of activity at pH 6.5
-
NEM
-
up to 90% inhibition at pH 6.5-7.0, slight increase at pH 9.0 when Mg2+ is the metal cofactor. 3fold increase of activity at alkaline pH, less activation at neutral pH when Mn2+ is the metal cofactor
oxidized glutathione
-
deactivates the enzyme activated by reduced thioredoxin f
p-mercuribenzoate
-
up to 90% inhibition at pH 6.5-7.0, slight increase at pH 9.0 when Mg2+ is the metal cofactor. 3fold increase of activity at alkaline pH, less activation at neutral pH when Mn2+ is the metal cofactor
papain
-
stimulates 2fold to 3fold at pH 9.0, loss of activity at pH 6.5
-
Pronase
-
stimulates 2fold to 3fold at pH 9.0, loss of activity at pH 6.5
-
propan-2-yl 4-[5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]-9-methyl-7-oxo-3,5,8-trioxa-4-phosphadecan-1-oate 4-oxide
-
-
pseudo-tetrapeptide OC252
-
the inhibition is synergistic with both AMP and fructose 2,6-bisphosphate, noncompetitive with respect to Mg2+ and, uncompetitive with respect to fructose 1,6-bisphosphate
Ribulose 1,5-diphosphate
-
1 mM, 48% inhibition of isoenzyme A, 3% inhibition of isoenzyme B
S-nitrosoglutathione
GSNO, the chloroplast FBPase isoform cFBP1 is efficiently S-nitrosylated in vitro. GSNO inhibits the FBPase activity in the mutant C173S/C178S but not in mutant C153S. 0.02 mM GSNO produces a 75% activity inhibition in the mutant C173S/C178S, compared with the nontreated protein, S-nitrosylation of FBPase mutants in the Cys of the redox regulatory domain
sedoheptulose 1,7-diphosphate
-
competitive inhibition of activity with fructose 1,6-diphosphate
tert-butyl 4-[5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]-9,9-dimethyl-7-oxo-3,5,8-trioxa-4-phosphadecan-1-oate 4-oxide
-
-
TNP-AMP
-
a fluorescent AMP analogue, 2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate (TNP-AMP), is used as a fluorescent probe as it is able to competitively inhibit AMP binding to the AMP allosteric site. AMP and fructose 1,6-bisphosphate both can reduce the fluorescence from the bound TNP-AMP through competition for FBPase, suggesting that TNP-AMP binds not only to the AMP allosteric site but also to the FBP active site. The residue K274 is very important for TNP-AMP to bind to the active site of FBPase. When the residue K274 is mutated to L274, TNP-AMP cannot bind to the active site, but can bind to the allosteric site
[(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl)(difluoro)methyl]phosphonic acid
-
[(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl)methyl]phosphonic acid
-
[(2R,3S,4R,5R)-5-[4-(aminocarbonyl)-1H-imidazol-1-yl]-3,4-dihydroxytetrahydrofuran-2-yl]methyl dihydrogen phosphate
-
-
[2-[(6-amino-8,9-dihydro-7H-purin-8-yl)amino]ethyl]phosphonate
-
[2-[[6-amino-9-(2-cyclohexylethyl)-8,9-dihydro-7H-purin-8-yl]amino]ethyl]phosphonate
-
[3-[6-amino-9-(2-cyclohexylethyl)-8,9-dihydro-7H-purin-8-yl]propyl]phosphonate
-
[5-(1,3-thiazol-4-yl)-2-furyl]phosphonic acid
-
-
[5-(2-amino-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
[5-(2-amino-5-isobutyl-1,3-oxazol-4-yl)-2-furyl]phosphonic acid
[5-(2-amino-5-isobutyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
-
non-competitive
[5-(2-amino-5-isobutyl-1H-imidazol-4-yl)-2-furyl]phosphonic acid
-
-
[5-(2-amino-5-phenyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
[5-(2-amino-5-phenyl-1,3-thiazol-4-yl)furan-2-yl]phosphonic acid
-
-
[5-(2-amino-5-propyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
-
-
[5-(2-amino-5-propyl-1,3-thiazol-4-yl)thiophen-2-yl]phosphonic acid
-
-
[5-(4-amino-1-tert-butyl-2,3-dihydro-1H-benzimidazol-2-yl)-2-furyl]phosphonate
-
[5-(4-amino-1-tert-butyl-7-ethyl-5-fluoro-2,3-dihydro-1H-benzimidazol-2-yl)-2-furyl]phosphonate
-
[5-(4-amino-5-bromo-1-cyclopropyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonic acid
[5-(5-isobutyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
[5-(6-amino-3-phenylpyridin-2-yl)-2-furyl]phosphonic acid
[5-(6-amino-9-tert-butyl-8,9-dihydro-7H-purin-8-yl)-2-furyl]phosphonate
-
[5-[2-amino-5-(2-methylpropyl)-1,3-selenazol-4-yl]furan-2-yl]phosphonic acid
[5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]phosphonic acid
[5-[2-amino-5-(ethoxycarbonyl)-1,3-thiazol-4-yl]furan-2-yl]phosphonic acid
-
-
[5-[2-amino-5-(propylsulfanyl)-1,3-thiazol-4-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-1-(2-ethylbutyl)-5-fluoro-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-5,7-dibromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-5,7-dichloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-5-bromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-5-bromo-6,7-dichloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-5-chloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-5-ethyl-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-7-phenyl-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-7-propyl-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-5-fluoro-1-(pentan-3-yl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-5-fluoro-7-(2-methoxyethyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-5-fluoro-7-(3-methylbutyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-5-fluoro-7-(4-fluorophenyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-5-hydroxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-5-methoxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-6-chloro-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-7-(3,3-dimethylbutyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-7-(4-chlorophenyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-7-(6-chlorohexyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-7-bromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-7-bromo-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-7-chloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-7-chloro-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-7-cyclopropyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-7-ethenyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-7-ethyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[5-(2-methylpropyl)-2-phenyl-1,3-thiazol-4-yl]furan-2-yl]phosphonic acid
-
-
[5-[6-amino-9-(2,2-dimethylpropyl)-8,9-dihydro-7H-purin-8-yl]-2-furyl]phosphonate
-
[5-[6-amino-9-(2-cyclohexylethyl)-8,9-dihydro-7H-purin-8-yl]-2-furyl]phosphonate
-
[5-[6-amino-9-(2-phenylethyl)-8,9-dihydro-7H-purin-8-yl]-2-furyl]phosphonate
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-[(3-methylbut-2-en-1-yl)oxy]phenyl]prop-2-en-1-one
-
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-[(3-methylbut-2-en-1-yl)oxy]phenyl]prop-2-en-1-one
-
-
(4-[3-(6,7-diethoxy-quinazolin-4-ylamino)-phenyl]-thiazol-2-yl)-methanol
i.e. PFE, allosteric inhibitor
(4-[3-(6,7-diethoxy-quinazolin-4-ylamino)-phenyl]-thiazol-2-yl)-methanol
i.e. PFE, allosteric inhibitor, residue L56 coordinates the (4-[3-(6,7-diethoxy-quinazolin-4-ylamino)-phenyl]-thiazol-2-yl)-methanol (PFE) inhibitor ligand, as does residue L73, both of which exhibit hydrophobic interactions with the ligand in the PFE-binding site. In addition, L73 and L56 are part of a network that leads from the allosteric binding site to the active site of the enzyme. This hydrophobic network, also involving residues V48 and L120 may stabilize previously described hydrogen bonding networks including residues R49, S169, and D127, shown in the network, leading to the active site where the metal binds D121, D118, and E280. The M177 and Y164 interfacial residues are positioned between the AMP-binding site and active sites
(5-[4-amino-7-[3-(dimethylamino)propyl]-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl)phosphonic acid
-
-
(5-[4-amino-7-[3-(dimethylamino)propyl]-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl)phosphonic acid
-
-
2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate
wild-type muscle enzyme, 50% inhibition at 0.00022 mM, wild-type liver enzyme, 50% inhibition at 0.0046 mM
2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate
-
able to bind not only to the AMP allosteric site but also to the fructose-1,6-bisphosphate active site
2,5-dichloro-N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
-
50% inhibition at 0.0034 mM
2,5-dichloro-N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
-
-
2,5-dichloro-N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
-
non-competitive
2-amino-4-[2-(5-phosphono)furanyl]-5-ethoxycarbonylthiazole
-
potent FBPase inhibitor
2-amino-4-[2-(5-phosphono)furanyl]-5-ethoxycarbonylthiazole
-
potent FBPase inhibitor: when administerd intravenously it lowers plasma glucose levels in 18 h fasted normal Sprague-Dawley rats above 50% at doses below 10 mg/kg
2-amino-4-[2-(5-phosphono)furanyl]-5-isobutylthiazole
-
potent FBPase inhibitor
2-amino-4-[2-(5-phosphono)furanyl]-5-isobutylthiazole
-
potent FBPase inhibitor: when administerd intravenously it lowers plasma glucose levels in 18 h fasted normal Sprague-Dawley rats above 50% at doses below 10 mg/kg
2-amino-4-[2-(5-phosphono)furanyl]-5-phenylthiazole
-
potent FBPase inhibitor
2-amino-4-[2-(5-phosphono)furanyl]-5-phenylthiazole
-
potent FBPase inhibitor: when administerd intravenously it lowers plasma glucose levels in 18 h fasted normal Sprague-Dawley rats above 50% at doses below 10 mg/kg
2-amino-4-[2-(5-phosphono)furanyl]-5-propylsulfanylthiazole
-
potent FBPase inhibitor
2-amino-4-[2-(5-phosphono)furanyl]-5-propylsulfanylthiazole
-
potent FBPase inhibitor: when administerd intravenously it lowers plasma glucose levels in 18 h fasted normal Sprague-Dawley rats above 50% at doses below 10 mg/kg
2-amino-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
poor oral bioavailability
2-amino-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
poor oral bioavailability
2-amino-5-methylsulfanyl-4-[2-(5-diethylphosphono)furanyl]thiazole
-
potent FBPase inhibitor
2-amino-5-methylsulfanyl-4-[2-(5-diethylphosphono)furanyl]thiazole
-
potent FBPase inhibitor: when administerd intravenously it lowers plasma glucose levels in 18 h fasted normal Sprague-Dawley rats above 50% at doses below 10 mg/kg
2-[3-methyl-5-([[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]sulfamoyl)thiophen-2-yl]ethyl acetate
-
-
2-[3-methyl-5-([[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]sulfamoyl)thiophen-2-yl]ethyl acetate
-
-
2-[5-([[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]sulfamoyl)-3-methylthiophen-2-yl]ethyl acetate
-
-
2-[5-([[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]sulfamoyl)-3-methylthiophen-2-yl]ethyl acetate
-
-
3-(2-carboxyethyl)-4,6-dichloro-1H-indole-2-carboxylic acid
-
non-competitive
3-(2-carboxyethyl)-4,6-dichloro-1H-indole-2-carboxylic acid
MDL-29951
3-chloro-N-[(3,5-dichlorophenyl)carbamoyl]benzenesulfonamide
-
-
3-chloro-N-[(3,5-dichlorophenyl)carbamoyl]benzenesulfonamide
-
-
5-(2-hydroxyethyl)-4-methyl-N-[[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
-
-
5-(2-hydroxyethyl)-4-methyl-N-[[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
-
-
5-(2-methoxyethyl)-4-methyl-N-([6-[(methylcarbamoyl)amino]-4-(methylsulfanyl)pyridin-2-yl]carbamoyl)thiophene-2-sulfonamide
-
-
5-(2-methoxyethyl)-4-methyl-N-([6-[(methylcarbamoyl)amino]-4-(methylsulfanyl)pyridin-2-yl]carbamoyl)thiophene-2-sulfonamide
-
-
5-(2-methoxyethyl)-4-methyl-N-[[4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
-
-
5-(2-methoxyethyl)-4-methyl-N-[[4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
-
-
5-(2-methoxyethyl)-4-methyl-N-[[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
-
-
5-(2-methoxyethyl)-4-methyl-N-[[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
-
-
5-(2-methoxyethyl)-N-([4-methoxy-6-[(methylcarbamoyl)amino]pyridin-2-yl]carbamoyl)-4-methylthiophene-2-sulfonamide
-
-
5-(2-methoxyethyl)-N-([4-methoxy-6-[(methylcarbamoyl)amino]pyridin-2-yl]carbamoyl)-4-methylthiophene-2-sulfonamide
-
-
ADP
33% inhibition; 38% inhibition
ADP
1.5 mM, 30% decrease in activity; 30% inhibition at 1.5 mM
AMP
-
-
AMP
inhibitory below 0.2 mM
AMP
-
50% inhibition at 0.015 mM
AMP
-
transformation of enzyme to inactive T-state, inhibition shows quarternary transition and cooperativity
AMP
FBPase undergoes a quaternary transition from the canonical R-state to a T-like state in response to AMP. Glc-6-P and AMP are synergistic inhibitors
AMP
AMP and D-fructose 2,6-bisphosphate are not synergistic inhibitors of the type I FBPase
AMP
-
at pH 7.4, 0.0004 mM, complete inhibition
AMP
-
susceptibility of enzyme decreases in complex with aldolase
AMP
50% inhibition at 0.00016 mM
AMP
-
no significant inhibition
AMP
lung enzyme is significantly less inhibited than the muscle enzyme
AMP
-
muscle enzyme is more strongly inhibited than the liver isoenzyme
AMP
wild-type muscle enzyme, 50% inhibition at 0.0001 mM, Hill coefficient 1.78, wild-type liver enzyme, 50% inhibition at 0.0044 mM, Hill coefficient 2.08
AMP
-
113Tyr and 31Thr play an mportant role, each via two hydrogen bonds affecting the binding affinity of inhibitor AMP to FBPase
AMP
inactive, AMP-associated T state of the enzyme, AMP binding results in improved thermal stability of muscle FBPase
AMP
-
allosteric inhibition. The fluorescent AMP analogue, 2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate (TNP-AMP), is used as a fluorescent probe as it is able to competitively inhibit AMP binding to the AMP allosteric site
AMP
allosteric inhibitor. AMP binding triggers a rearrangement of hydrogen bonds across the large and small interfaces. Retraction of the effector loop required for AMP binding releases the side chain of His23 from the dimer-dimer interface. This is coupled with a flip of the side chain of Arg48 which ties down the key catalytic dynamic loop in a disengaged conformation and also locks the tetramer in an inactive rotated T-state; AMP binds to an effector site about 30 A distant from the active site and acts as an allosteric inhibitor, the crystal structure of LmFBPase complexed with its allosteric inhibitor AMP shows an inactive form of the tetramer, in which the dimer pairs are rotated by 18° relative to each other, revealing an allosteric mechanism in which AMP binding triggers a rearrangement of hydrogen bonds across the large and small interfaces. Retraction of the effector loop required for AMP binding releases the side chain of His23 from the dimer-dimer interface. This is coupled with a flip of the side chain of Arg48 which ties down the key catalytic dynamic loop in a disengaged conformation and also locks the tetramer in an inactive rotated T-state. AMP inhibits the catalytic activity of LmFBPase without eliminating the substrate binding
AMP
-
non-competitive. AMP, D-fructose 6-phosphate, D-fructose 1,6-bisphosphate interact in a synergistic way to inhibit the enzyme activity
AMP
-
sensitivity decreases greatly with increasing pH or temperature. Inhibition of Zn2+ and AMP is synergistic
AMP
-
sensitivity to AMP is decreased with increase in pH, temperature and Mg2+ concentration
AMP
-
0.073 mM, 50% inhibition
AMP
-
non-competitive inhibition of cytosolic enzyme, the chloroplastic enzyme is AMP-insensitive
AMP
-
non-competitive inhibition of cytosolic enzyme, the chloroplatic enzyme is AMP-insensitive
AMP
-
acts synergistically with fructose-2,6-bisphosphate on the frog muscle FBPase
AMP
non-competitive inhibition
AMP
-
the AMP binding is mainly located in the N-terminal region
AMP
-
muscle enzyme: 50% inhibition at 0.00054 mM, liver enzyme: 50% inhibition at 0.085 mM
AMP
-
0.1 mM, 9% inhibition of isoenzyme A, complete inhibition of isoenzyme B
AMP
-
mixed linear inhibitor
AMP
-
the phosphoenzyme is about 3fold more sensitive than the dephosphoenzyme
AMP
-
inhibits cytoplasmic enzyme, no inhibition of chloroplastic enzyme
AMP
-
no inhibition of the enzyme from chloroplast
AMP
-
structural aspects of the allosteric inhibition
AMP
-
uptake of 1 M of NEM per mol of subunit is accompanied by a loss of sensitivity towards AMP. K+ induces a conformational change on the enzyme derivative which hinders AMP interaction with the protein
AMP
-
comparison of inhibition of homotetramer and hybrid tetramers
AMP
-
study of allosteric inhibition, two classes of binding sites with two distinct affinities for AMP are possible
AMP
wild-type, 50% inhibition at 0.0016 mM, mutant E97A, 50% inhibition at 0.0038 mM, mutant D118A, 50% inhibition at 0.0069 mM, mutant D121A, 50% inhibition at 0.0074 mM
AMP
-
isoenzyme F-I is inhibited, isoenzyme F-II is not inhibited
AMP
Thermosynechococcus vestitus
a regulatory inhibitor, AMP-binding loop structure analysis
ATP
50% inhibition; 56% inhibition
ATP
1 mM, reduces activity by 40%
ATP
-
activates the microsomal and mitochondrial enzyme, inhibits the cytosoli enzyme
ATP
1.5 mM, 90% decrease in activity; 90% inhibition at 1.5 mM
Ca2+
-
Ca2+
-
inhibition is potentiated by Li+
Ca2+
-
wild type and mutant enzyme
Ca2+
unique divalent metal ion inhibitor
Ca2+
-
Ca2+ affects conformation of the catalytic loop 52-72 of muscle FBPase and inhibits its activity by competing with activatory divalent cations, e.g. Mg2+ and Zn2+. Aldolase associates with FBPase in its active form, i.e. with loop 52-72 in the engaged conformation, while Ca2+ stabilizes the disengaged-like form of the loop
Ca2+
similar inhibition constant as Mn2+
Ca2+
-
0.05 mM, 41% residual activity
Ca2+
-
50% inhibition at 59 nM, muscle enzyme. At elevated Ca2+ concentration, enzyme dissociates from Z-line
Ca2+
-
Glu 69 is essential for the high sensitivity of muscle fructose-1,6-bisphosphatase inhibition by calcium ions
Ca2+
-
competitive with respect to Mg2+
Ca2+
-
chloroplastic enzyme
Ca2+
-
at high concentration depending on the concentration of Mg2+
citrate
-
-
citrate
-
mixed type of inhibition with a change from a hyperbolic velocity curve in absence of citrate to a sigmoidal one in its presence
Cu2+
-
-
Cu2+
-
1 mM, no residual activity
D-fructose 1,6-bisphosphate
-
D-fructose 1,6-bisphosphate
substrate inhibition at high concentrations
D-fructose 1,6-bisphosphate
-
D-fructose 1,6-bisphosphate
-
-
D-fructose 1,6-bisphosphate
-
competitive, changes substrate saturation curve from hyperbolic to sigmoidal. AMP, D-fructose 6-phosphate, D-fructose 1,6-bisphosphate interact in a synergistic way to inhibit the enzyme activity
D-fructose 1,6-bisphosphate
-
substrate inhibition at higher concentrations
D-fructose 1,6-bisphosphate
-
-
D-fructose 2,6-bisphosphate
-
-
D-fructose 2,6-bisphosphate
AMP and fructose 2,6-bisphosphate are not synergistic inhibitors of the type I FBPase
D-fructose 2,6-bisphosphate
the Lys residue, which is known to be essential for inhibiting Fru 2,6-P2 in gluconeogenic FBPases, is also conserved in EgFBPaseIII at Lys408
D-fructose 2,6-bisphosphate
-
D-fructose 2,6-bisphosphate
a natural heterotropic inhibitor
D-fructose 2,6-bisphosphate
-
-
D-fructose 2,6-bisphosphate
-
D-fructose 2,6-bisphosphate
-
-
D-fructose 2,6-bisphosphate
-
D-fructose 2,6-bisphosphate
-
the binding of fructose 1,6-bisphosphate induces the appearance of catalytic sites with lower affinity for substrate and lower catalytic activity. The inhibitor, fructose 1,6-bisphosphate, competes with the substrate for the high-affinity sites. Binding of substrate to the low-affinity sites acts as a stapler that prevents dissociation of the tetramer and hence exchange of subunits, and results in substrate inhibition
D-fructose 2,6-bisphosphate
a natural heterotropic inhibitor
D-fructose-2,6-bisphosphate
-
-
D-fructose-2,6-bisphosphate
-
-
D-fructose-2,6-bisphosphate
-
acts synergistically with AMP on the frog muscle FBPase
D-fructose-2,6-bisphosphate
competitive inhibition
D-fructose-2,6-bisphosphate
-
-
D-fructose-2,6-bisphosphate
competitive inhibition
D-fructose-2,6-bisphosphate
kinetic mechanism
D-fructose-2,6-bisphosphate
-
two pathways of allosteric inhibition are possible
D-fructose-2,6-bisphosphate
-
-
D-fructose-2,6-bisphosphate
-
D-glucose 6-phosphate
allosteric inhibition. FBPase undergoes a quaternary transition from the canonical R-state to a T-like state in response to glucose 6-phosphate. Glc-6-P and AMP are synergistic inhibitors
diethyl (5-[4-amino-1-[(1R,2R)-bicyclo[2.2.1]hept-2-ylamino]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
-
-
diethyl (5-[4-amino-1-[(1R,2R)-bicyclo[2.2.1]hept-2-ylamino]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
-
-
diethyl (5-[4-amino-1-[3-(thiophen-3-ylmethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
-
-
diethyl (5-[4-amino-1-[3-(thiophen-3-ylmethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
-
-
diethyl (5-[4-amino-1-[4-(furan-3-ylmethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
-
-
diethyl (5-[4-amino-1-[4-(furan-3-ylmethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
-
-
diethyl (5-[4-amino-1-[4-(trifluoromethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
-
-
diethyl (5-[4-amino-1-[4-(trifluoromethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
-
-
diethyl [5-(4-amino-1-benzyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
-
-
diethyl [5-(4-amino-1-benzyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
-
-
diethyl [5-(4-amino-1-ethyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
-
-
diethyl [5-(4-amino-1-ethyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
-
-
diethyl [5-(4-amino-1-methyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
-
-
diethyl [5-(4-amino-1-methyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
-
-
diethyl [5-(4-amino-1-propyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
-
-
diethyl [5-(4-amino-1-propyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(3-hydroxybenzyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(3-hydroxybenzyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(4-tert-butylbenzyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(4-tert-butylbenzyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(biphenyl-4-ylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(biphenyl-4-ylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(cyclobutylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(cyclobutylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(cycloheptylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(cycloheptylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(cyclohexylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(cyclohexylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(cyclopentylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(cyclopentylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(cyclopropylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(cyclopropylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
EDTA
at an equimolar concentration to the bivalent metal ions, almost complete loss of activity; at an equimolar concentration to the bivalent metal ions, almost complete loss of activity
EDTA
5 mM, complete inhibition of phosphatase activity; complete inhibition of phosphatase activity by 5 mM EDTA
EDTA
-
0.1 mM, complete inhibition
fructose 1,6-diphosphate
-
at high concentrations
fructose 1,6-diphosphate
-
above 0.1 mM
fructose 1,6-diphosphate
-
substrate inhibition above 0.05 M
fructose 1,6-diphosphate
-
-
fructose 1,6-diphosphate
-
above 0.015 mM
fructose 1,6-diphosphate
-
concentration required for 50% inhibition is 0.045 mM for the muscle enzyme, 0.060 mM for the intestinal enzyme and 0.065 mM for the liver enzyme
fructose 1,6-diphosphate
-
at high concentrations
fructose 1,6-diphosphate
-
the substrate is unable to bind to the free enzyme as an inhibitor
fructose 1,6-diphosphate
-
no inhibition up to 1 mM
fructose 1,6-diphosphate
-
above 4 mM
fructose 1,6-diphosphate
-
0.4 mM, 58% loss of maximal activity
fructose 1,6-diphosphate
-
at high concentrations
fructose 2,6-bisphosphate
global conformational change in porcine FBPase induced by fructose 2,6-bisphosphate in the absence of AMP
fructose 2,6-bisphosphate
-
fructose 2,6-diphosphate
-
competitive
fructose 2,6-diphosphate
-
-
fructose 2,6-diphosphate
lung enzyme is slightly more sensitive to inhibition than the liver enzyme. Synergistic effect of AMP and fructose 2,6-diphosphate on lung and liver enzyme
fructose 2,6-diphosphate
-
-
fructose 2,6-diphosphate
-
-
fructose 2,6-diphosphate
-
-
fructose 2,6-diphosphate
-
muscle enzyme: 50% inhibition at 0.0063 mM, liver enzyme: 50% inhibition at 0.0015 mM
fructose 2,6-diphosphate
-
-
fructose 2,6-diphosphate
-
-
fructose 2,6-diphosphate
-
the phosphoenzyme is about 3fold more sensitive than the dephosphoenzyme
fructose 2,6-diphosphate
-
-
fructose 2,6-diphosphate
-
-
fructose 2,6-diphosphate
-
-
fructose-2,6-bisphosphate
-
-
fructose-2,6-bisphosphate
fructose 2,6-bisphosphate binds at the active site, and shows a synergistic inhibitory effect with AMP
fructose-2,6-bisphosphate
-
fructose-2,6-bisphosphate
50% inhibition in the presence of 0.2 mM fructose-1,6-bisphosphate
H2O2
isozyme EgFBPaseI is inhibited by 1 mM H2O2 and recovers when incubated with DTT
H2O2
the activity of EgFBPaseIII is partially inhibited by the H2O2 treatment, but is not reactivated when incubated with DTT, indicating that EgFBPaseIII is nonspecifically oxidized at amino acid residues, but not specifically at Cys residues
K+
-
inhibitory in the cytosol, activating in mitochondria and microsomes, depedent on the presence of Mg2+ or Mn2+, overview
K+
-
at 5 mM Mg2+, increasing K+ up to 140 mM are progressively inhibitory for neutral and alkaline isoenzyme from liver, muscle neutral isoenzyme is activated, 10% at 5 mM Mg2+ but inhibited at 1 mM Mg2+
KCl
50 mM, residual activity 20%
KCl
-
in vitro: at higher concentration KCl inhibits the salt-sensitive rice, but the salt-tolerant rice remains unaffected
Li+
-
Li+
1 mM, 50% residual activity; 1 mM, 50% residual activity
Li+
50% inhibition at 1.1 mM
Li+
-
linear competitive inhibitor
MB06322
-
-
MB06322
-
oral administration of the prodrug, MB06322, to Zucker Diabetic Fatty rats leads to dose-dependent inhibition of gluconeogenesis and endogenous glucose production and consequently to significant blood glucose reduction
Mg2+
inhibitory above 10 mM
Mg2+
-
inhibits above the optimal concentration of 1-1.5 mM
Mg2+
-
inhibition at nonphysiological high concentrations
Mg2+
-
inhibitory at higher concentration on free enzyme. Not inhibitory for enzyme in complex with aldolase. Mg2+ at physiological concentration increases the affinity of enzyme to aldolase, at higher concentration decreases the concentration of the complex
Mn2+
thermostability of LmFBPase is increased by more than 9°C in the presence of Mn2+
Mn2+
-
inhibits above the optimal concentration of 0.05-0.07 mM
Mn2+
-
inhibition above 0.5 mM
Mn2+
-
inhibitory above 3 mM
N-(5-chloro-1,3-benzoxazol-2-yl)naphthalene-2-sulfonamide
-
-
N-(5-chloro-1,3-benzoxazol-2-yl)naphthalene-2-sulfonamide
-
non-competitive
N-([4-bromo-6-[(2,2,2-trifluoroethyl)amino]pyridin-2-yl]carbamoyl)-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-([4-bromo-6-[(2,2,2-trifluoroethyl)amino]pyridin-2-yl]carbamoyl)-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-([4-bromo-6-[(methylcarbamoyl)amino]pyridin-2-yl]carbamoyl)-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-([4-bromo-6-[(methylcarbamoyl)amino]pyridin-2-yl]carbamoyl)-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-[(5-bromo-1,3-thiazol-2-yl)carbamoyl]-3-chlorobenzenesulfonamide
-
-
N-[(5-bromo-1,3-thiazol-2-yl)carbamoyl]-3-chlorobenzenesulfonamide
-
-
N-[(6-amino-4-bromopyridin-2-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-[(6-amino-4-bromopyridin-2-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-[(6-amino-4-methoxypyridin-2-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-[(6-amino-4-methoxypyridin-2-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-[(6-bromo-1H-indazol-4-yl)carbamoyl]-3-chlorobenzenesulfonamide
-
-
N-[(6-bromo-1H-indazol-4-yl)carbamoyl]-3-chlorobenzenesulfonamide
-
-
N-[(6-bromo-1H-indazol-4-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-[(6-bromo-1H-indazol-4-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-[(6-bromo-1H-indol-4-yl)carbamoyl]-3-chlorobenzenesulfonamide
-
-
N-[(6-bromo-1H-indol-4-yl)carbamoyl]-3-chlorobenzenesulfonamide
-
-
N-[(7-bromoimidazo[1,2-a]pyridin-5-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-[(7-bromoimidazo[1,2-a]pyridin-5-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-[[6-amino-4-(methylsulfanyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-[[6-amino-4-(methylsulfanyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-[[6-amino-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-[[6-amino-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-[[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-hydroxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-[[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-hydroxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-[[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-[[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
Na+
-
-
NAD+
-
-
NAD+
-
no inhibition of isoenzyme A, 67% inhibition of isoenzyme B
NaF
-
-
NH4+
-
-
NH4+
-
0.01-0.02 mM, slight activation of neutral and alkaline isoenzyme, progressive inhibition at increasing concentration
p-hydroxymercuribenzoate
-
strong
p-hydroxymercuribenzoate
-
-
phosphate
-
-
phosphate
-
product inhibitor
phosphoenolpyruvate
-
-
UDP
-
-
Zn2+
-
-
Zn2+
-
0.001-0.010 mM has no significant effect, with 0.002-0.0035 mM Zn2+, in absence of EDTA, 50% inhibition, 80% inhibition by 0.01 mM Zn2+
Zn2+
-
pH 7.5, 0.0015 mM, 92% inhibition. Inhibition of Zn2+ and AMP is synergistic
Zn2+
-
strong inhibitor at low concentrations, activator at high concentrations
Zn2+
-
due to binding to a noncatalytic divalent metal binding site
Zn2+
-
inhibitory above 3 mM
Zn2+
-
the enzyme activity is completely inhibited at concentrations higher than 1 mM in presence of 10 mM Mg2+
[5-(2-amino-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
-
-
[5-(2-amino-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
-
-
[5-(2-amino-5-isobutyl-1,3-oxazol-4-yl)-2-furyl]phosphonic acid
-
-
[5-(2-amino-5-isobutyl-1,3-oxazol-4-yl)-2-furyl]phosphonic acid
-
-
[5-(2-amino-5-phenyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
-
-
[5-(2-amino-5-phenyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
-
-
[5-(4-amino-5-bromo-1-cyclopropyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonic acid
-
-
[5-(4-amino-5-bromo-1-cyclopropyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonic acid
-
-
[5-(5-isobutyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
-
-
[5-(5-isobutyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
-
-
[5-(6-amino-3-phenylpyridin-2-yl)-2-furyl]phosphonic acid
-
-
[5-(6-amino-3-phenylpyridin-2-yl)-2-furyl]phosphonic acid
-
-
[5-[2-amino-5-(2-methylpropyl)-1,3-selenazol-4-yl]furan-2-yl]phosphonic acid
-
-
[5-[2-amino-5-(2-methylpropyl)-1,3-selenazol-4-yl]furan-2-yl]phosphonic acid
-
-
[5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]phosphonic acid
-
[5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-1-(2-ethylbutyl)-5-fluoro-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-1-(2-ethylbutyl)-5-fluoro-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5,7-dibromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5,7-dibromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5,7-dichloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5,7-dichloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-bromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-bromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-bromo-6,7-dichloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-bromo-6,7-dichloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-chloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-chloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-ethyl-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-ethyl-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-7-phenyl-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-7-phenyl-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-7-propyl-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-7-propyl-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-fluoro-1-(pentan-3-yl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-fluoro-1-(pentan-3-yl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-fluoro-7-(2-methoxyethyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-fluoro-7-(2-methoxyethyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-fluoro-7-(3-methylbutyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-fluoro-7-(3-methylbutyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-fluoro-7-(4-fluorophenyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-fluoro-7-(4-fluorophenyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-hydroxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-hydroxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-methoxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-methoxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-6-chloro-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-6-chloro-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-(3,3-dimethylbutyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-(3,3-dimethylbutyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-(4-chlorophenyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-(4-chlorophenyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-(6-chlorohexyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-(6-chlorohexyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-bromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-bromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-bromo-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-bromo-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-chloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-chloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-chloro-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-chloro-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-cyclopropyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-cyclopropyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-ethenyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-ethenyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-ethyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-ethyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
additional information
-
AMP, ADP or glucose have no effect on enzyme activity
-
additional information
I3DTM3
not inhibitory: AMP, phosphoenolpyruvate, D-fructose 1-phosphate, D-fructose 6-phosphate, and D-fructose 2,6-bisphosphate up to 5 mM; not inhibitory: AMP, phosphoenolpyruvate, D-fructose 1-phosphate, D-fructose 6-phosphate, and D-fructose 2,6-bisphosphate up to 5 mM
-
additional information
not inhibitory: AMP, phosphoenolpyruvate, D-fructose 1-phosphate, D-fructose 6-phosphate, and D-fructose 2,6-bisphosphate up to 5 mM; not inhibitory: AMP, phosphoenolpyruvate, D-fructose 1-phosphate, D-fructose 6-phosphate, and D-fructose 2,6-bisphosphate up to 5 mM
-
additional information
-
not inhibitory: AMP, phosphoenolpyruvate, D-fructose 1-phosphate, D-fructose 6-phosphate, and D-fructose 2,6-bisphosphate up to 5 mM; not inhibitory: AMP, phosphoenolpyruvate, D-fructose 1-phosphate, D-fructose 6-phosphate, and D-fructose 2,6-bisphosphate up to 5 mM
-
additional information
-
AMP, ADP or glucose have no effect on enzyme activity
-
additional information
-
cytosolic Fru-1,6-P2ase is inhibited by the effects of 15 months of elevated CO2 concentration. 37.2% decrease of activity
-
additional information
not: AMP
-
additional information
-
not: AMP
-
additional information
activity of FBPase diminishes upon dilution into assay buffers. Relative activity falls to about 70% after 2 min and reaches a threshold of about 35% after 1 h
-
additional information
-
activity of FBPase diminishes upon dilution into assay buffers. Relative activity falls to about 70% after 2 min and reaches a threshold of about 35% after 1 h
-
additional information
isozyme EgFBPaseII is resistant to H2O2 up to concentrations of 1 mM; not inhibited by concentrations of AMP up to 1 mM; not inhibited by concentrations of AMP up to 1 mM
-
additional information
isozyme EgFBPaseII is resistant to H2O2 up to concentrations of 1 mM; not inhibited by concentrations of AMP up to 1 mM; not inhibited by concentrations of AMP up to 1 mM
-
additional information
-
isozyme EgFBPaseII is resistant to H2O2 up to concentrations of 1 mM; not inhibited by concentrations of AMP up to 1 mM; not inhibited by concentrations of AMP up to 1 mM
-
additional information
no inhibition but slight activation by AMP
-
additional information
-
no inhibition but slight activation by AMP
-
additional information
-
cytosolic Fru-1,6-P2ase is inhibited by the effects of 15 months of elevated CO2 concentration. 13.3% decrease of activity
-
additional information
-
cytosolic Fru-1,6-P2ase is inhibited by the effects of 15 months of elevated CO2 concentration. 56.7% decrease of activity
-
additional information
-
inhibitor design, synthesis and molecular modeling, overview
-
additional information
-
design, synthesis, and structure-activity relationship of a series of phosphonic acid containing benzimidazoles that function as fructose-1,6-bisphosphatase inhibitors and AMP mimics
-
additional information
-
synthesis and evaluation of a series of phosphonic acid-containing thiazoles as enzyme inhibitors, structure-guided drug design approach, optimization of both the thiazole FBPase inhibitors and their prodrugs, overview
-
additional information
mammalian muscle FBPase is about 100times more susceptible to the allosteric inhibitors AMP and NAD+ and about 1000times more sensitive to inhibition by Ca2+ than the liver isozyme
-
additional information
-
mammalian muscle FBPase is about 100times more susceptible to the allosteric inhibitors AMP and NAD+ and about 1000times more sensitive to inhibition by Ca2+ than the liver isozyme
-
additional information
the FBPase pig kidney tetramer overlay of human and pig kidney (PDB IDs 1FTA and 1KZ8, respectively) show nearly identical orientation and conformation in the active site, AMP allosteric binding site, and inhibitor (4-[3-(6,7-diethoxy-quinazolin-4-ylamino)-phenyl]-thiazol-2-yl)-methanol allosteric binding site architecture
-
additional information
-
the FBPase pig kidney tetramer overlay of human and pig kidney (PDB IDs 1FTA and 1KZ8, respectively) show nearly identical orientation and conformation in the active site, AMP allosteric binding site, and inhibitor (4-[3-(6,7-diethoxy-quinazolin-4-ylamino)-phenyl]-thiazol-2-yl)-methanol allosteric binding site architecture
-
additional information
-
a series of novel indole derivatives is designed and synthesized as inhibitors of fructose-1,6-bisphosphatase (FBPase), structure-activity relationships, molecular docking, overview. No inhibition by 3-(2-carboxyethyl)-4-nitro-1H-indole-2-carboxylic acid and 3-(2-carboxyethyl)-6-nitro-1H-indole-2-carboxylic acid
-
additional information
a series of novel indole derivatives is designed and synthesized as inhibitors of fructose-1,6-bisphosphatase (FBPase), structure-activity relationships, molecular docking, overview. No inhibition by 3-(2-carboxyethyl)-4-nitro-1H-indole-2-carboxylic acid and 3-(2-carboxyethyl)-6-nitro-1H-indole-2-carboxylic acid
-
additional information
-
the FBP active site works by stabilizing the FBPase, and the allosteric site impairs the activity of FBPase through its binding of a nonsubstrate molecule. Competitive inhibition of AMP, fructose 1,6-bisphosphate, or fructose 6-phosphate binding to FBPase with fluorescent AMP analogue, 2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate (TNP-AMP)-binding FBPase
-
additional information
-
AMP, ADP or glucose have no effect on enzyme activity
-
additional information
-
rapid regulation of frucose-1,6-diphosphatase following glucose addition is controlled mainly by enzyme inhibitors
-
additional information
-
sorbitol increases the susceptibility of the enzyme to inhibition by high concentrations of D-fructose 1,6-bisphosphate
-
additional information
-
not inhibited by AMP
-
additional information
-
inhibitor design, synthesis and molecular modeling, overview
-
additional information
phosphoenolpyruvate, AMP, ADP, citrate, not inhibitory up to 1 mM
-
additional information
-
phosphoenolpyruvate, AMP, ADP, citrate, not inhibitory up to 1 mM
-
additional information
no inhibition by isocitrate
-
additional information
no inhibition by isocitrate
-
additional information
-
no inhibition by isocitrate
-
additional information
enzyme mutant T84S can be used to trap reaction intermediates, through crystallographic methods, facilitating the design of potent inhibitors via structure-based drug design
-
additional information
-
2,3-dihydro-1H-cyclopenta[b]quinoline moiety may represent a suitable scaffold for the synthesis of potent F16BPase inhibitors endowed with significantly lower epidermal growth factor receptor tyrosine kinase inhibitory activity
-
additional information
-
not: NaCl, KCl, NH4Cl
-
additional information
-
not: NH4CL
-
additional information
cFBP1 is quite sensitive to higher oxidant concentrations
-
additional information
-
cFBP1 is quite sensitive to higher oxidant concentrations
-
additional information
no inhibition by AMP; no significant effect of AMP on the phosphatase activity
-
additional information
Na+, K+, phosphoenolpyruvate
-
additional information
-
Na+, K+, phosphoenolpyruvate
-
additional information
-
not: AMP
-
additional information
-
design, synthesis, and structure-activity relationship of a series of phosphonic acid containing benzimidazoles that function as fructose-1,6-bisphosphatase inhibitors and AMP mimics
-
additional information
-
rapid inactivation in vivo by addition of glucose is caused by phosphorylation of the enzyme
-
additional information
-
cytosolic Fru-1,6-P2ase is inhibited by the effects of 15 months of elevated CO2 concentration. 30.8% decrease of activity
-
additional information
-
repression of chloroplastic enzyme in tomato fruits, using of antisence technique, does not influence metabolite levels as greatly as it does in leaves, probably because any alterations are buffered by the ability of the fruit to import sugars
-
additional information
the FBPase pig kidney tetramer overlay of human and pig kidney (PDB IDs 1FTA and 1KZ8, respectively) show nearly identical orientation and conformation in the active site, AMP allosteric binding site, and inhibitor (4-[3-(6,7-diethoxy-quinazolin-4-ylamino)-phenyl]-thiazol-2-yl)-methanol allosteric binding site architecture
-
additional information
not: AMP
-
additional information
-
not: AMP
-
additional information
-
no inhibition by AMP
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.0026 - 0.17
beta-D-glucose 1,6-bisphosphate
0.0001 - 3.2
D-fructose 1,6-bisphosphate
0.0111 - 99.98
D-fructose 1,6-diphosphate
1
D-Fructose 1-phosphate
pH 7.7
0.0018 - 0.035
D-fructose-1,6-bisphosphate
0.1 - 0.45
fructose 1,6-bisphosphate
0.00054 - 0.057
fructose 1,6-diphosphate
0.0031 - 0.021
Ribulose 1,5-diphosphate
0.016
sedoheptulose 1,6-diphosphate
-
-
0.0026 - 1.4
sedoheptulose 1,7-diphosphate
0.118
sedoheptulose-1,7-diphosphate
-
-
additional information
additional information
-
0.0026
beta-D-glucose 1,6-bisphosphate
-
wild type enzyme, in 50 mM K+HEPES pH 7.0 at 25°C
0.0048
beta-D-glucose 1,6-bisphosphate
-
mutant enzyme T16P, in 50 mM K+HEPES pH 7.0 at 25°C
0.031
beta-D-glucose 1,6-bisphosphate
-
wild type enzyme, in 50 mM K+HEPES pH 7.0 at 25°C
0.041
beta-D-glucose 1,6-bisphosphate
-
mutant enzyme H20A, in 50 mM K+HEPES pH 7.0 at 25°C
0.045
beta-D-glucose 1,6-bisphosphate
-
mutant enzyme H20Q, in 50 mM K+HEPES pH 7.0 at 25°C
0.066
beta-D-glucose 1,6-bisphosphate
-
mutant enzyme K76A, in 50 mM K+HEPES pH 7.0 at 25°C
0.17
beta-D-glucose 1,6-bisphosphate
-
mutant enzyme H20N, in 50 mM K+HEPES pH 7.0 at 25°C
0.0001
D-fructose 1,6-bisphosphate
-
pH 7.5, 30°C, wild-type enzyme
0.00011
D-fructose 1,6-bisphosphate
-
pH 7.5, 30°C, recombinant enzyme
0.00014
D-fructose 1,6-bisphosphate
-
pH 7.5, 30°C, chimeric enzyme
0.00094
D-fructose 1,6-bisphosphate
-
mutant L54A, 22°C, pH 7.5
0.0011
D-fructose 1,6-bisphosphate
mutant D121A, E-tagged, pH 7.5
0.0012
D-fructose 1,6-bisphosphate
-
wild-type, 22°C, pH 7.5
0.00125
D-fructose 1,6-bisphosphate
pH 7.5, 37°C, recombinant mutant M248D
0.00125
D-fructose 1,6-bisphosphate
mutant enzyme M248D, pH 7.5, 37°C
0.0013
D-fructose 1,6-bisphosphate
pH 7.5, mutant K50P/Y57W
0.0013
D-fructose 1,6-bisphosphate
mutant D118A, E-tagged, pH 7.5
0.0013
D-fructose 1,6-bisphosphate
wild-type muscle enzyme, pH 7.5, 37°C
0.0014
D-fructose 1,6-bisphosphate
pH 7.5, 30°C
0.0014
D-fructose 1,6-bisphosphate
22°C, pH 7.5, assay mixtures contains 1 mM phosphoenolpyruvate. Enzyme was incubated for 1 h in assay mixture. The reaction was initiated by the addition of Mg2+
0.0014
D-fructose 1,6-bisphosphate
-
mutant DELTA6
0.0014
D-fructose 1,6-bisphosphate
-
mutant DELTA8
0.0015
D-fructose 1,6-bisphosphate
liver enzyme mutant E20K/M177T/C179Q, pH 7.5, 37°C
0.0015
D-fructose 1,6-bisphosphate
muscle enzyme mutant T177M/Q179C, pH 7.5, 37°C
0.0015
D-fructose 1,6-bisphosphate
-
mutant DELTA5
0.0017
D-fructose 1,6-bisphosphate
-
wild-type enzyme
0.0017
D-fructose 1,6-bisphosphate
muscle enzyme mutant K20E/T177M/Q179C, pH 7.5, 37°C
0.0017
D-fructose 1,6-bisphosphate
22°C, pH 7.5, assay is initiated by the addition of enzyme
0.0017
D-fructose 1,6-bisphosphate
-
wild-type muscle isoenzyme enzyme
0.00175
D-fructose 1,6-bisphosphate
pH 7.5, wild-type enzyme
0.0018
D-fructose 1,6-bisphosphate
wild-type, pH 7.5
0.0018
D-fructose 1,6-bisphosphate
mutant E97A, E-tagged, pH 7.5
0.0019
D-fructose 1,6-bisphosphate
liver enzyme mutant M177T/C179Q, pH 7.5, 37°C
0.0019
D-fructose 1,6-bisphosphate
muscle enzyme mutant K20E, pH 7.5, 37°C
0.0019
D-fructose 1,6-bisphosphate
-
mutant DELTA10
0.002
D-fructose 1,6-bisphosphate
-
mutant DELTA3
0.0021
D-fructose 1,6-bisphosphate
pH 7.5, mutant K50P
0.0021
D-fructose 1,6-bisphosphate
wild-type liver enzyme, pH 7.5, 37°C
0.0021
D-fructose 1,6-bisphosphate
-
native rabbit muscle FBPase
0.0021
D-fructose 1,6-bisphosphate
-
mutant DELTA4
0.0021
D-fructose 1,6-bisphosphate
-
mutant DELTA7
0.0022
D-fructose 1,6-bisphosphate
wild-type, E-tagged, pH 7.5
0.0022
D-fructose 1,6-bisphosphate
-
wild-type liver isoenzyme enzyme
0.0023
D-fructose 1,6-bisphosphate
liver enzyme mutant E20K, pH 7.5, 37°C
0.0025
D-fructose 1,6-bisphosphate
pH 6.6, 25°C, native enzyme
0.0025
D-fructose 1,6-bisphosphate
pH 7.5, mutant A51P
0.0025
D-fructose 1,6-bisphosphate
pH 7.5, 37°C, recombinant mutant Y113A
0.0025
D-fructose 1,6-bisphosphate
mutant enzyme Y113A, pH 7.5, 37°C
0.0028
D-fructose 1,6-bisphosphate
-
mutant Y116F
0.0031
D-fructose 1,6-bisphosphate
-
-
0.0031
D-fructose 1,6-bisphosphate
-
mutant E69Q of rabbit muscle FBPase
0.00325
D-fructose 1,6-bisphosphate
pH 7.5, 37°C, recombinant mutant K112A
0.00325
D-fructose 1,6-bisphosphate
mutant enzyme K112A, pH 7.5, 37°C
0.0037
D-fructose 1,6-bisphosphate
pH 8.0, 22°C, recombinant wild-type enzyme
0.0042
D-fructose 1,6-bisphosphate
mutant enzyme M177A, pH 7.5, 37°C
0.0042 - 0.0048
D-fructose 1,6-bisphosphate
pH 7.5, 37°C, recombinant mutant M177A
0.0043
D-fructose 1,6-bisphosphate
30°C, pH 7.5, mutant enzyme F89W
0.0046
D-fructose 1,6-bisphosphate
30°C, pH 7.5, mutant enzyme F232W
0.0048
D-fructose 1,6-bisphosphate
wild-type enzyme, pH 7.5, 37°C
0.0048
D-fructose 1,6-bisphosphate
pH 7.5, 37°C, recombinant wild-type enzyme
0.0048
D-fructose 1,6-bisphosphate
30°C, pH 7.5, recombinant wild-type enzyme
0.005
D-fructose 1,6-bisphosphate
pH 6.6, 25°C, Trombin treated enzyme
0.005
D-fructose 1,6-bisphosphate
30°C, pH 7.5, mutant enzyme F16W
0.0051
D-fructose 1,6-bisphosphate
pH 7.5, 37°C, recombinant mutant L73A
0.0051
D-fructose 1,6-bisphosphate
mutant enzyme L73A, pH 7.5, 37°C
0.0052
D-fructose 1,6-bisphosphate
pH 7.5, 37°C, recombinant mutant L56A
0.0052
D-fructose 1,6-bisphosphate
mutant enzyme L56A, pH 7.5, 37°C
0.0053
D-fructose 1,6-bisphosphate
pH 7.5, 37°C, recombinant mutant Y164A
0.0053
D-fructose 1,6-bisphosphate
mutant enzyme Y164A, pH 7.5, 37°C
0.0057
D-fructose 1,6-bisphosphate
pH 8.0, 22°C, recombinant mutant T84S
0.0059
D-fructose 1,6-bisphosphate
30°C, pH 7.5, nonrecombinant enzyme
0.006
D-fructose 1,6-bisphosphate
30°C, pH 7.5, mutant enzyme F219W
0.0085
D-fructose 1,6-bisphosphate
-
pH 7.5, mutant enzyme T23I
0.0095
D-fructose 1,6-bisphosphate
-
pH 7.5, mutant enzyme T19I
0.01
D-fructose 1,6-bisphosphate
pH 6.6, 25°C, recombinant enzyme
0.0107
D-fructose 1,6-bisphosphate
-
mutant K115Q
0.0108
D-fructose 1,6-bisphosphate
-
wild-type
0.0108
D-fructose 1,6-bisphosphate
-
pH 7.5, wild-type enzyme
0.014
D-fructose 1,6-bisphosphate
pH 7.7, 50°
0.015
D-fructose 1,6-bisphosphate
37°C
0.0154
D-fructose 1,6-bisphosphate
-
pH 7.5, 30°C
0.016
D-fructose 1,6-bisphosphate
22°C, pH 7.5, the enzyme is incubated for 1 h in assay mixture. The reaction is initiated by the addition of Mg2+
0.0165
D-fructose 1,6-bisphosphate
pH and temperature not specified in the publication
0.0165
D-fructose 1,6-bisphosphate
pH 8.0, temperature not specified in the publication, recombinant enzyme
0.018
D-fructose 1,6-bisphosphate
-
pH 7.4, temperature not specified in the publication, wild-type enzyme
0.0198
D-fructose 1,6-bisphosphate
pH 8.0, 37°C
0.0201
D-fructose 1,6-bisphosphate
-
pH 7.5, mutant enzyme G20D
0.027
D-fructose 1,6-bisphosphate
pH 7.8, 48°C, mutant enzyme Y229F
0.027
D-fructose 1,6-bisphosphate
pH 7.8, 48°C, wild-type enzyme
0.03
D-fructose 1,6-bisphosphate
-
0.036
D-fructose 1,6-bisphosphate
pH 7.8, 48°C, mutant enzyme Y348F
0.04
D-fructose 1,6-bisphosphate
-
pH 7.5, 60°C, purified recombinant enzyme
0.04
D-fructose 1,6-bisphosphate
-
pH not specified in the publication, 40°C
0.04
D-fructose 1,6-bisphosphate
-
pH 7.4, temperature not specified in the publication, mutant enzyme K274L
0.0419
D-fructose 1,6-bisphosphate
pH 7.5, 37°C
0.044
D-fructose 1,6-bisphosphate
-
pH 7.7, 30°C
0.059
D-fructose 1,6-bisphosphate
recombinant enzyme, pH 8.0, 55°C
0.06
D-fructose 1,6-bisphosphate
pH 8.0, 25°C
0.06
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, mutant K29A
0.066
D-fructose 1,6-bisphosphate
-
pH 7.5, 37°C, chloroplastic enzyme
0.07
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, wild-type
0.076
D-fructose 1,6-bisphosphate
-
pH 7.5, 37°C, chloroplastic enzyme
0.08
D-fructose 1,6-bisphosphate
mutant N213A, Hill coefficient 1.8, pH 8.0, 28°C
0.08
D-fructose 1,6-bisphosphate
mutant R314A, Hill coefficient 1.8, pH 8.0, 28°C
0.08
D-fructose 1,6-bisphosphate
wild-type, Hill coefficient 1.9, pH 8.0, 28°C
0.1
D-fructose 1,6-bisphosphate
95°C
0.1
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, mutant E59A
0.1
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, mutant K239A
0.1
D-fructose 1,6-bisphosphate
mutant H215A, Hill coefficient 1.4, pH 8.0, 28°C
0.1
D-fructose 1,6-bisphosphate
mutant T102A, Hill coefficient 2.5, pH 8.0, 28°C
0.11
D-fructose 1,6-bisphosphate
mutant R164A, Hill coefficient 2.1, pH 8.0, 28°C
0.11
D-fructose 1,6-bisphosphate
pH 8.0, 26-27°C, recombinant nontreated mutant C173S/C178S
0.12
D-fructose 1,6-bisphosphate
-
pH 7.5, 80°C, purified recombinant enzyme
0.121
D-fructose 1,6-bisphosphate
-
pH 8.8, 25°C, recombinant enzyme
0.15
D-fructose 1,6-bisphosphate
-
70°C
0.15
D-fructose 1,6-bisphosphate
-
55°C
0.15
D-fructose 1,6-bisphosphate
mutant K29A, Hill coefficient 2.0, pH 8.0, 28°C
0.165
D-fructose 1,6-bisphosphate
pH and temperature not specified in the publication
0.165
D-fructose 1,6-bisphosphate
isozyme EgFBPaseI, pH 8.0, temperature not specified in the publication
0.17
D-fructose 1,6-bisphosphate
mutant D198H, Hill coefficient 1.9, pH 8.0, 28°C
0.2
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, wild-type enzyme
0.2
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, mutant D186A
0.2
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, mutant R235A
0.21
D-fructose 1,6-bisphosphate
mutant F309A, Hill coefficient 1.8, pH 8.0, 28°C
0.24
D-fructose 1,6-bisphosphate
mutant R307A, Hill coefficient 1.6, pH 8.0, 28°C
0.26
D-fructose 1,6-bisphosphate
mutant Y131A, Hill coefficient 1.6, pH 8.0, 28°C
0.3
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant R69A
0.3
D-fructose 1,6-bisphosphate
pH 8.0, 26-27°C, recombinant S-nitrosoglutathione-treated mutant C173S/C178S
0.31
D-fructose 1,6-bisphosphate
pH 8.0, 50°C
0.32
D-fructose 1,6-bisphosphate
pH 8.0, 22°C
0.43
D-fructose 1,6-bisphosphate
pH and temperature not specified in the publication
0.43
D-fructose 1,6-bisphosphate
pH and temperature not specified in the publication
0.44
D-fructose 1,6-bisphosphate
pH 7.7, 50°
0.5
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant H268A
0.5
D-fructose 1,6-bisphosphate
mutant K134A, Hill coefficient 2.2, pH 8.0, 28°C
0.6
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant Y24A
0.61
D-fructose 1,6-bisphosphate
mutant R178A, Hill coefficient 1.1, pH 8.0, 28°C
0.7
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant S19A
0.73
D-fructose 1,6-bisphosphate
pH and temperature not specified in the publication
0.9
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant S65A
0.9
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant W131A
1.32
D-fructose 1,6-bisphosphate
mutant D200A, Hill coefficient 1.4, pH 8.0, 28°C
1.4
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant R181A
1.5
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant H178A
2.2
D-fructose 1,6-bisphosphate
pH and temperature not specified in the publication
2.2
D-fructose 1,6-bisphosphate
isozyme EgFBPaseII, pH 8.0, temperature not specified in the publication
2.3
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant H244A
3.2
D-fructose 1,6-bisphosphate
mutant R176A, Hill coefficient 1.2, pH 8.0, 28°C
0.0111
D-fructose 1,6-diphosphate
pH 8.0, 23°C
99.98
D-fructose 1,6-diphosphate
-
-
0.0018
D-fructose-1,6-bisphosphate
-
pH 7.5, 22°C, wild-type enzyme
0.014
D-fructose-1,6-bisphosphate
-
pH 7.7, 30°C
0.035
D-fructose-1,6-bisphosphate
pH 7.7
0.1
fructose 1,6-bisphosphate
wild-type
0.45
fructose 1,6-bisphosphate
-
37°C, pH 10.0
0.00054
fructose 1,6-diphosphate
-
-
0.00077
fructose 1,6-diphosphate
-
-
0.0008
fructose 1,6-diphosphate
-
-
0.00084
fructose 1,6-diphosphate
mutant enzyme G191A
0.001
fructose 1,6-diphosphate
-
at 10 mM Mg2+
0.00103
fructose 1,6-diphosphate
-
mutant enzyme D74E, pH 8.5
0.0013
fructose 1,6-diphosphate
-
-
0.00131
fructose 1,6-diphosphate
-
mutant enzyme D68E, pH 7.5
0.00142
fructose 1,6-diphosphate
-
mutant enzyme N64A, pH 8.5
0.00142
fructose 1,6-diphosphate
mutant enzyme Q32L
0.0015
fructose 1,6-diphosphate
-
-
0.00153
fructose 1,6-diphosphate
mutant enzyme K42T
0.0016
fructose 1,6-diphosphate
-
mutant enzyme K71M/K72M, pH 7.5
0.00167
fructose 1,6-diphosphate
mutant enzyme K42E
0.0017
fructose 1,6-diphosphate
-
-
0.0017
fructose 1,6-diphosphate
-
mutant enzyme N64E, pH 8.5
0.00172
fructose 1,6-diphosphate
-
-
0.00181
fructose 1,6-diphosphate
mutant enzyme I190T
0.002
fructose 1,6-diphosphate
-
-
0.002
fructose 1,6-diphosphate
-
-
0.002
fructose 1,6-diphosphate
-
alkaline isoenzyme
0.0022
fructose 1,6-diphosphate
-
wild type enzyme, pH 8.5
0.0025
fructose 1,6-diphosphate
-
-
0.0028
fructose 1,6-diphosphate
-
wild type enzyme, pH 7.5
0.0028
fructose 1,6-diphosphate
-
mutant enzyme K71A, pH 7.5
0.003
fructose 1,6-diphosphate
-
activated by Mg2+ or Mn2+, at 9°C
0.0034
fructose 1,6-diphosphate
-
neutral isoenzyme
0.00344
fructose 1,6-diphosphate
-
mutant enzyme R49L
0.00351
fructose 1,6-diphosphate
-
wild type enzyme
0.00351
fructose 1,6-diphosphate
wild type enzyme
0.004
fructose 1,6-diphosphate
-
activated by Mg2+, at 17°C
0.00402
fructose 1,6-diphosphate
-
mutant enzyme K50M
0.00407
fructose 1,6-diphosphate
-
mutant enzyme R49C
0.00442
fructose 1,6-diphosphate
-
mutant enzyme R49D
0.005
fructose 1,6-diphosphate
-
-
0.005
fructose 1,6-diphosphate
-
activated by Mg2+, at 22°C or activated by Mn2+ at 17°C
0.006
fructose 1,6-diphosphate
-
without phosphoenolpyruvate
0.008
fructose 1,6-diphosphate
-
-
0.008
fructose 1,6-diphosphate
-
activated by Mn2+
0.008
fructose 1,6-diphosphate
-
activated by Mn2+ at 35°C or at 22°C
0.0083
fructose 1,6-diphosphate
-
-
0.01
fructose 1,6-diphosphate
-
at 2 mM Mg2+
0.01
fructose 1,6-diphosphate
-
activated by Mg2+, at 27°C or activated by Mn2+ at 31°C
0.011
fructose 1,6-diphosphate
-
activated by Mg2+
0.011
fructose 1,6-diphosphate
-
activated by Mg2+, at 31°C or at 35°C
0.013
fructose 1,6-diphosphate
-
in presence of 0.01 mM phosphoenolpyruvate
0.017
fructose 1,6-diphosphate
-
isoenzyme A and B
0.022
fructose 1,6-diphosphate
-
enzyme from ethanol-grown cells
0.025
fructose 1,6-diphosphate
-
isoenzyme F-II
0.029
fructose 1,6-diphosphate
-
enzyme from methanol-grown cells
0.045
fructose 1,6-diphosphate
-
-
0.052
fructose 1,6-diphosphate
-
isoenzyme F-I
0.057
fructose 1,6-diphosphate
-
isoenzyme F-I
0.0031
Ribulose 1,5-diphosphate
-
-
0.021
Ribulose 1,5-diphosphate
-
-
0.0026
sedoheptulose 1,7-diphosphate
-
-
0.008
sedoheptulose 1,7-diphosphate
-
-
0.015
sedoheptulose 1,7-diphosphate
-
isoenzyme A and B
0.03
sedoheptulose 1,7-diphosphate
-
-
0.18
sedoheptulose 1,7-diphosphate
-
isoenzyme F-I
0.3
sedoheptulose 1,7-diphosphate
-
-
1
sedoheptulose 1,7-diphosphate
-
in presence of 5 mM Mg2+
1.4
sedoheptulose 1,7-diphosphate
-
in presence of 5 mM Mn2+
additional information
additional information
-
-
-
additional information
additional information
kinetics
-
additional information
additional information
-
illumination of the chloroplast causes a decrease in Km
-
additional information
additional information
-
comparison of KM of wild-type and hybrid enzymes
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
enzyme shows a mechanism of cooperativity that arises from within a single subunit
-
additional information
additional information
-
enzyme shows a mechanism of cooperativity that arises from within a single subunit
-
additional information
additional information
-
enzyme shows unusual temperature dependence for its main substrate di-myo-inositol 1,1-phosphate
-
additional information
additional information
the Km of FBPase reaches its highest significant value in January. In March, May and June, the Km-value remains constant, and lower than January. In October the value increases again significantly with regard to the previous months, although it does not reach the peak attained in January. The lowest significant value is reached in Novemer
-
additional information
additional information
with all natural substrates, YK23 shows classical hyperbolic saturation kinetics
-
additional information
additional information
-
with all natural substrates, YK23 shows classical hyperbolic saturation kinetics
-
additional information
additional information
activity assays show that the substrate D-fructose 1,6-bisphosphate binds to the enzyme with positive cooperativity, Michaelis-Menten plot
-
additional information
additional information
-
activity assays show that the substrate D-fructose 1,6-bisphosphate binds to the enzyme with positive cooperativity, Michaelis-Menten plot
-
additional information
additional information
Michaelis-Menten kinetics, from Arrhenius plots, activation energies for phosphatase and aldolase reactions are calculated 46.5 and 75.62 kJ/mol, respectively
-
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0.026 - 175
beta-D-glucose 1,6-bisphosphate
0.0014 - 212
D-fructose 1,6-bisphosphate
3.2 - 22
D-fructose-1,6-bisphosphate
2.5
fructose 1,6-bisphosphate
wild-type
0.0004 - 34
fructose 1,6-diphosphate
additional information
additional information
-
0.026
beta-D-glucose 1,6-bisphosphate
-
mutant enzyme H20A, in 50 mM K+HEPES pH 7.0 at 25°C
0.026
beta-D-glucose 1,6-bisphosphate
-
mutant enzyme T16P, in 50 mM K+HEPES pH 7.0 at 25°C
0.62
beta-D-glucose 1,6-bisphosphate
-
mutant enzyme H20N, in 50 mM K+HEPES pH 7.0 at 25°C
1.56
beta-D-glucose 1,6-bisphosphate
-
mutant enzyme K76A, in 50 mM K+HEPES pH 7.0 at 25°C
20
beta-D-glucose 1,6-bisphosphate
-
wild type enzyme, in 50 mM K+HEPES pH 7.0 at 25°C
21.9
beta-D-glucose 1,6-bisphosphate
-
mutant enzyme H20Q, in 50 mM K+HEPES pH 7.0 at 25°C
175
beta-D-glucose 1,6-bisphosphate
-
wild type enzyme, in 50 mM K+HEPES pH 7.0 at 25°C
0.0014
D-fructose 1,6-bisphosphate
-
mutant DELTA6
0.0014
D-fructose 1,6-bisphosphate
-
mutant DELTA8
0.0015
D-fructose 1,6-bisphosphate
-
mutant DELTA5
0.0019
D-fructose 1,6-bisphosphate
-
mutant DELTA10
0.002
D-fructose 1,6-bisphosphate
-
mutant DELTA3
0.0021
D-fructose 1,6-bisphosphate
-
mutant DELTA4
0.0021
D-fructose 1,6-bisphosphate
-
mutant DELTA7
0.17
D-fructose 1,6-bisphosphate
pH and temperature not specified in the publication
0.17
D-fructose 1,6-bisphosphate
isozyme EgFBPaseI, pH 8.0, temperature not specified in the publication
0.22
D-fructose 1,6-bisphosphate
pH 8.0, 22°C, recombinant mutant T84S
0.26
D-fructose 1,6-bisphosphate
pH 7.8, 48°C, mutant enzyme Y348F
0.3
D-fructose 1,6-bisphosphate
pH 8.0, 50°C
0.3
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant S65A
0.5
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant H178A
0.55
D-fructose 1,6-bisphosphate
-
pH 7.5, lung
0.62
D-fructose 1,6-bisphosphate
pH 7.8, 48°C, wild-type enzyme
0.63
D-fructose 1,6-bisphosphate
mutant D200A, Hill coefficient 1.4, pH 8.0, 28°C
0.66
D-fructose 1,6-bisphosphate
pH 7.8, 48°C, mutant enzyme Y229F
0.7
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant Y24A
0.7
D-fructose 1,6-bisphosphate
mutant R176A, Hill coefficient 1.2, pH 8.0, 28°C
0.7
D-fructose 1,6-bisphosphate
mutant T102A, Hill coefficient 2.5, pH 8.0, 28°C
0.84
D-fructose 1,6-bisphosphate
mutant D198H, Hill coefficient 1.9, pH 8.0, 28°C
1.08
D-fructose 1,6-bisphosphate
pH and temperature not specified in the publication
1.08
D-fructose 1,6-bisphosphate
isozyme EgFBPaseII, pH 8.0, temperature not specified in the publication
1.1
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, mutant E59A
1.2
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, mutant D186A
1.2
D-fructose 1,6-bisphosphate
mutant H215A, Hill coefficient 1.4, pH 8.0, 28°C
1.2
D-fructose 1,6-bisphosphate
mutant Y131A, Hill coefficient 1.6, pH 8.0, 28°C
1.2
D-fructose 1,6-bisphosphate
pH 7.7, 50°
1.6
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant R181A
1.8
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant R69A
1.8
D-fructose 1,6-bisphosphate
mutant K134A, Hill coefficient 2.2, pH 8.0, 28°C
1.9
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant W131A
2.1
D-fructose 1,6-bisphosphate
pH 8.0, 22°C, recombinant wild-type enzyme
2.3
D-fructose 1,6-bisphosphate
mutant R164A, Hill coefficient 2.1, pH 8.0, 28°C
2.6
D-fructose 1,6-bisphosphate
mutant R314A, Hill coefficient 1.8, pH 8.0, 28°C
2.8
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant H244A
2.9
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant S19A
3.9
D-fructose 1,6-bisphosphate
mutant D118A, E-tagged, pH 7.5
3.9
D-fructose 1,6-bisphosphate
pH 7.7, 50°
4.6
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant H268A
4.9
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, wild-type enzyme
5.2
D-fructose 1,6-bisphosphate
mutant F309A, Hill coefficient 1.8, pH 8.0, 28°C
5.2
D-fructose 1,6-bisphosphate
mutant N213A, Hill coefficient 1.8, pH 8.0, 28°C
5.2
D-fructose 1,6-bisphosphate
mutant R307A, Hill coefficient 1.6, pH 8.0, 28°C
5.3
D-fructose 1,6-bisphosphate
mutant E97A, E-tagged, pH 7.5
5.4
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, mutant R235A
5.7
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, wild-type
5.8
D-fructose 1,6-bisphosphate
mutant D121A, E-tagged, pH 7.5
6.7
D-fructose 1,6-bisphosphate
pH 7.5, mutant K50P
7.1
D-fructose 1,6-bisphosphate
mutant R178A, Hill coefficient 1.1, pH 8.0, 28°C
7.5
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, mutant K239A
8
D-fructose 1,6-bisphosphate
pH 8.0, 37°C
8
D-fructose 1,6-bisphosphate
22°C, pH 7.5, the enzyme is incubated for 1 h in assay mixture. The reaction is initiated by the addition of Mg2+
8.4
D-fructose 1,6-bisphosphate
pH and temperature not specified in the publication
8.57
D-fructose 1,6-bisphosphate
-
pH 7.5, 60°C, purified recombinant enzyme
9.2
D-fructose 1,6-bisphosphate
pH 7.5, mutant K50P/Y57W
10.5
D-fructose 1,6-bisphosphate
wild-type, Hill coefficient 1.9, pH 8.0, 28°C
11.3
D-fructose 1,6-bisphosphate
-
mutant L54A, 22°C, pH 7.5
11.5 - 12.8
D-fructose 1,6-bisphosphate
pH 7.5, 37°C, recombinant mutant M177A
12.4
D-fructose 1,6-bisphosphate
pH 7.5, mutant A51P
12.8
D-fructose 1,6-bisphosphate
mutant enzyme M177A, pH 7.5, 37°C
13.5
D-fructose 1,6-bisphosphate
pH 7.5, 37°C, recombinant mutant Y164A
13.5
D-fructose 1,6-bisphosphate
mutant enzyme Y164A, pH 7.5, 37°C
14
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, mutant K29A
14.2
D-fructose 1,6-bisphosphate
30°C, pH 7.5, mutant enzyme F232W
14.6
D-fructose 1,6-bisphosphate
-
pH 7.5, 30°C
14.8
D-fructose 1,6-bisphosphate
-
pH 7.5, lung
15
D-fructose 1,6-bisphosphate
-
pH 7.5, mutant enzyme G20D
16.1
D-fructose 1,6-bisphosphate
-
pH 7.5, lung
16.7
D-fructose 1,6-bisphosphate
-
wild-type liver isoenzyme enzyme
17
D-fructose 1,6-bisphosphate
95°C
17.6
D-fructose 1,6-bisphosphate
muscle enzyme mutant K20E/T177M/Q179C, pH 7.5, 37°C
18
D-fructose 1,6-bisphosphate
pH 8.0, 22°C
18.1
D-fructose 1,6-bisphosphate
30°C, pH 7.5, mutant enzyme F16W
18.4
D-fructose 1,6-bisphosphate
liver enzyme mutant M177T/C179Q, pH 7.5, 37°C
18.6
D-fructose 1,6-bisphosphate
liver enzyme mutant E20K, pH 7.5, 37°C
18.7
D-fructose 1,6-bisphosphate
30°C, pH 7.5, mutant enzyme F219W
19.2
D-fructose 1,6-bisphosphate
30°C, pH 7.5, mutant enzyme F89W
19.7
D-fructose 1,6-bisphosphate
30°C, pH 7.5, recombinant wild-type enzyme
19.9
D-fructose 1,6-bisphosphate
muscle enzyme mutant T177M/Q179C, pH 7.5, 37°C
20
D-fructose 1,6-bisphosphate
-
wild-type, 22°C, pH 7.5
20.4
D-fructose 1,6-bisphosphate
-
pH 7.5, mutant enzyme T23I
20.5
D-fructose 1,6-bisphosphate
wild-type enzyme, pH 7.5, 37°C
20.5
D-fructose 1,6-bisphosphate
pH 7.5, 37°C, recombinant wild-type enzyme
20.7
D-fructose 1,6-bisphosphate
30°C, pH 7.5, nonrecombinant enzyme
20.8
D-fructose 1,6-bisphosphate
wild-type liver enzyme, pH 7.5, 37°C
21
D-fructose 1,6-bisphosphate
pH 7.5, 30°C
21.1
D-fructose 1,6-bisphosphate
muscle enzyme mutant K20E, pH 7.5, 37°C
21.3
D-fructose 1,6-bisphosphate
mutant K29A, Hill coefficient 2.0, pH 8.0, 28°C
21.7
D-fructose 1,6-bisphosphate
liver enzyme mutant E20K/M177T/C179Q, pH 7.5, 37°C
21.7
D-fructose 1,6-bisphosphate
-
wild-type, pH 7.0, 37°C
22
D-fructose 1,6-bisphosphate
-
pH 7.5
22
D-fructose 1,6-bisphosphate
wild-type, pH 7.5
22
D-fructose 1,6-bisphosphate
pH 7.5, wild-type enzyme
22.5
D-fructose 1,6-bisphosphate
pH 7.5, 37°C, recombinant mutant L73A
22.5
D-fructose 1,6-bisphosphate
mutant enzyme L73A, pH 7.5, 37°C
22.9
D-fructose 1,6-bisphosphate
-
pH 8.8, 25°C, recombinant enzyme
23
D-fructose 1,6-bisphosphate
wild-type, E-tagged, pH 7.5
23.4
D-fructose 1,6-bisphosphate
wild-type muscle enzyme, pH 7.5, 37°C
23.5
D-fructose 1,6-bisphosphate
-
wild-type muscle isoenzyme enzyme
24
D-fructose 1,6-bisphosphate
22°C, pH 7.5, assay is initiated by the addition of enzyme
24.3
D-fructose 1,6-bisphosphate
-
pH 7.5, wild-type enzyme
24.7
D-fructose 1,6-bisphosphate
-
mutant Y57W, pH 7.0, 37°C
25.6
D-fructose 1,6-bisphosphate
pH 7.5, 37°C, recombinant mutant L56A
25.6
D-fructose 1,6-bisphosphate
mutant enzyme L56A, pH 7.5, 37°C
26
D-fructose 1,6-bisphosphate
22°C, pH 7.5, assay mixtures contains 1 mM phosphoenolpyruvate. Enzyme was incubated for 1 h in assay mixture. The reaction was initiated by the addition of Mg2+
26.4
D-fructose 1,6-bisphosphate
pH and temperature not specified in the publication
26.4
D-fructose 1,6-bisphosphate
pH 8.0, temperature not specified in the publication, recombinant enzyme
26.8
D-fructose 1,6-bisphosphate
-
pH 7.5, mutant enzyme T19I
26.8
D-fructose 1,6-bisphosphate
pH 7.5, 37°C, recombinant mutant K112A
26.8
D-fructose 1,6-bisphosphate
mutant enzyme K112A, pH 7.5, 37°C
27.2
D-fructose 1,6-bisphosphate
pH 7.5, 37°C, recombinant mutant Y113A
27.2
D-fructose 1,6-bisphosphate
mutant enzyme Y113A, pH 7.5, 37°C
30.5
D-fructose 1,6-bisphosphate
pH 7.5, 37°C, recombinant mutant M248D
30.5
D-fructose 1,6-bisphosphate
mutant enzyme M248D, pH 7.5, 37°C
58.7
D-fructose 1,6-bisphosphate
-
pH 7.5, 80°C, purified recombinant enzyme
212
D-fructose 1,6-bisphosphate
pH and temperature not specified in the publication
212
D-fructose 1,6-bisphosphate
pH and temperature not specified in the publication
3.2
D-fructose-1,6-bisphosphate
-
pH 7.7, 30°C
22
D-fructose-1,6-bisphosphate
-
pH 7.5, 22°C, wild-type enzyme
0.0004
fructose 1,6-diphosphate
-
mutant enzyme D74A, pH 8.5
0.01
fructose 1,6-diphosphate
-
mutant enzyme D74N, pH 8.5
1.2
fructose 1,6-diphosphate
-
mutant enzyme D74E, pH 8.5
2.3
fructose 1,6-diphosphate
mutant enzyme G191A
5.4
fructose 1,6-diphosphate
-
mutant enzyme N64E, pH 8.5
6.4
fructose 1,6-diphosphate
-
mutant enzyme D68E, pH 7.5
7.1
fructose 1,6-diphosphate
-
mutant enzyme N64A, pH 8.5
9.1
fructose 1,6-diphosphate
-
wild type enzyme, pH 8.5
16
fructose 1,6-diphosphate
-
mutant enzyme K71A, pH 7.5
18
fructose 1,6-diphosphate
-
wild type enzyme
18
fructose 1,6-diphosphate
wild type enzyme
18.3
fructose 1,6-diphosphate
mutant enzyme K42T
19.3
fructose 1,6-diphosphate
mutant enzyme K42E
20.1
fructose 1,6-diphosphate
-
mutant enzyme R49D
21
fructose 1,6-diphosphate
-
wild type enzyme, pH 7.5
21.1
fructose 1,6-diphosphate
mutant enzyme I190T
22.4
fructose 1,6-diphosphate
-
mutant enzyme K50M
23.6
fructose 1,6-diphosphate
-
mutant enzyme R49L and R49C
32.1
fructose 1,6-diphosphate
mutant enzyme Q32L
34
fructose 1,6-diphosphate
-
mutant enzyme K71M/K72M, pH 7.5
additional information
additional information
-
-
additional information
additional information
-
-
-
additional information
additional information
-
comparison of kcat of wild-type and hybrid enzymes
-
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0.0031
(1H-indol-1-yl)(4-(trifluoromethyl)phenyl)methanone
Mus musculus
-
pH 7.5, 37°C
0.01091
(2,3-diethoxy-7,8,9,10-tetrahydro-6H-cyclohepta[b]quinolin-11-yl)[3-(2-methylthiazol-4-yl)phenyl]amine
Oryctolagus cuniculus
-
37°C
0.0164
(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-7-yl)methyl dihydrogen phosphate
Homo sapiens
-
0.354
(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-7-yl)phosphonic acid
Homo sapiens
-
0.0191
(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl)methyl dihydrogen phosphate
Homo sapiens
-
0.00932
(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl)phosphonic acid
Homo sapiens
-
0.0215
(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-9-yl)methyl dihydrogen phosphate
Homo sapiens
-
0.354
(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-9-yl)phosphonic acid
Homo sapiens
-
0.0417
(2-amino-5,6-dihydro-4H-benzo[6,7]cyclohepta[1,2-d][1,3]thiazol-9-yl)methyl dihydrogen phosphate
Homo sapiens
-
0.000169
(2-amino-5,6-dihydro-4H-benzo[6,7]cyclohepta[1,2-d][1,3]thiazol-9-yl)phosphonic acid
Homo sapiens
-
0.000124
(2-amino-8H-indeno[1,2-d][1,3]thiazol-4-yl)methyl dihydrogen phosphate
Homo sapiens
-
0.0284
(2-amino-8H-indeno[1,2-d][1,3]thiazol-4-yl)phosphonic acid
Homo sapiens
-
0.112
(2-amino-8H-indeno[1,2-d][1,3]thiazol-5-yl)methyl dihydrogen phosphate
Homo sapiens
-
0.0187
(2-amino-8H-indeno[1,2-d][1,3]thiazol-5-yl)phosphonic acid
Homo sapiens
-
0.112
(2-amino-8H-indeno[1,2-d][1,3]thiazol-6-yl)methyl dihydrogen phosphate
Homo sapiens
-
0.0919
(2-amino-8H-indeno[1,2-d][1,3]thiazol-6-yl)phosphonic acid
Homo sapiens
-
0.02171
(2-aminomethyl-6,7-diethoxy-2,3-dihydro-1H-cyclopenta[b]quinolin-9-yl)[3-(2-methylthiazol-4-yl)phenyl]-amine
Oryctolagus cuniculus
-
37°C
0.00029 - 0.0045
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-[(3-methylbut-2-en-1-yl)oxy]phenyl]prop-2-en-1-one
0.0017
(3-Bromo-phenyl)-(6,7-diethoxy-quinazolin-4-yl)-amine
Homo sapiens
-
IC50: 0.0017 mM
0.0045
(3-Bromo-phenyl)-(6,7-dimethoxy-2-methyl-quinazolin-4-yl)-amine
Homo sapiens
-
IC50: 0.0045 mM
0.001
(3-Bromo-phenyl)-(6,7-dimethoxy-quinazolin-4-yl)-amine
Homo sapiens
-
IC50: 0.001 mM
0.0039
(3-Bromo-phenyl)-(7-ethoxy-6-nitro-quinazolin-4-yl)-amine
Homo sapiens
-
IC50: 0.0039 mM
0.0029
(3-Bromo-phenyl)-[6-(2-methoxy-ethoxy)-quinazolin-4-yl]-amine
Homo sapiens
-
IC50: 0.0029 mM
0.0055
(3-Bromo-phenyl)-[7-methoxy-6-(2-methoxy-ethoxy)-quinazolin-4-yl]-amine
Homo sapiens
-
IC50: 0.0055 mM
0.00053
(3-Chloro-4-fluoro-phenyl)-(6,7-diethoxy-quinazolin-4-yl)-amine
Homo sapiens
-
IC50: 0.00053 mM
0.0016
(3-Chloro-phenyl)-(6,7-diethoxy-quinazolin-4-yl)-amine
Homo sapiens
-
IC50: 0.0016 mM
0.0013
(3-Chloro-phenyl)-(6,7-dimethoxy-quinazolin-4-yl)-amine
Homo sapiens
-
IC50: 0.0013 mM
0.000858
(5-[2-amino-5-[(propylsulfanyl)carbonyl]-1,3-thiazol-4-yl]furan-2-yl)phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000055 - 0.0004
(5-[4-amino-7-[3-(dimethylamino)propyl]-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl)phosphonic acid
0.0026
(6,7-diethoxy-1,2,3,4-tetrahydroacridin-9-yl)[3-(2-methylthiazol-4-yl)phenyl]amine
Oryctolagus cuniculus
-
37°C
0.0041
(6,7-diethoxy-2,3-dihydro-1H-cyclopenta[b]quinolin-9-yl)[3-(2-methylthiazol-4-yl)phenyl]amine
Oryctolagus cuniculus
-
37°C
0.0024
(6,7-Diethoxy-quinazolin-4-yl)-(3-ethynyl-phenyl)-amine
Homo sapiens
-
IC50: 0.0024 mM
0.0092
(6,7-Diethoxy-quinazolin-4-yl)-(3-fluoro-phenyl)-amine
Homo sapiens
-
IC50: 0.0092 mM
0.0021
(6,7-Diethoxy-quinazolin-4-yl)-(3-iodo-phenyl)-amine
Homo sapiens
-
IC50: 0.0021 mM
0.0009
(6,7-Dimethoxy-quinazolin-4-yl)-(3-ethynyl-phenyl)-amine
Homo sapiens
-
IC50: 0.0009 mM
0.05
1-(cyclopropyl)methyl-3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
above, pH 7.5, 37°C, recombinant His-tagged enzyme
0.05
1-benzyl-3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
above, pH 7.5, 37°C, recombinant His-tagged enzyme
0.055
2,5-dichloro-N-(4-methyl-1,3-benzoxazol-2-yl)benzenesulfonamide
Homo sapiens
-
-
0.0034
2,5-dichloro-N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
0.0064
2,5-dichloro-N-(5-methyl-1,3-benzoxazol-2-yl)benzenesulfonamide
Homo sapiens
-
-
0.0081
2,5-dichloro-N-(6-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
Homo sapiens
-
-
0.008
2,5-dichloro-N-(6-methoxy-1,3-benzoxazol-2-yl)benzenesulfonamide
Homo sapiens
-
-
0.01
2,5-dichloro-N-(6-methyl-1,3-benzoxazol-2-yl)benzenesulfonamide
Homo sapiens
-
-
0.004
2,5-dichloro-N-[5-(3-furyl)-1,3-benzoxazol-2-yl]benzenesulfonamide
Homo sapiens
-
-
0.0035
2,5-dichloro-N-[5-methoxy-7-(4-methoxypyridin-3-yl)-1,3-benzoxazol-2-yl]benzenesulfonamide
Homo sapiens
-
-
0.0017
2,5-dichloro-N-[7-(3-hydroxyphenyl)-5-methoxy-1,3-benzoxazol-2-yl]benzenesulfonamide
Homo sapiens
-
-
0.0018
2,5-dichloro-N-[7-(4-hydroxyphenyl)-5-methoxy-1,3-benzoxazol-2-yl]benzenesulfonamide
Homo sapiens
-
-
0.119
2-(2-(phenylamino)thiazol-4-yl)phenol
Sus scrofa
-
0.00022
2-(2-aminoethyl)-6,7-diethoxy-N-[3-(2-methyl-1,3-thiazol-4-yl)phenyl]quinazolin-4-amine
Homo sapiens
-
uncompetitive
0.008
2-(2-thienyl)-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.005
2-(3-pyridyl)-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.015
2-(4-(4-hydroxyphenyl)thiazol-2-ylamino)phenol
Sus scrofa
-
0.27
2-(4-phenylthiazol-2-ylamino)phenol
Sus scrofa
-
0.01
2-acetamido-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.112
2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-7-yl dihydrogen phosphate
Homo sapiens
-
0.000013
2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl dihydrogen phosphate
Homo sapiens
-
0.335
2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-9-yl dihydrogen phosphate
Homo sapiens
-
0.0013
2-amino-4-[1-(3-phosphono)phenyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002
2-amino-4-[2-(6-phosphono)pyridyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000022
2-amino-5,6-dihydro-4H-benzo[6,7]cyclohepta[1,2-d][1,3]thiazol-9-yl dihydrogen phosphate
Homo sapiens
-
0.000028
2-amino-5-(2,2,2-trifluoroethyl)-4-[2-(5-phosphono)furanyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00004
2-amino-5-(2-furanyl)-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000043
2-amino-5-(2-methoxyphenyl)-4-[2-(5-phosphono)furanyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000012
2-amino-5-(2-naphthyl)-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.95
2-amino-5-(2-thienyl)-4-[(N-phosphonomethyl)carbamoyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000044
2-amino-5-(2-thienyl)-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000021
2-amino-5-(3-methoxyphenyl)-4-[2-(5-phosphono)furanyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000032
2-amino-5-(4-acetylphenyl)-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000013
2-amino-5-(4-chlorophenyl)-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000016
2-amino-5-(4-fluorophenyl)-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000041
2-amino-5-(4-methanesulfonyl)-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000014
2-amino-5-(4-methoxycarbonylphenyl)-4-[2-(5-phosphono)-furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000022
2-amino-5-(4-methoxyphenyl)-4-[2-(5-phosphono)furanyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000021
2-amino-5-(4-methylthiophenyl)-4-[2-(5-phosphono)furanyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000034
2-amino-5-(4-phenylphenyl)-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000088
2-amino-5-(4-tert-butylphenyl)-4-[2-(5-phosphono)furanyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000016
2-amino-5-(N-morpholinyl)-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000059
2-amino-5-benzyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000015
2-amino-5-benzyloxycarbonyl-4-[2-(5-phosphono)furanyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00005
2-amino-5-bromo-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00007
2-amino-5-chloro-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000012
2-amino-5-cyclobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000021
2-amino-5-cyclohexyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000018
2-amino-5-cyclohexylmethyl-4-[2-(5-phosphono)furanyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000019
2-amino-5-cyclopentyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00002
2-amino-5-cyclopentylmethyl-4-[2-(5-phosphono)furanyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00001
2-amino-5-cyclopropylmethyl-4-[2-(5-phosphono)furanyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000033
2-amino-5-ethylthio-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00012
2-amino-5-hydroxymethyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0001
2-amino-5-iodo-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.016 - 0.061
2-amino-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
0.21
2-amino-5-isopropyl- 4-[1-(4-methoxy-3-phosphono)phenyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00003
2-amino-5-isopropyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000024
2-amino-5-isopropylthio-4-[2-(5-phosphono)furanyl]thiazole hydrobromide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00045
2-amino-5-methyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000057
2-amino-5-neopentyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.08
2-amino-5-phenyl- 4-[1-(4-fluoro-3-phosphono)phenyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.01
2-amino-5-phenyl-4-[2-(5-methyl-4-phosphono)oxazolyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.01
2-amino-5-phenyl-4-[3-(1-phosphono)pyrrolyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0003
2-amino-5-phenylthio-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.135
2-amino-5-propyl- 4-[1-(4-methyl-3-phosphono)phenyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.05
2-amino-5-propyl-4-phosphonomethoxycarbonylthiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.25
2-amino-5-propyl-4-[1-(3-phosphono)phenyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0005
2-amino-5-propyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000024
2-amino-5-tert-butylthio-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00015
2-amino-5-[(4-morpholinyl)methyl]-4-[2-(5-phosphono)furanyl]-thiazole dihydrobromide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0017
2-amino-5-[(N,N-dimethyl)carbamoyl]-4-[2-(5-phosphono)-furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00007
2-amino-8H-indeno[1,2-d][1,3]thiazol-4-yl dihydrogen phosphate
Homo sapiens
-
0.307
2-amino-8H-indeno[1,2-d][1,3]thiazol-5-yl dihydrogen phosphate
Homo sapiens
-
0.146
2-amino-8H-indeno[1,2-d][1,3]thiazol-6-yl dihydrogen phosphate
Homo sapiens
-
0.00008
2-bromo-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0065
2-bromo-N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
Homo sapiens
-
-
0.00275
2-carbamoyl-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00018
2-chloro-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002
2-cyano-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0004
2-ethyl-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00022
2-hydroxymethyl-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0001
2-methyl-5-isobutyl-4-[2-(5-phosphono)furanyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.001
2-methylamino-5-isobutyl-4-[2-(5-hosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00089
2-methylthio-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
3.1
2-oxoglutarate
Mycobacterium tuberculosis
versus MtFBPaseII, pH and temperature not specified in the publication
0.0135
2-phenyl-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0005
2-thiocarbamoyl-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0012
2-vinyl-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00187
2-[(3S,11aS)-3-(4-hydroxybenzyl)-1,4-dioxo-1,3,4,6,11,11a-hexahydro-2H-pyrazino[1,2-b]isoquinolin-2-yl]-N-[2-(4-hydroxyphenyl)ethyl]pentanamide
Homo sapiens
-
uncompetitive
0.00052 - 0.0073
2-[3-methyl-5-([[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]sulfamoyl)thiophen-2-yl]ethyl acetate
0.00067 - 0.0035
2-[5-([[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]sulfamoyl)-3-methylthiophen-2-yl]ethyl acetate
0.0147
3,4-dihydroxy-N'-[(E)-[4-oxo-6-(propan-2-yl)-4H-chromen-3-yl]methylidene]benzohydrazide
Synechocystis sp.
pH 7.5, temperature not specified in the publication
0.0061
3,5-diphenyl-1-(3-(trifluoromethyl) phenyl)-1H-pyrazole
Mus musculus
-
pH 7.5, 37°C
0.05
3-(2-(ethoxycarbonyl)-7-nitro-1H-indol-3-yl)propanoic acid
Homo sapiens
above, pH 7.5, 37°C, recombinant His-tagged enzyme
0.0025
3-(2-carboxyethyl)-4,6-dichloro-1H-indole-2-carboxylic acid
Homo sapiens
-
non-competitive
0.0024
3-(2-carboxyethyl)-4-(2-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid
0.00069
3-(2-carboxyethyl)-4-(2-methylpropyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
-
0.00527
3-(2-carboxyethyl)-4-(3-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid
0.00131
3-(2-carboxyethyl)-4-(3-methoxyanilino)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
-
0.00522
3-(2-carboxyethyl)-4-(3-methoxyphenyl)-7-nitro-1H-indole-2-carboxylic acid
0.0024
3-(2-carboxyethyl)-4-(4-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid
0.0017
3-(2-carboxyethyl)-4-(4-methoxyanilino)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
-
0.0018
3-(2-carboxyethyl)-4-(4-methoxyphenyl)-7-nitro-1H-indole-2-carboxylic acid
0.00088
3-(2-carboxyethyl)-4-chloro-7-nitro-1H-indole-2-carboxylic acid
0.00276
3-(2-carboxyethyl)-4-ethyl-7-nitro-1H-indole-2-carboxylic acid
0.00069
3-(2-carboxyethyl)-4-isobutyl-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00045
3-(2-carboxyethyl)-5-(2-methylpropyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
-
0.00129
3-(2-carboxyethyl)-5-bromo-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00207
3-(2-carboxyethyl)-5-chloro-7-nitro-1H-indole-2-carboxylic acid
0.0001
3-(2-carboxyethyl)-5-ethyl-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.0001
3-(2-carboxyethyl)-5-ethyl-7-nitro-1H-indole-2-carboxylicacid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00045
3-(2-carboxyethyl)-5-isobutyl-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.05
3-(2-carboxyethyl)-5-nitro-1H-indole-2-carboxylic acid
Homo sapiens
above, pH 7.5, 37°C, recombinant His-tagged enzyme
0.0016
3-(2-carboxyethyl)-5-phenylamino-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00517
3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
0.00131
3-(2-carboxyethyl)-7-nitro-4-(3-methoxyphenylamino)-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.0011
3-(2-carboxyethyl)-7-nitro-4-(3-nitrophenyl)-1H-indole-2-carboxylic acid
0.0017
3-(2-carboxyethyl)-7-nitro-4-(4-methoxyphenylamino)-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.002
3-(2-carboxyethyl)-7-nitro-4-(4-nitrophenyl)-1H-indole-2-carboxylic acid
0.0014
3-(2-carboxyethyl)-7-nitro-4-phenyl-1H-indole-2-carboxylic acid
0.00069
3-(2-carboxyethyl)-7-nitro-4-phenylamino-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00643
3-(2-carboxyethyl)-7-nitro-5-phenyl-1H-indole-2-carboxylic acid
0.05
3-(4-(4-hydroxyphenyl)thiazol-2-ylamino)benzenesulfonamide
Sus scrofa
-
0.013
3-(4-(4-hydroxyphenyl)thiazol-2-ylamino)phenol
Sus scrofa
-
0.104
3-(4-phenylthiazol-2-ylamino)benzenesulfonamide
Sus scrofa
-
0.035
3-(4-phenylthiazol-2-ylamino)phenol
Sus scrofa
-
0.0013
3-chloro-N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
Homo sapiens
-
-
0.00064 - 0.012
3-chloro-N-[(3,5-dichlorophenyl)carbamoyl]benzenesulfonamide
0.00099
3-ethyl-5-isobutyl-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
-
pH 7.5, 37°C
0.02
4-(2-(2-hydroxyphenylamino)thiazol-4-yl)benzene-1,3-diol
Sus scrofa
-
0.006
4-(2-(3-hydroxyphenylamino)thiazol-4-yl)benzene-1,3-diol
Sus scrofa
-
0.048
4-(2-(3-nitrophenylamino)thiazol-4-yl)phenol
Sus scrofa
-
0.011
4-(2-(4-hydroxyphenylamino)thiazol-4-yl)benzene-1,3-diol
Sus scrofa
-
0.246
4-(2-(4-nitrophenylamino)thiazol-4-yl)phenol
Sus scrofa
-
0.343
4-(2-(phenylamino)thiazol-4-yl)benzene-1,3-diol
Sus scrofa
-
0.055
4-(4-(2,4-dihydroxyphenyl)thiazol-2-ylamino)benzenesulfonamide
Sus scrofa
-
0.032
4-(4-(4-hydroxyphenyl)thiazol-2-ylamino)benzenesulfonamide
Sus scrofa
-
0.048
4-(4-(4-hydroxyphenyl)thiazol-2-ylamino)phenol
Sus scrofa
-
0.145
4-(4-phenylthiazol-2-ylamino)benzenesulfonamide
Sus scrofa
-
0.124
4-(4-phenylthiazol-2-ylamino)phenol
Sus scrofa
-
0.00069
4-anilino-3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
-
0.024
4-tert-butyl-N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
Homo sapiens
-
-
0.015
4-[[(2R,4S)-4-(3-chlorophenyl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazole
Hominoidea
-
-
0.1
4-[[(2R,4S)-4-(3-methoxyphenyl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazole
Hominoidea
-
value above
0.066
4-[[(2R,4S)-4-(4-chlorophenyl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazole
Hominoidea
-
-
0.1
4-[[(2S,4S)-4-(3-chlorophenyl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazole
Hominoidea
-
value above
0.1
4-[[(2S,4S)-4-(3-methoxyphenyl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazole
Hominoidea
-
value above
0.1
4-[[(2S,4S)-4-(4-chlorophenyl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazole
Hominoidea
-
value above
0.00298
5-(1H-tetrazol-5-yl)-N-(3-(5-p-tolyl-1,3,4-oxadiazol-2-yl)phenyl)pentanamide
Homo sapiens
-
pH 7.5, temperature not specified in the publication
0.00035 - 0.004
5-(2-hydroxyethyl)-4-methyl-N-[[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
0.00017 - 0.0016
5-(2-methoxyethyl)-4-methyl-N-([6-[(methylcarbamoyl)amino]-4-(methylsulfanyl)pyridin-2-yl]carbamoyl)thiophene-2-sulfonamide
0.0017 - 0.0083
5-(2-methoxyethyl)-4-methyl-N-[[4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
0.00053 - 0.007
5-(2-methoxyethyl)-4-methyl-N-[[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
0.00022 - 0.0026
5-(2-methoxyethyl)-N-([4-methoxy-6-[(methylcarbamoyl)amino]pyridin-2-yl]carbamoyl)-4-methylthiophene-2-sulfonamide
0.0016
5-anilino-3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
-
0.00129
5-bromo-3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
-
0.0005
5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0041
6,7-diethoxy-N-[3-(2-methyl-1,3-thiazol-4-yl)phenyl]quinazolin-4-amine
Oryctolagus cuniculus
-
-
0.022
6,7-dimethyl-4-[[(2R,4S)-2-oxido-4-(pyridin-2-yl)-1,3,2-dioxaphosphinan-2-yl]methoxy]-8H-indeno[1,2-d][1,3]thiazole
Hominoidea
-
-
0.0088
6,7-dimethyl-4-[[(2R,4S)-2-oxido-4-(pyridin-3-yl)-1,3,2-dioxaphosphinan-2-yl]methoxy]-8H-indeno[1,2-d][1,3]thiazole
Hominoidea
-
-
0.041
6,7-dimethyl-4-[[(2R,4S)-2-oxido-4-(pyridin-4-yl)-1,3,2-dioxaphosphinan-2-yl]methoxy]-8H-indeno[1,2-d][1,3]thiazole
Hominoidea
-
-
0.004 - 0.011
6,7-dimethyl-4-[[(2R,4S)-4-(2-methylpyridin-3-yl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-8H-indeno[1,2-d][1,3]thiazole
0.1
6,7-dimethyl-4-[[(2R,4S)-4-(6-methylpyridin-3-yl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-8H-indeno[1,2-d][1,3]thiazole
Hominoidea
-
value above
0.00132
6-hydroxy-N-(3-(5-p-tolyl-1,3,4-oxadiazol-2-yl)phenyl)hexanamide
Homo sapiens
-
pH 7.5, temperature not specified in the publication
0.00532
6-oxo-6-(3-(5-p-tolyl-1,3,4-oxadiazol-2-yl)phenylamino)hexanoic acid
Homo sapiens
-
pH 7.5, temperature not specified in the publication
0.05
7-amino-3-(2-carboxyethyl)-1H-indole-2-carboxylic acid
Homo sapiens
above, pH 7.5, 37°C, recombinant His-tagged enzyme
3.1
alpha-ketoglutarate
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.055
D-fructose 1,6-bisphosphate
Pelophylax lessonae
-
pH 7.5, 25°C
0.00062 - 0.0105
D-fructose 2,6-bisphosphate
0.002
diethyl (5-[4-amino-1-[(1R,2R)-bicyclo[2.2.1]hept-2-ylamino]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
0.004 - 0.02
diethyl (5-[4-amino-1-[3-(thiophen-3-ylmethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
0.0042 - 0.02
diethyl (5-[4-amino-1-[4-(furan-3-ylmethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
0.007 - 0.02
diethyl (5-[4-amino-1-[4-(trifluoromethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
0.005 - 0.02
diethyl [5-(4-amino-1-benzyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
0.00225 - 0.04
diethyl [5-(4-amino-1-ethyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
0.006 - 0.02
diethyl [5-(4-amino-1-methyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
0.0011 - 0.002
diethyl [5-(4-amino-1-propyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
0.0015 - 0.004
diethyl [5-[4-amino-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
0.00185 - 0.02
diethyl [5-[4-amino-1-(3-hydroxybenzyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
0.0095 - 0.02
diethyl [5-[4-amino-1-(4-tert-butylbenzyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
0.0025 - 0.02
diethyl [5-[4-amino-1-(biphenyl-4-ylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
0.0008 - 0.002
diethyl [5-[4-amino-1-(cyclobutylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
0.00325 - 0.02
diethyl [5-[4-amino-1-(cycloheptylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
0.002 - 0.0025
diethyl [5-[4-amino-1-(cyclohexylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
0.0015 - 0.002
diethyl [5-[4-amino-1-(cyclopentylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
0.0008 - 0.2
diethyl [5-[4-amino-1-(cyclopropylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
0.0068
ethyl (2S,6S)-4-[[(6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazol-4-yl)oxy]methyl]-2,6-dimethyl-7-oxo-8-oxa-3,5-diaza-4-phosphadecan-1-oate 4-oxide
Hominoidea
-
-
0.0119
ethyl 3,3,3-trifluoro-2-hydroxy-2-(1-methyl-1H-indol-3-yl)propanoate
Mus musculus
-
pH 7.5, 37°C
0.0048
ethyl 3-(3,5-dimethyl-1H-pyrrol-2-yl)-4,4,4-trifluoro-3-hydroxybutanoate
Mus musculus
-
pH 7.5, 37°C
0.00075 - 0.0105
fructose 2,6-bisphosphate
0.019
N'-[(E)-(6-ethyl-4-oxo-4H-chromen-3-yl)methylidene]-3,4-dihydroxybenzohydrazide
Synechocystis sp.
pH 7.5, temperature not specified in the publication
0.0141
N'-[(E)-(6-tert-butyl-4-oxo-4H-chromen-3-yl)methylidene]-3,4-dihydroxybenzohydrazide
Synechocystis sp.
pH 7.5, temperature not specified in the publication
0.318 - 2.5
N,4-diphenylthiazol-2-amine
0.0026
N,N'-bis(6,7-diethoxy-2,3-dihydro-1H-cyclopenta[b]quinolin-9-yl)pentane-1,5-diamine
Homo sapiens
-
uncompetitive
0.0031
N,N'-bis-(6,7-diethoxy-2,3-dihydro-1H-cyclopenta[b]quinolin-9-yl)hexan-1,6-diamine
Oryctolagus cuniculus
-
37°C
0.0295
N,N'-bis-(6,7-diethoxy-2,3-dihydro-1H-cyclopenta[b]quinolin-9-yl)propan-1,3-diamine
Oryctolagus cuniculus
-
37°C
0.0019
N-(5-bromo-1,3-benzoxazol-2-yl)-2,5-dichlorobenzenesulfonamide
Homo sapiens
-
-
0.0094
N-(5-chloro-1,3-benzoxazol-2-yl)-1-methyl-1H-imidazole-4-sulfonamide
Homo sapiens
-
-
0.023
N-(5-chloro-1,3-benzoxazol-2-yl)-2-(1H-imidazol-1-yl)benzenesulfonamide
Homo sapiens
-
-
0.006
N-(5-chloro-1,3-benzoxazol-2-yl)-2-cyanobenzenesulfonamide
Homo sapiens
-
-
0.0018
N-(5-chloro-1,3-benzoxazol-2-yl)-3-nitrobenzenesulfonamide
Homo sapiens
-
-
0.0067
N-(5-chloro-1,3-benzoxazol-2-yl)-4-(3-furyl)benzenesulfonamide
Homo sapiens
-
-
0.0078
N-(5-chloro-1,3-benzoxazol-2-yl)-4-(trifluoromethoxy)benzenesulfonamide
Homo sapiens
-
-
0.0028
N-(5-chloro-1,3-benzoxazol-2-yl)-4-fluorobenzenesulfonamide
Homo sapiens
-
-
0.0062
N-(5-chloro-1,3-benzoxazol-2-yl)-4-methylbenzenesulfonamide
Homo sapiens
-
-
0.0034
N-(5-chloro-1,3-benzoxazol-2-yl)anthracene-2-sulfonamide
Homo sapiens
-
-
0.0077
N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
Homo sapiens
-
-
0.0038
N-(5-chloro-1,3-benzoxazol-2-yl)biphenyl-2-sulfonamide
Homo sapiens
-
-
0.0098
N-(5-chloro-1,3-benzoxazol-2-yl)biphenyl-3-sulfonamide
Homo sapiens
-
-
0.004
N-(5-chloro-1,3-benzoxazol-2-yl)biphenyl-4-sulfonamide
Homo sapiens
-
-
0.0025
N-(5-chloro-1,3-benzoxazol-2-yl)naphthalene-2-sulfonamide
0.013
N-(5-chloro-1,3-benzoxazol-2-yl)thiophene-2-sulfonamide
Homo sapiens
-
-
0.032
N-(5-tert-butyl-1,3-benzoxazol-2-yl)-2,5-dichlorobenzenesulfonamide
Homo sapiens
-
-
0.00851
N-(6,7-diethoxy-9-[3-(2-methylthiazol-4-yl)phenylamino]-2,3-dihydro-1H-cyclopenta[b]quinolin-1-yl)-acetamide
Oryctolagus cuniculus
-
37°C
0.0002 - 0.0037
N-([4-bromo-6-[(2,2,2-trifluoroethyl)amino]pyridin-2-yl]carbamoyl)-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
0.00008 - 0.001
N-([4-bromo-6-[(methylcarbamoyl)amino]pyridin-2-yl]carbamoyl)-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
0.00033 - 0.0058
N-[(5-bromo-1,3-thiazol-2-yl)carbamoyl]-3-chlorobenzenesulfonamide
0.00013 - 0.0015
N-[(6-amino-4-bromopyridin-2-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
0.0004 - 0.03
N-[(6-amino-4-methoxypyridin-2-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
0.00033 - 0.0033
N-[(6-bromo-1H-indazol-4-yl)carbamoyl]-3-chlorobenzenesulfonamide
0.00014 - 0.0017
N-[(6-bromo-1H-indazol-4-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
0.00035 - 0.005
N-[(6-bromo-1H-indol-4-yl)carbamoyl]-3-chlorobenzenesulfonamide
0.00082 - 0.008
N-[(7-bromoimidazo[1,2-a]pyridin-5-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
0.012
N-[4-[[(5-chloro-1,3-benzoxazol-2-yl)amino]sulfonyl]phenyl]butanamide
Homo sapiens
-
-
0.00057
N-[6-(4-aminophenyl)-5-methoxy-1,3-benzoxazol-2-yl]-2,5-dichlorobenzenesulfonamide
Homo sapiens
-
non-competitive
0.00057
N-[7-(3-aminophenyl)-5-methoxy-1,3-benzoxazol-2-yl]-2,5-dichlorobenzenesulfonamide
Homo sapiens
-
-
0.0013
N-[7-(4-aminophenyl)-5-methoxy-1,3-benzoxazol-2-yl]-2,5-dichlorobenzenesulfonamide
Homo sapiens
-
-
0.0026
N-[7-[3-(aminomethyl)phenyl]-5-methoxy-1,3-benzoxazol-2-yl]-2,5-dichlorobenzenesulfonamide
Homo sapiens
-
-
0.0018 - 0.009
N-[[6-amino-4-(methylsulfanyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
0.00076 - 0.006
N-[[6-amino-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
0.00042 - 0.004
N-[[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-hydroxyethyl)-4-methylthiophene-2-sulfonamide
0.0006 - 0.0035
N-[[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
0.0119
N4-(3-Bromo-phenyl)-7-chloro-quinazoline-4,6-diamine
Homo sapiens
-
IC50: 0.0119 mM
0.000047
[(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl)(difluoro)methyl]phosphonic acid
Homo sapiens
-
0.00084
[(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl)methyl]phosphonic acid
Homo sapiens
-
0.012
[(2R,3S,4R,5R)-5-[4-(aminocarbonyl)-1H-imidazol-1-yl]-3,4-dihydroxytetrahydrofuran-2-yl]methyl dihydrogen phosphate
Homo sapiens
-
-
0.5
[2-[(6-amino-8,9-dihydro-7H-purin-8-yl)amino]ethyl]phosphonate
Homo sapiens
-
0.097
[2-[[6-amino-9-(2-cyclohexylethyl)-8,9-dihydro-7H-purin-8-yl]amino]ethyl]phosphonate
Homo sapiens
-
0.026
[3-[6-amino-9-(2-cyclohexylethyl)-8,9-dihydro-7H-purin-8-yl]propyl]phosphonate
Homo sapiens
-
0.005
[5-(1,3-thiazol-4-yl)-2-furyl]phosphonic acid
Homo sapiens
-
-
0.00045 - 0.013
[5-(2-amino-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
0.00012 - 0.002
[5-(2-amino-5-isobutyl-1,3-oxazol-4-yl)-2-furyl]phosphonic acid
0.000016
[5-(2-amino-5-isobutyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
Homo sapiens
-
non-competitive
0.005
[5-(2-amino-5-isobutyl-1H-imidazol-4-yl)-2-furyl]phosphonic acid
Homo sapiens
-
-
0.000014 - 0.0005
[5-(2-amino-5-phenyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
0.000014
[5-(2-amino-5-phenyl-1,3-thiazol-4-yl)furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00003
[5-(2-amino-5-propyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
Homo sapiens
-
-
0.01
[5-(2-amino-5-propyl-1,3-thiazol-4-yl)thiophen-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0016
[5-(4-amino-1-tert-butyl-2,3-dihydro-1H-benzimidazol-2-yl)-2-furyl]phosphonate
Homo sapiens
-
0.00009
[5-(4-amino-1-tert-butyl-7-ethyl-5-fluoro-2,3-dihydro-1H-benzimidazol-2-yl)-2-furyl]phosphonate
Homo sapiens
-
0.000055 - 0.00218
[5-(4-amino-5-bromo-1-cyclopropyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonic acid
0.0005 - 0.0035
[5-(5-isobutyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
0.000042 - 0.0016
[5-(6-amino-3-phenylpyridin-2-yl)-2-furyl]phosphonic acid
0.0022
[5-(6-amino-9-tert-butyl-8,9-dihydro-7H-purin-8-yl)-2-furyl]phosphonate
Homo sapiens
-
0.000039 - 0.00015
[5-[2-amino-5-(2-methylpropyl)-1,3-selenazol-4-yl]furan-2-yl]phosphonic acid
0.000001 - 0.000025
[5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]phosphonic acid
0.000014
[5-[2-amino-5-(ethoxycarbonyl)-1,3-thiazol-4-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000016
[5-[2-amino-5-(propylsulfanyl)-1,3-thiazol-4-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00015 - 0.00085
[5-[4-amino-1-(2-ethylbutyl)-5-fluoro-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.001 - 0.002
[5-[4-amino-5,7-dibromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.00045 - 0.002
[5-[4-amino-5,7-dichloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.0004 - 0.002
[5-[4-amino-5-bromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.01
[5-[4-amino-5-bromo-6,7-dichloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0002 - 0.002
[5-[4-amino-5-chloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.0025 - 0.02
[5-[4-amino-5-ethyl-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.0001 - 0.00225
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.00009 - 0.0009
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-7-phenyl-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.0001 - 0.00065
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-7-propyl-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.00085 - 0.00215
[5-[4-amino-5-fluoro-1-(pentan-3-yl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.00008 - 0.00045
[5-[4-amino-5-fluoro-7-(2-methoxyethyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.0001 - 0.0021
[5-[4-amino-5-fluoro-7-(3-methylbutyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.00018 - 0.0013
[5-[4-amino-5-fluoro-7-(4-fluorophenyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.0005 - 0.02
[5-[4-amino-5-hydroxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.0007 - 0.02
[5-[4-amino-5-methoxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.000225 - 0.002
[5-[4-amino-6-chloro-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.00021 - 0.0016
[5-[4-amino-7-(3,3-dimethylbutyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.00009 - 0.002
[5-[4-amino-7-(4-chlorophenyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.00007 - 0.0005
[5-[4-amino-7-(6-chlorohexyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.0004 - 0.002
[5-[4-amino-7-bromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.00013 - 0.00209
[5-[4-amino-7-bromo-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.0009
[5-[4-amino-7-chloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0001 - 0.002
[5-[4-amino-7-chloro-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.00006 - 0.00035
[5-[4-amino-7-cyclopropyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.00028 - 0.0009
[5-[4-amino-7-ethenyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.000055 - 0.00055
[5-[4-amino-7-ethyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.00056
[5-[5-(2-methylpropyl)-2-phenyl-1,3-thiazol-4-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0011
[5-[6-amino-9-(2,2-dimethylpropyl)-8,9-dihydro-7H-purin-8-yl]-2-furyl]phosphonate
Homo sapiens
-
0.0012
[5-[6-amino-9-(2-cyclohexylethyl)-8,9-dihydro-7H-purin-8-yl]-2-furyl]phosphonate
Homo sapiens
-
0.005 - 0.015
[5-[6-amino-9-(2-phenylethyl)-8,9-dihydro-7H-purin-8-yl]-2-furyl]phosphonate
0.00029
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-[(3-methylbut-2-en-1-yl)oxy]phenyl]prop-2-en-1-one
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0045
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-[(3-methylbut-2-en-1-yl)oxy]phenyl]prop-2-en-1-one
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.000055
(5-[4-amino-7-[3-(dimethylamino)propyl]-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl)phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0004
(5-[4-amino-7-[3-(dimethylamino)propyl]-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl)phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0034
2,5-dichloro-N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
Homo sapiens
-
-
0.0034
2,5-dichloro-N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
Homo sapiens
-
non-competitive
0.016
2-amino-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
-
0.061
2-amino-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Rattus norvegicus
-
-
0.00052
2-[3-methyl-5-([[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]sulfamoyl)thiophen-2-yl]ethyl acetate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0073
2-[3-methyl-5-([[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]sulfamoyl)thiophen-2-yl]ethyl acetate
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.00067
2-[5-([[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]sulfamoyl)-3-methylthiophen-2-yl]ethyl acetate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0035
2-[5-([[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]sulfamoyl)-3-methylthiophen-2-yl]ethyl acetate
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.0024
3-(2-carboxyethyl)-4-(2-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.0024
3-(2-carboxyethyl)-4-(2-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00527
3-(2-carboxyethyl)-4-(3-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.00527
3-(2-carboxyethyl)-4-(3-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00522
3-(2-carboxyethyl)-4-(3-methoxyphenyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.00522
3-(2-carboxyethyl)-4-(3-methoxyphenyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.0024
3-(2-carboxyethyl)-4-(4-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.0024
3-(2-carboxyethyl)-4-(4-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.0018
3-(2-carboxyethyl)-4-(4-methoxyphenyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.0018
3-(2-carboxyethyl)-4-(4-methoxyphenyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00088
3-(2-carboxyethyl)-4-chloro-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.00088
3-(2-carboxyethyl)-4-chloro-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00276
3-(2-carboxyethyl)-4-ethyl-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.00276
3-(2-carboxyethyl)-4-ethyl-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00207
3-(2-carboxyethyl)-5-chloro-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.00207
3-(2-carboxyethyl)-5-chloro-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00517
3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.00517
3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.0011
3-(2-carboxyethyl)-7-nitro-4-(3-nitrophenyl)-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.0011
3-(2-carboxyethyl)-7-nitro-4-(3-nitrophenyl)-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.002
3-(2-carboxyethyl)-7-nitro-4-(4-nitrophenyl)-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.002
3-(2-carboxyethyl)-7-nitro-4-(4-nitrophenyl)-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.0014
3-(2-carboxyethyl)-7-nitro-4-phenyl-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.0014
3-(2-carboxyethyl)-7-nitro-4-phenyl-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00643
3-(2-carboxyethyl)-7-nitro-5-phenyl-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.00643
3-(2-carboxyethyl)-7-nitro-5-phenyl-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00064
3-chloro-N-[(3,5-dichlorophenyl)carbamoyl]benzenesulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.012
3-chloro-N-[(3,5-dichlorophenyl)carbamoyl]benzenesulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.00035
5-(2-hydroxyethyl)-4-methyl-N-[[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.004
5-(2-hydroxyethyl)-4-methyl-N-[[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.00017
5-(2-methoxyethyl)-4-methyl-N-([6-[(methylcarbamoyl)amino]-4-(methylsulfanyl)pyridin-2-yl]carbamoyl)thiophene-2-sulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0016
5-(2-methoxyethyl)-4-methyl-N-([6-[(methylcarbamoyl)amino]-4-(methylsulfanyl)pyridin-2-yl]carbamoyl)thiophene-2-sulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.0017
5-(2-methoxyethyl)-4-methyl-N-[[4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0083
5-(2-methoxyethyl)-4-methyl-N-[[4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.00053
5-(2-methoxyethyl)-4-methyl-N-[[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.007
5-(2-methoxyethyl)-4-methyl-N-[[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.00022
5-(2-methoxyethyl)-N-([4-methoxy-6-[(methylcarbamoyl)amino]pyridin-2-yl]carbamoyl)-4-methylthiophene-2-sulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0026
5-(2-methoxyethyl)-N-([4-methoxy-6-[(methylcarbamoyl)amino]pyridin-2-yl]carbamoyl)-4-methylthiophene-2-sulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.004
6,7-dimethyl-4-[[(2R,4S)-4-(2-methylpyridin-3-yl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-8H-indeno[1,2-d][1,3]thiazole
Hominoidea
-
shows weak CYP3A4 inhibitor potency
0.011
6,7-dimethyl-4-[[(2R,4S)-4-(2-methylpyridin-3-yl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-8H-indeno[1,2-d][1,3]thiazole
Hominoidea
-
-
0.00014
AMP
Homo sapiens
-
mutant DELTA3
0.00016
AMP
Homo sapiens
-
wild-type enzyme
0.00016
AMP
Oryctolagus cuniculus
-
native rabbit muscle FBPase
0.00016
AMP
Homo sapiens
-
wild-type muscle enzyme
0.00019
AMP
Homo sapiens
wild-type, pH 7.4, 25°C, Hill-coefficient 1.34
0.0002
AMP
Pelophylax lessonae
-
pH 7.5, 25°C
0.00021
AMP
Oryctolagus cuniculus
-
mutant E69Q of rabbit muscle FBPase
0.00033
AMP
Homo sapiens
-
mutant DELTA4
0.00081
AMP
Homo sapiens
-
mutant DELTA5
0.001
AMP
Homo sapiens
-
-
0.00139
AMP
Homo sapiens
-
mutant DELTA6
0.00197
AMP
Homo sapiens
-
mutant DELTA10
0.0022
AMP
Escherichia coli
22°C, pH 7.5, the enzyme is incubated for 1 h in assay mixture. The reaction is initiated by the addition of Mg2+
0.0025
AMP
Sus scrofa
mutant enzyme Y164A, pH 7.5, 37°C
0.0025 - 0.0035
AMP
Sus scrofa
pH 7.5, 37°C, recombinant mutant Y164A
0.0031
AMP
Sus scrofa
30°C, pH 7.5, mutant enzyme F89W
0.0034
AMP
Sus scrofa
30°C, pH 7.5, mutant enzyme F219W
0.0035
AMP
Sus scrofa
mutant enzyme M177A, pH 7.5, 37°C
0.0035 - 0.0039
AMP
Sus scrofa
pH 7.5, 37°C, recombinant mutant M177A
0.00365
AMP
Homo sapiens
mutant Q32R, pH 7.4, 25°C, Hill-coefficient 0.59
0.00393
AMP
Homo sapiens
-
mutant DELTA7
0.00425
AMP
Homo sapiens
-
mutant DELTA8
0.0046
AMP
Sus scrofa
30°C, pH 7.5, mutant enzyme F232W
0.00506
AMP
Homo sapiens
-
wild-type liver enzyme
0.0057
AMP
Sus scrofa
30°C, pH 7.5, mutant enzyme F16W
0.00695
AMP
Sus scrofa
pH 7.5, 37°C, recombinant mutant L73A
0.00695
AMP
Sus scrofa
mutant enzyme L73A, pH 7.5, 37°C
0.0071
AMP
Sus scrofa
30°C, pH 7.5, recombinant wild-type enzyme
0.0072
AMP
Sus scrofa
pH 7.5, 37°C, recombinant mutant M248D
0.0072
AMP
Sus scrofa
mutant enzyme M248D, pH 7.5, 37°C
0.00735
AMP
Sus scrofa
pH 7.5, 37°C, recombinant mutant L56A
0.00735
AMP
Sus scrofa
mutant enzyme L56A, pH 7.5, 37°C
0.0075
AMP
Sus scrofa
pH 7.5, 37°C, recombinant wild-type enzyme
0.0075
AMP
Sus scrofa
wild-type enzyme, pH 7.5, 37°C
0.01
AMP
Pisum sativum
-
wild-type
0.0102
AMP
Sus scrofa
30°C, pH 7.5, nonrecombinant enzyme
0.015
AMP
Synechocystis sp.
mutant Y131A, pH 8.0, 28°C
0.0181
AMP
Escherichia coli
22°C, pH 7.5, assay is initiated by the addition of enzyme
0.02
AMP
Rattus norvegicus
-
-
0.02
AMP
Escherichia coli
22°C, pH 7.5, assay mixtures contains 1 mM phosphoenolpyruvate. Enzyme is incubated for 1 h in assay mixture. The reaction is initiated by the addition of Mg2+
0.0214
AMP
Synechocystis sp.
mutant R176A, pH 8.0, 28°C
0.027
AMP
Synechocystis sp.
mutant R178A, pH 8.0, 28°C
0.028
AMP
Synechocystis sp.
mutant K29A, pH 8.0, 28°C
0.034
AMP
Synechocystis sp.
wild-type, pH 8.0, 28°C
0.0486
AMP
Sus scrofa
mutant enzyme Y113A, pH 7.5, 37°C
0.0486 - 0.0553
AMP
Sus scrofa
pH 7.5, 37°C, recombinant mutant Y113A
0.0523 - 0.0685
AMP
Sus scrofa
pH 7.5, 37°C, recombinant mutant K112A
0.0685
AMP
Sus scrofa
mutant enzyme K112A, pH 7.5, 37°C
0.21
AMP
Synechocystis sp.
mutant N213A, pH 8.0, 28°C
0.225
AMP
Synechocystis sp.
mutant D200A, pH 8.0, 28°C
1.23
AMP
Synechocystis sp.
mutant D198H, pH 8.0, 28°C
1.241
AMP
Synechocystis sp.
mutant T102A, pH 8.0, 28°C
2.099
AMP
Synechocystis sp.
mutant K134A, pH 8.0, 28°C
5.81
AMP
Pisum sativum
-
mutant K115Q
15.96
AMP
Pisum sativum
-
mutant Y116F
0.75
ATP
Pyrobaculum calidifontis
pH 8.0, 25°C
0.75
ATP
Pyrobaculum calidifontis
recombinant enzyme, pH 8.0, 60°C
0.00074
Ca2+
Oryctolagus cuniculus
-
native rabbit muscle FBPase
0.00077
Ca2+
Homo sapiens
-
mutant DELTA4
0.00091
Ca2+
Homo sapiens
-
wild-type muscle enzyme
0.00099
Ca2+
Homo sapiens
-
mutant DELTA3
0.00131
Ca2+
Homo sapiens
-
mutant DELTA6
0.00137
Ca2+
Homo sapiens
-
mutant DELTA5
0.00218
Ca2+
Homo sapiens
-
mutant DELTA7
0.00689
Ca2+
Homo sapiens
-
wild-type liver enzyme, biphasic inhibition by Ca2+
0.00731
Ca2+
Homo sapiens
-
mutant DELTA10
0.091
Ca2+
Pelophylax lessonae
-
pH 7.5, 25°C
0.934
Ca2+
Homo sapiens
-
wild-type liver enzyme, biphasic inhibition by Ca2+
2
citrate
Mycobacterium tuberculosis
pH and temperature not specified in the publication
2
citrate
Mycobacterium tuberculosis
versus MtFBPaseII, pH and temperature not specified in the publication
0.00062 - 0.00075
D-fructose 2,6-bisphosphate
Sus scrofa
pH 7.5, 37°C, recombinant mutant M177A
0.0007
D-fructose 2,6-bisphosphate
Sus scrofa
30°C, pH 7.5, mutant enzyme F16W
0.0007
D-fructose 2,6-bisphosphate
Sus scrofa
30°C, pH 7.5, mutant enzyme F89W
0.0009
D-fructose 2,6-bisphosphate
Sus scrofa
30°C, pH 7.5, nonrecombinant enzyme
0.00095
D-fructose 2,6-bisphosphate
Sus scrofa
pH 7.5, 37°C, recombinant mutant Y164A
0.001
D-fructose 2,6-bisphosphate
Sus scrofa
30°C, pH 7.5, recombinant wild-type enzyme
0.0015
D-fructose 2,6-bisphosphate
Sus scrofa
pH 7.5, 37°C, recombinant wild-type enzyme
0.0015
D-fructose 2,6-bisphosphate
Sus scrofa
pH 7.5, 37°C, recombinant mutant K112A
0.0016
D-fructose 2,6-bisphosphate
Sus scrofa
30°C, pH 7.5, mutant enzyme F219W
0.0017 - 0.0018
D-fructose 2,6-bisphosphate
Sus scrofa
pH 7.5, 37°C, recombinant mutant Y113A
0.0019
D-fructose 2,6-bisphosphate
Sus scrofa
30°C, pH 7.5, mutant enzyme F232W
0.00725
D-fructose 2,6-bisphosphate
Sus scrofa
pH 7.5, 37°C, recombinant mutant L73A
0.0075
D-fructose 2,6-bisphosphate
Sus scrofa
pH 7.5, 37°C, recombinant mutant L56A
0.0105
D-fructose 2,6-bisphosphate
Sus scrofa
pH 7.5, 37°C, recombinant mutant M248D
0.002
diethyl (5-[4-amino-1-[(1R,2R)-bicyclo[2.2.1]hept-2-ylamino]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002
diethyl (5-[4-amino-1-[(1R,2R)-bicyclo[2.2.1]hept-2-ylamino]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.004
diethyl (5-[4-amino-1-[3-(thiophen-3-ylmethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.02
diethyl (5-[4-amino-1-[3-(thiophen-3-ylmethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0042
diethyl (5-[4-amino-1-[4-(furan-3-ylmethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.02
diethyl (5-[4-amino-1-[4-(furan-3-ylmethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.007
diethyl (5-[4-amino-1-[4-(trifluoromethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.02
diethyl (5-[4-amino-1-[4-(trifluoromethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.005
diethyl [5-(4-amino-1-benzyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.02
diethyl [5-(4-amino-1-benzyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.00225
diethyl [5-(4-amino-1-ethyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.04
diethyl [5-(4-amino-1-ethyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.006
diethyl [5-(4-amino-1-methyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.02
diethyl [5-(4-amino-1-methyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0011
diethyl [5-(4-amino-1-propyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002
diethyl [5-(4-amino-1-propyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0015
diethyl [5-[4-amino-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.004
diethyl [5-[4-amino-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.00185
diethyl [5-[4-amino-1-(3-hydroxybenzyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.02
diethyl [5-[4-amino-1-(3-hydroxybenzyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0095
diethyl [5-[4-amino-1-(4-tert-butylbenzyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.02
diethyl [5-[4-amino-1-(4-tert-butylbenzyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0025
diethyl [5-[4-amino-1-(biphenyl-4-ylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.02
diethyl [5-[4-amino-1-(biphenyl-4-ylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0008
diethyl [5-[4-amino-1-(cyclobutylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002
diethyl [5-[4-amino-1-(cyclobutylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.00325
diethyl [5-[4-amino-1-(cycloheptylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.02
diethyl [5-[4-amino-1-(cycloheptylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.002
diethyl [5-[4-amino-1-(cyclohexylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0025
diethyl [5-[4-amino-1-(cyclohexylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0015
diethyl [5-[4-amino-1-(cyclopentylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002
diethyl [5-[4-amino-1-(cyclopentylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0008
diethyl [5-[4-amino-1-(cyclopropylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.2
diethyl [5-[4-amino-1-(cyclopropylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.00075
fructose 2,6-bisphosphate
Sus scrofa
mutant enzyme M177A, pH 7.5, 37°C
0.00095
fructose 2,6-bisphosphate
Sus scrofa
mutant enzyme Y164A, pH 7.5, 37°C
0.0015
fructose 2,6-bisphosphate
Sus scrofa
wild-type enzyme, pH 7.5, 37°C
0.0015
fructose 2,6-bisphosphate
Sus scrofa
mutant enzyme K112A, pH 7.5, 37°C
0.0018
fructose 2,6-bisphosphate
Sus scrofa
mutant enzyme Y113A, pH 7.5, 37°C
0.00725
fructose 2,6-bisphosphate
Sus scrofa
mutant enzyme L73A, pH 7.5, 37°C
0.0075
fructose 2,6-bisphosphate
Sus scrofa
mutant enzyme L56A, pH 7.5, 37°C
0.0105
fructose 2,6-bisphosphate
Sus scrofa
mutant enzyme M248D, pH 7.5, 37°C
0.2
Li+
Mycobacterium tuberculosis
-
pH 7.7, 30°C
0.25
Li+
Mycobacterium tuberculosis
pH 8.0, 22°C, recombinant wild-type enzyme
0.28
Li+
Mycobacterium tuberculosis
pH 8.0, 22°C, recombinant mutant T84S
290
Li+
Archaeoglobus fulgidus
pH 8.0, 85°C
15.8
LiCl
Escherichia coli
-
70
LiCl
Escherichia coli
-
3.3
malate
Mycobacterium tuberculosis
pH and temperature not specified in the publication
3.3
malate
Mycobacterium tuberculosis
versus MtFBPaseII, pH and temperature not specified in the publication
3.2
malonate
Mycobacterium tuberculosis
pH and temperature not specified in the publication
3.2
malonate
Mycobacterium tuberculosis
versus MtFBPaseII, pH and temperature not specified in the publication
0.318
N,4-diphenylthiazol-2-amine
Sus scrofa
-
2.5
N,4-diphenylthiazol-2-amine
Sus scrofa
-
0.0025
N-(5-chloro-1,3-benzoxazol-2-yl)naphthalene-2-sulfonamide
Homo sapiens
-
-
0.0025
N-(5-chloro-1,3-benzoxazol-2-yl)naphthalene-2-sulfonamide
Homo sapiens
-
non-competitive
0.0002
N-([4-bromo-6-[(2,2,2-trifluoroethyl)amino]pyridin-2-yl]carbamoyl)-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0037
N-([4-bromo-6-[(2,2,2-trifluoroethyl)amino]pyridin-2-yl]carbamoyl)-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.00008
N-([4-bromo-6-[(methylcarbamoyl)amino]pyridin-2-yl]carbamoyl)-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.001
N-([4-bromo-6-[(methylcarbamoyl)amino]pyridin-2-yl]carbamoyl)-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.00033
N-[(5-bromo-1,3-thiazol-2-yl)carbamoyl]-3-chlorobenzenesulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0058
N-[(5-bromo-1,3-thiazol-2-yl)carbamoyl]-3-chlorobenzenesulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.00013
N-[(6-amino-4-bromopyridin-2-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0015
N-[(6-amino-4-bromopyridin-2-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.0004
N-[(6-amino-4-methoxypyridin-2-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.03
N-[(6-amino-4-methoxypyridin-2-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.00033
N-[(6-bromo-1H-indazol-4-yl)carbamoyl]-3-chlorobenzenesulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0033
N-[(6-bromo-1H-indazol-4-yl)carbamoyl]-3-chlorobenzenesulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.00014
N-[(6-bromo-1H-indazol-4-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0017
N-[(6-bromo-1H-indazol-4-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.00035
N-[(6-bromo-1H-indol-4-yl)carbamoyl]-3-chlorobenzenesulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.005
N-[(6-bromo-1H-indol-4-yl)carbamoyl]-3-chlorobenzenesulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.00082
N-[(7-bromoimidazo[1,2-a]pyridin-5-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.008
N-[(7-bromoimidazo[1,2-a]pyridin-5-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.0018
N-[[6-amino-4-(methylsulfanyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.009
N-[[6-amino-4-(methylsulfanyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.00076
N-[[6-amino-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.006
N-[[6-amino-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.00042
N-[[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-hydroxyethyl)-4-methylthiophene-2-sulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.004
N-[[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-hydroxyethyl)-4-methylthiophene-2-sulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.0006
N-[[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0035
N-[[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
6.4
oxaloacetate
Mycobacterium tuberculosis
pH and temperature not specified in the publication
6.4
oxaloacetate
Mycobacterium tuberculosis
versus MtFBPaseII, pH and temperature not specified in the publication
1.2
phosphate
Escherichia coli
-
3
phosphate
Escherichia coli
-
0.00045
[5-(2-amino-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
Homo sapiens
-
-
0.013
[5-(2-amino-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
Rattus norvegicus
-
-
0.00012
[5-(2-amino-5-isobutyl-1,3-oxazol-4-yl)-2-furyl]phosphonic acid
Homo sapiens
-
-
0.002
[5-(2-amino-5-isobutyl-1,3-oxazol-4-yl)-2-furyl]phosphonic acid
Rattus norvegicus
-
-
0.000014
[5-(2-amino-5-phenyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
Homo sapiens
-
-
0.0005
[5-(2-amino-5-phenyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
Rattus norvegicus
-
-
0.000055
[5-(4-amino-5-bromo-1-cyclopropyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00218
[5-(4-amino-5-bromo-1-cyclopropyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0005
[5-(5-isobutyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
Homo sapiens
-
-
0.0035
[5-(5-isobutyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
Rattus norvegicus
-
-
0.000042
[5-(6-amino-3-phenylpyridin-2-yl)-2-furyl]phosphonic acid
Homo sapiens
-
-
0.0016
[5-(6-amino-3-phenylpyridin-2-yl)-2-furyl]phosphonic acid
Rattus norvegicus
-
-
0.000039
[5-[2-amino-5-(2-methylpropyl)-1,3-selenazol-4-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
-
0.00015
[5-[2-amino-5-(2-methylpropyl)-1,3-selenazol-4-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
-
0.000001
[5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
0.000025
[5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00015
[5-[4-amino-1-(2-ethylbutyl)-5-fluoro-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00085
[5-[4-amino-1-(2-ethylbutyl)-5-fluoro-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.001
[5-[4-amino-5,7-dibromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002
[5-[4-amino-5,7-dibromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.00045
[5-[4-amino-5,7-dichloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002
[5-[4-amino-5,7-dichloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0004
[5-[4-amino-5-bromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002
[5-[4-amino-5-bromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0002
[5-[4-amino-5-chloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002
[5-[4-amino-5-chloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0025
[5-[4-amino-5-ethyl-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.02
[5-[4-amino-5-ethyl-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0001
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00225
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.00009
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-7-phenyl-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0009
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-7-phenyl-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0001
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-7-propyl-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00065
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-7-propyl-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.00085
[5-[4-amino-5-fluoro-1-(pentan-3-yl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00215
[5-[4-amino-5-fluoro-1-(pentan-3-yl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.00008
[5-[4-amino-5-fluoro-7-(2-methoxyethyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00045
[5-[4-amino-5-fluoro-7-(2-methoxyethyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0001
[5-[4-amino-5-fluoro-7-(3-methylbutyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0021
[5-[4-amino-5-fluoro-7-(3-methylbutyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.00018
[5-[4-amino-5-fluoro-7-(4-fluorophenyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0013
[5-[4-amino-5-fluoro-7-(4-fluorophenyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0005
[5-[4-amino-5-hydroxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.02
[5-[4-amino-5-hydroxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0007
[5-[4-amino-5-methoxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002
[5-[4-amino-5-methoxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.003
[5-[4-amino-5-methoxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.02
[5-[4-amino-5-methoxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.000225
[5-[4-amino-6-chloro-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002
[5-[4-amino-6-chloro-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.00021
[5-[4-amino-7-(3,3-dimethylbutyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0016
[5-[4-amino-7-(3,3-dimethylbutyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.00009
[5-[4-amino-7-(4-chlorophenyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002
[5-[4-amino-7-(4-chlorophenyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.00007
[5-[4-amino-7-(6-chlorohexyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0005
[5-[4-amino-7-(6-chlorohexyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0004
[5-[4-amino-7-bromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002
[5-[4-amino-7-bromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.00013
[5-[4-amino-7-bromo-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00209
[5-[4-amino-7-bromo-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0001
[5-[4-amino-7-chloro-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002
[5-[4-amino-7-chloro-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.00006
[5-[4-amino-7-cyclopropyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00035
[5-[4-amino-7-cyclopropyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.00028
[5-[4-amino-7-ethenyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0009
[5-[4-amino-7-ethenyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.000055
[5-[4-amino-7-ethyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00055
[5-[4-amino-7-ethyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.005
[5-[6-amino-9-(2-phenylethyl)-8,9-dihydro-7H-purin-8-yl]-2-furyl]phosphonate
Homo sapiens
-
0.015
[5-[6-amino-9-(2-phenylethyl)-8,9-dihydro-7H-purin-8-yl]-2-furyl]phosphonate
Homo sapiens
-
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drug target
potential drug target against Leishmania parasites
drug target
potential drug target for type 2 diabetes
drug target
the enzyme (FBPase-1) is considered to be a new target for the control of diabetes
drug target
-
the enzyme (FBPase-1) is considered to be a new target for the control of diabetes
-
evolution
-
virtually all archaeal groups as well as the deeply branching bacterial lineages contain the bifunctional D-fructose 1,6-bisphosphate aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity. This enzyme is missing in most other bacteria and in eukaryota. Phylogenetic analysis, overview
evolution
-
virtually all archaeal groups as well as the deeply branching bacterial lineages contain the bifunctional D-fructose 1,6-bisphosphate aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity. This enzyme is missing in most other bacteria and in eukaryota. Phylogenetic analysis, overview
evolution
-
virtually all archaeal groups as well as the deeply branching bacterial lineages contain the bifunctional D-fructose 1,6-bisphosphate aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity. This enzyme is missing inmost other Bacteria and in Eukaryota. Phylogenetic analysis, overview
evolution
YK23 is a member of the histidine phosphatase (phosphoglyceromutase) superfamily. YK23 represents the first family of metal-independent FBPases and a second FBPase family in eukaryotes
evolution
chloroplastic FBPase isoenzymes are widely distributed in photosynthetic organisms, i.e. bacteria, blue-green and green algae, lichens, and plants
evolution
FBPases are homotetrameric enzymes with three different isoforms present in plants, two in chloroplasts (cFBP1 and cFBP2) and one in the cytosol (cyFBP). Only cFBP1 needs to be redox activated in order to be fully active, whilst cFBP2 is not redox regulated and, despite its activity, resists higher oxidant concentrations than cFBP1
evolution
structural comparison of class I versus class II FBPases
evolution
structures of Leishmania fructose-1,6-bisphosphatase (FBPase) reveal species-specific differences in the mechanism of allosteric inhibition of FBPases
evolution
the amino acid sequence of EgFBPaseIII shows low identity (35%) with EgFBPaseI and II, while it shows higher identity of 51-52% with other cytosolic FBPases from plants. EgFBPaseIII has an additional sequence at the N-terminus that other cytosolic FBPases do not possess, this N-terminal region contains no signal peptide or known domain architecture
evolution
the archaeal enzyme belongs to the class V of fructose-1, 6-bisphosphatases. Gene expression of class V FBPase is regulated at the transcription level. The substrate binding residues, including Tyr229, Lys232, and Tyr358, and the residues involved in metal binding, including Asp11, His18, Asp52, Asp53, Gln95, Asp132, Asp233, and Glu357 are completely conserved in all the archaeal FBPases
evolution
Thermosynechococcus vestitus
the FBP/SBPase found in Thermosynechococcus elongatus is a type II FBPase, a member of the larger Li+-sensitive phosphatase superfamily. It shares 80% sequence identity with the Synechocystis sp. PCC 6803 FBP/SBPase
evolution
-
the amino acid sequence of EgFBPaseIII shows low identity (35%) with EgFBPaseI and II, while it shows higher identity of 51-52% with other cytosolic FBPases from plants. EgFBPaseIII has an additional sequence at the N-terminus that other cytosolic FBPases do not possess, this N-terminal region contains no signal peptide or known domain architecture
-
evolution
-
chloroplastic FBPase isoenzymes are widely distributed in photosynthetic organisms, i.e. bacteria, blue-green and green algae, lichens, and plants
-
evolution
-
structural comparison of class I versus class II FBPases
-
evolution
-
the archaeal enzyme belongs to the class V of fructose-1, 6-bisphosphatases. Gene expression of class V FBPase is regulated at the transcription level. The substrate binding residues, including Tyr229, Lys232, and Tyr358, and the residues involved in metal binding, including Asp11, His18, Asp52, Asp53, Gln95, Asp132, Asp233, and Glu357 are completely conserved in all the archaeal FBPases
-
evolution
-
the archaeal enzyme belongs to the class V of fructose-1, 6-bisphosphatases. Gene expression of class V FBPase is regulated at the transcription level. The substrate binding residues, including Tyr229, Lys232, and Tyr358, and the residues involved in metal binding, including Asp11, His18, Asp52, Asp53, Gln95, Asp132, Asp233, and Glu357 are completely conserved in all the archaeal FBPases
-
evolution
-
the archaeal enzyme belongs to the class V of fructose-1, 6-bisphosphatases. Gene expression of class V FBPase is regulated at the transcription level. The substrate binding residues, including Tyr229, Lys232, and Tyr358, and the residues involved in metal binding, including Asp11, His18, Asp52, Asp53, Gln95, Asp132, Asp233, and Glu357 are completely conserved in all the archaeal FBPases
-
malfunction
EgFBPaseI gene suppression by gene silencing markedly decreases photosynthetic activity and inhibits cell growth
malfunction
genetic silencing of enzyme fructose-1,6-bisphosphatase (FBP1) reduces aerobic glycolysis and the malignant potential of breast cancer cells. FBP1 down-regulation enhances the activity of Wnt/b-Catenin pathway and increases the level of its downstream targets, including c-Myc and MMP7
malfunction
homology modeling using the Escherichia coli enzyme structure suggests that the replacement of the critical nucleophile OH- in the Thr84 residue of the wild-type MtFBPase by Ser84 results in subtle alterations of the position and orientation that reduce the catalytic efficiency
malfunction
no significant differences are observed in the production of paramylon in transiently suppressed EgFBPaseIII gene expression cells by RNAi (KD-EgFBPaseIII), but FBPase activity is markedly decreased in KD-EgFBPaseIII cells. Growth of KD-EgFBPaseIII cells is slightly increased compared to control cells
malfunction
overexpression of bifunctional fructose-1,6-bisphosphatase/sedoheptulose-1,7-bisphosphatase (BiBPase) alters the carbon partitioning to extracellular carbohydrate. It induces carbohydrate partitioning which is significantly different from that in the wild-type and more towards extracellular carbohydrate and less towards glycogen. The activities of aldolase and ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) are enhanced by overexpression of BiBPase compared to wild-type, while glucose 6-phosphate dehydrogenase activity is decreased. Overexpression of BiBPase leads to enhanced cell size and photosynthetic O2 evolution. Overexpression of BiBPase in Synechococcus sp. PCC 7002 confers faster growth under elevated [CO2] and light conditions, but not under conditions where the amount of either light or CO2 is limiting
malfunction
two significant mutations in the coding region of the FBPase gene in patients with hypoglycemia link the AMP-binding site to the active site of the enzyme. Individuals with FBPase deficiency exhibit hypoglycemia and metabolic acidosis due to impaired gluconeogenesis. In rare cases, hypoglycemia, an autosomal recessive disorder characterized by insufficient blood glucose levels, is genetically linked to FBPase deficiency in clinical studies. The M177 and Y164 interfacial residues are positioned between the AMP-binding site and active sites and are mutated in humans with hypoglycemia
malfunction
-
no significant differences are observed in the production of paramylon in transiently suppressed EgFBPaseIII gene expression cells by RNAi (KD-EgFBPaseIII), but FBPase activity is markedly decreased in KD-EgFBPaseIII cells. Growth of KD-EgFBPaseIII cells is slightly increased compared to control cells
-
malfunction
-
EgFBPaseI gene suppression by gene silencing markedly decreases photosynthetic activity and inhibits cell growth
-
malfunction
-
homology modeling using the Escherichia coli enzyme structure suggests that the replacement of the critical nucleophile OH- in the Thr84 residue of the wild-type MtFBPase by Ser84 results in subtle alterations of the position and orientation that reduce the catalytic efficiency
-
malfunction
-
homology modeling using the Escherichia coli enzyme structure suggests that the replacement of the critical nucleophile OH- in the Thr84 residue of the wild-type MtFBPase by Ser84 results in subtle alterations of the position and orientation that reduce the catalytic efficiency
-
malfunction
-
overexpression of bifunctional fructose-1,6-bisphosphatase/sedoheptulose-1,7-bisphosphatase (BiBPase) alters the carbon partitioning to extracellular carbohydrate. It induces carbohydrate partitioning which is significantly different from that in the wild-type and more towards extracellular carbohydrate and less towards glycogen. The activities of aldolase and ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) are enhanced by overexpression of BiBPase compared to wild-type, while glucose 6-phosphate dehydrogenase activity is decreased. Overexpression of BiBPase leads to enhanced cell size and photosynthetic O2 evolution. Overexpression of BiBPase in Synechococcus sp. PCC 7002 confers faster growth under elevated [CO2] and light conditions, but not under conditions where the amount of either light or CO2 is limiting
-
malfunction
-
overexpression of bifunctional fructose-1,6-bisphosphatase/sedoheptulose-1,7-bisphosphatase (BiBPase) alters the carbon partitioning to extracellular carbohydrate. It induces carbohydrate partitioning which is significantly different from that in the wild-type and more towards extracellular carbohydrate and less towards glycogen. The activities of aldolase and ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) are enhanced by overexpression of BiBPase compared to wild-type, while glucose 6-phosphate dehydrogenase activity is decreased. Overexpression of BiBPase leads to enhanced cell size and photosynthetic O2 evolution. Overexpression of BiBPase in Synechococcus sp. PCC 7002 confers faster growth under elevated [CO2] and light conditions, but not under conditions where the amount of either light or CO2 is limiting
-
metabolism
Calvin cycle enzyme
metabolism
-
fructose 1,6-bisphosphatase II is a key gluconeogenic enzyme
metabolism
-
fructose bisphosphatase is the key enzyme of gluconeogenesis
metabolism
-
fructose bisphosphatase is the key enzyme of gluconeogenesis
metabolism
-
fructose-1,6-bisphosphatase is a key enzyme in gluconeogenesis
metabolism
-
fructose-1,6-bisphosphatase is secreted into the periplasm during prolonged glucose starvation and is internalized into vacuole import and degradation vesicles/endosomes following glucose re-feeding. Fructose-1,6-bisphosphatase does not contain signal sequences required for the classical secretory and endocytic pathways, the secretion and internalization are mediated via the non-classical pathways and involves protein Vps34, which is involved in multiple protein trafficking events
metabolism
gluconeogenic enzyme
metabolism
-
effects of the enzyme activity on the flux balance analyses of Kluyveromyces marxianus grown on glucose and xylose as respective carbon sources (e.g. cofactor balances and sugar uptake fluxes), simulations, detailed overview. Simulation of anaerobic conditions
metabolism
enzyme FBPase is a key rate-controlling enzyme in the gluconeogenic pathway
metabolism
enzyme FBPase is a key rate-controlling enzyme in the gluconeogenic pathway
metabolism
fructose-1,6-bisphosphatase (FBPase) catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate and is a key enzyme of gluconeogenesis and glyconeogenesis
metabolism
fructose-1,6-bisphosphatase (FBPase) is the key enzyme in the Calvin-Benson cycle (CBC). The enzyme is involved in redox regulation in chloroplasts, model of the redox regulation, overview
metabolism
the chloroplastic fructose-1,6-bisphosphatase (FBPase) is a late-limiting enzyme in the Calvin cycle
metabolism
the enzyme fructose 1,6-bisphosphatase takes part in the Calvin cycle, but unlike the situation in higher plants, FBPase probably does not catalyze a rate-limiting step in the Chlamydomonas reinhardtii Calvin cycle, since under photoautotrophic growth conditions and/or with elevated CO2 levels, an elevation in FBPase activity has a negative effect overall on growth rate and biomass production
metabolism
the enzyme is part of the carbohydrate metabolism in the carnivorous fish species. Fructose-1,6-bisphosphatase (FBPase) plays a crucial role in glucose metabolism, together with glucokinase. Feeding with dietary carbohydrates causes no significant differences in FBPase activity and mRNA expression in the glucose as well as dextrin group, while both hepatic glucokinase activity and mRNA expression are highly induced in turbot. The increased hepatic glucokinase activity and gene expression indicates that the first step of glycolysis is activated in turbot by dietary carbohydrates
metabolism
essential enzyme for pathogenesis
metabolism
key enzyme in gluconeogenesis and position branch point of carbon partitioning between paramylon and wax ester biosynthesis. The activity of the enzyme (EgFBPaseIII) is not regulated by AMP or reversible redox modulation
metabolism
key enzyme of the gluconeogenic pathway
metabolism
metabolic conditions modulate aldolase B and FBPase-1 activity at the cellular level through the regulation of their interaction, suggesting that their association confers a catalytic advantage for both enzymes
metabolism
one of the key enzymes in gluconeogenesis
metabolism
overexpression of bifunctional fructose-1,6-bisphosphatase/sedoheptulose-1,7-bisphosphatase leads to enhanced photosynthesis and global reprogramming of carbon metabolism
metabolism
-
regulatory enzyme in the gluconeogenesis pathway
metabolism
-
simulation study of yeast metabolism, that investigates the complex interplay between the cofactors ATP, NAD+ and NADP+, in particular, how they may affect the possible roles of fructose-1,6-bisphosphatase, the pentose phosphate pathway, glycerol production and the pyruvate dehydrogenase bypass. Using flux balance analysis, it is found that the potential role of fructose-1,6-bisphosphatase is highly dependent on the cofactor specificity of the oxidative pentose phosphate pathway and on the carbon source. The fructose-1,6-bisphosphatase/phosphofructokinase substrate cycle and its regulation probably plays a key role in energy homeostasis, even in yeasts under selected conditions, which could determine phenotype switching
metabolism
the enzyme (EgFBPaseI) is critical for the Calvin cycle in Euglena chloroplasts in order to maintain normal cell growth under photoautotrophic conditions
metabolism
the enzyme (FBP1) is rate-limiting in gluconeogenes. Its downregulation enhances the activity of Wnt/beta-catenin pathway and increases the level of its downstream targets, including c-Myc and MMP7. Elevated fructose-1,6-bisphosphatase is a critical modulator in breast cancer progression by altering glucose metabolism and the activity of Wnt/beta-Catenin pathway. The enzyme is a tumor suppressor that is frequently down-regulated in cancers, especially breast cancer. Lower FBP1 expression is associated with poor clinical outcome. Up-regulated FBP1 predicts a good prognosis in breast cancer
metabolism
the enzyme belongs to the Calvin-Benson cycle
metabolism
-
the increased fructose 1,6-bisphosphatase activity in nodules of RIL115 positively correlates with higher use efficiency of both the rhizobial symbiosis (23%) and P for symbiotic nitrogen fixation (14% calculated as the ratio of N2 fixed per nodule total P content)
metabolism
-
key enzyme in gluconeogenesis and position branch point of carbon partitioning between paramylon and wax ester biosynthesis. The activity of the enzyme (EgFBPaseIII) is not regulated by AMP or reversible redox modulation
-
metabolism
-
the chloroplastic fructose-1,6-bisphosphatase (FBPase) is a late-limiting enzyme in the Calvin cycle
-
metabolism
-
the enzyme (EgFBPaseI) is critical for the Calvin cycle in Euglena chloroplasts in order to maintain normal cell growth under photoautotrophic conditions
-
metabolism
-
effects of the enzyme activity on the flux balance analyses of Kluyveromyces marxianus grown on glucose and xylose as respective carbon sources (e.g. cofactor balances and sugar uptake fluxes), simulations, detailed overview. Simulation of anaerobic conditions
-
metabolism
-
simulation study of yeast metabolism, that investigates the complex interplay between the cofactors ATP, NAD+ and NADP+, in particular, how they may affect the possible roles of fructose-1,6-bisphosphatase, the pentose phosphate pathway, glycerol production and the pyruvate dehydrogenase bypass. Using flux balance analysis, it is found that the potential role of fructose-1,6-bisphosphatase is highly dependent on the cofactor specificity of the oxidative pentose phosphate pathway and on the carbon source. The fructose-1,6-bisphosphatase/phosphofructokinase substrate cycle and its regulation probably plays a key role in energy homeostasis, even in yeasts under selected conditions, which could determine phenotype switching
-
metabolism
-
fructose-1,6-bisphosphatase is a key enzyme in gluconeogenesis
-
metabolism
-
fructose 1,6-bisphosphatase II is a key gluconeogenic enzyme
-
metabolism
-
essential enzyme for pathogenesis
-
metabolism
-
essential enzyme for pathogenesis
-
metabolism
-
metabolic conditions modulate aldolase B and FBPase-1 activity at the cellular level through the regulation of their interaction, suggesting that their association confers a catalytic advantage for both enzymes
-
metabolism
-
overexpression of bifunctional fructose-1,6-bisphosphatase/sedoheptulose-1,7-bisphosphatase leads to enhanced photosynthesis and global reprogramming of carbon metabolism
-
metabolism
-
key enzyme of the gluconeogenic pathway
-
metabolism
-
overexpression of bifunctional fructose-1,6-bisphosphatase/sedoheptulose-1,7-bisphosphatase leads to enhanced photosynthesis and global reprogramming of carbon metabolism
-
metabolism
-
key enzyme of the gluconeogenic pathway
-
metabolism
-
Calvin cycle enzyme
-
metabolism
-
the enzyme fructose 1,6-bisphosphatase takes part in the Calvin cycle, but unlike the situation in higher plants, FBPase probably does not catalyze a rate-limiting step in the Chlamydomonas reinhardtii Calvin cycle, since under photoautotrophic growth conditions and/or with elevated CO2 levels, an elevation in FBPase activity has a negative effect overall on growth rate and biomass production
-
metabolism
-
key enzyme of the gluconeogenic pathway
-
physiological function
fructose-1,6-bisphosphatase is a key enzyme of gluconeogenesis and photosynthetic CO2 fixation, catalyzes the hydrolysis of fructose 1,6-bisphosphate to produce fructose 6-phosphate, an important precursor in various biosynthetic pathways
physiological function
-
the enzyme plays a regulatory role in gluconeogenesis in the retina. FBPase, in addition to its gluconeogenic role, participates in the protection of the retina against reactive oxygen species, it is also involved in non-enzymatic nuclear processes
physiological function
-
the enzyme's bifunctionality ensures that heat-labile triosephosphates are quickly removed and trapped in stabie D-fructose 6-phosphate, rendering gluconeogenesis unidirectional
physiological function
-
the enzyme's bifunctionality ensures that heat-labile triosephosphates are quickly removed and trapped in stable D-fructose 6-phosphate, rendering gluconeogenesis unidirectional
physiological function
-
the enzyme's bifunctionality ensures that heat-labile triosephosphates are quickly removed and trapped in stable D-fructose 6-phosphate, rendering gluconeogenesis unidirectional
physiological function
-
the enzyme is involved in glycogen catabolism
physiological function
a fructose bisphosphatase-negative Corynebacterium glutamicum mutant can be phenotypically complemented with both the chromosome-encoded and the plasmid-encoded isoforms from Bacillus methanolicus
physiological function
compared with negative littermates, liver-specific FBPase transgenic mice have 50% less adiposity and eat 15% less food but do not have altered energy expenditure. The reduced food consumption is associated with increased circulating leptin and cholecystokinin, elevated fatty acid oxidation, and 3-beta-hydroxybutyrate ketone levels, and reduced appetite-stimulating neuropeptides, neuropeptide Y and Agouti-related peptide
physiological function
-
heterologous expression in Corynebacterium glutamicum leads to a recombinant protein that is insensitive to fructose 1-phosphate and fructose 2,6-bisphosphate, whereas the homologous fructose-1,6-bisphosphatase is inhibited by fructose 1-phosphate and fructose 2,6-bisphosphate. The relative enzyme activity of heterologous fructose-1,6-bisphosphatase is 90.8% and 89.1% during supplement with 3 mM fructose 1-phosphate and fructose 2,6-bisphosphate, respectively. Phosphoenolpyruvate is an activator of heterologous fructose-1,6-bisphosphatase, whereas the homologous fructose-1,6-bisphosphatase is very sensitive to phosphoenolpyruvate. Overexpression of the heterologous fructose 1,6-bisphosphatase in wild-type Corynebacterium glutamicum has no effect on L-lysine production, but fructose-1,6-bisphosphatase activities are increased 9- to 13fold. Overexpression increases L-lysine production in Corynebacterim glutamicum lysC(T311I) by 57.3% on fructose, 48.7% on sucrose, and 43% on glucose. The dry cell weight and maximal specific growth rate are increased by overexpression of heterologous fructose 1,6-bisphosphatase
physiological function
the quaternary structure of isoform FBP2 plays a crucial role in the binding binds to mitochondria where it interacts with proteins involved in regulation of energy homeostasis interaction. The AMP-driven transition of the FBP2 subunit arrangement from active to inactive precludes its association with the mitochondria. Truncation of the evolutionarily conserved N-terminal residues of FBP2 results in a loss of its mitochondria-protective functions
physiological function
Thermosynechococcus vestitus
bifunctional enzyme FBP/SBPase is unique in that it catalyses two separate reactions in the Calvin cycle, both of which are catalysed by separate enzymes in plants. The reactions catalysed by FBP/SBPase are important for Calvin cycle flux, as indicated by their high predicted metabolic control coefficients
physiological function
class II fructose-1,6-bisphosphatase enzyme in Mycobacterium tuberculosis is an essential enzyme for pathogenesis
physiological function
cytosolic fructose-1,6-bisphosphatase (FBPase) appears to be a key enzyme in gluconeogenesis and position branch point of carbon partitioning between paramylon and wax ester biosynthesis. Euglena gracilis accumulates the storage polysaccharide paramylon, a beta-1,3-glucan, under aerobic conditions. Under anaerobic conditions, the cells degrade paramylon and synthesize wax esters. The activity of EgFBPaseIII is not regulated by AMP or reversible redox modulation
physiological function
enzyme FBPase is a key rate-controlling enzyme in the gluconeogenic pathway. FBPase activity is regulated synergistically by the allosteric inhibitors AMP and fructose-2,6-bisphosphate (F2,6-BP). FBPase functions in the degradation of fructose-1,6-bisphosphate (FBP), which hydrolyzes to fructose-6-phosphate (F6P) and phosphate
physiological function
enzyme FBPase is a key rate-controlling enzyme in the gluconeogenic pathway. FBPase activity is regulated synergistically by the allosteric inhibitors AMP and fructose-2,6-bisphosphate. FBPase functions in the degradation of fructose-1,6-bisphosphate, which hydrolyzes to fructose-6-phosphate and phosphate
physiological function
expression of enzyme in Euglena gracilis cells to enhance its photosynthetic activity. The cell volume of the transgenic cell line is significantly larger than that of wild-type cells under normal growth conditions and the photosynthetic activity is significantly higher than that of wild type under high light and high CO2, resulting in enhanced biomass production. The accumulation of paramylon is increased. Transgenic cell lines grown under high light and high CO2 and placed on anaerobiosis show approximately 13- to 100fold higher productivity of wax esters than in wild-type cells
physiological function
fructose 1,6-bisphosphatase (FBPase) is a major control point in gluconeogenesis, catalyzing the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate and phosphate. This step in gluconeogenesis is synergistically downregulated by fructose 2,6-bisphosphate and AMP, which bind to the active site and an allosteric site of FBPase, respectively
physiological function
fructose-1,6-bisphophatase catalyzes the breakdown of fructose 1,6-bisphosphate to fructose 6-phosphate and phosphate. Two FBPase isoenzymes are identified in photosynthetic eukaryotic cells: a cytosolic form, a key enzyme in gluconeogenesis, and a chloroplastic form, a rate-limiting enzyme involved in the Calvin cycle
physiological function
fructose-1,6-bisphosphatase (FBP1), the rate-limiting enzyme in gluconeogenesis, is a tumor suppressor, especially of breast cancer. The enzyme is commonly upregulated in tumor tissues compared with non-tumor tissues regardless of histological type, and lower FBP1 expression is associated with poor clinical outcome. Genetic silencing of FBP1 reduces aerobic glycolysis and the malignant potential of breast cancer cells. Elevated FBP1 is a critical modulator in breast cancer progression by altering glucose metabolism and the activity of Wnt/ beta-catenin pathway. Mechanism by which FBP1 inhibits tumor progression in breast cancer, overview. The inhibitory effect of FBP1 in glycolysis might be mediated by downregulation of c-Myc
physiological function
fructose-1,6-bisphosphatase (FBPase) plays a crucial role in glucose metabolism, together with glucokinase
physiological function
fructose-1,6-bisphosphatase is a highly regulated key enzyme in gluconeogenesis and glyconeogenesis (glycogen synthesis from gluconeogenic precursors). The enzyme catalyses the hydrolysis of fructose-1,6-bisphosphate to fructose 6-phosphate and phosphate in the presence of divalent metal cations. In vitro protein-protein interaction analysis between liver fructose 1,6-bisphosphate aldolase B and liver FBPase-1 shows a specific and regulable interaction between them, whereas aldolase A (muscle isozyme) and FBPase-1 show no interaction, by real-time interaction analysis by surface plasmon resonance. The interaction between aldolase B and FBPase-1 is specific and reversible. The affinity of the aldolase B and FBPase-1 complex is modulated by intermediate metabolites, but only in the presence of K+. A decreased association constant is observed in the presence of adenosine monophosphate, fructose-2,6-bisphosphate, fructose-6-phosphate and inhibitory concentrations of fructose-1,6-bisphosphate. Conversely, the association constant of the complex increases in the presence of dihydroxyacetone phosphate (DHAP) and non-inhibitory concentrations of fructose-1,6-bisphosphate
physiological function
overexpression of BiBPase enhances growth, cell size, and photosynthetic O2 evolution, and coordinately upregulates enzymes in the Calvin Benson cycle including RuBisCO and fructose-1,6-bisphosphate aldolase. Overexpression downregulates enzymes in respiratory carbon metabolism including glucose-6-phosphate dehydrogenase. The content of glycogen is significantly reduced while the soluble carbohydrate content is increased
physiological function
the Calvin-Benson cycle (CBC) fructose-1,6-bisphosphatase (FBPase) isoform is well known to be redox activated by thioredoxin f through the reduction of a disulfide bridge involving Cys153 and Cys173. cFBP1 needs to be redox activated in order to be fully active
physiological function
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the enzyme contributes to phosphate use efficiency (PUE) under symbiotic nitrogen fixation (SNF) in Phaseolus vulgaris, expression of a phosphate-starvation inducible fructose-1,6-bisphosphatase gene in common bean nodules correlates with phosphorus use efficiency. Two contrasting recombinant inbred lines (RILs) of Phaseolus vulgaris, namely RILs 115 (phosphate-efficient) and 147 (phosphate-inefficient), that are grown under sufficient versus deficient phosphate supply. Under phosphate deficiency, higher FBPase transcript fluorescence is found in the inner cortex as compared to the infected zone of RIL115. In addition, both the specific FBPase and total APase enzyme activities significantly increase in both RILs, but to a more significant extent in RIL115 as compared to RIL147. Furthermore, the increased FBPase activity in nodules of RIL115 positively correlates with higher use efficiency of both the rhizobial symbiosis (23%) and phosphate for symbiotic nitrogen fixation (14% calculated as the ratio of N2 fixed per nodule total phosphate content). The abundant tissue-specific localized FBPase transcript along with induced enzymatic activity provides evidence of a specific tolerance mechanism where N2-fixing nodules overexpress under phosphate-deficiency conditions
physiological function
the physiological role of muscle FBPase goes beyond its enzymatic function, as this isozyme is localized inside cell nuclei and is shown to interact with mitochondria, where it is involved in regulation of the cell cycle. The behaviour of the muscle isozyme differs greatly from the liver isozyme
physiological function
the enzyme regulates the intracellular balance of NAD(H) and NADP(H)
physiological function
key enzyme in hepatic gluconeogenesis pathway
physiological function
key regulator of gluconeogenesis
physiological function
overexpression of fructose 1,6-bisphosphatase has a detrimental effect on growth
physiological function
-
the enzyme is involved in the Calvin cycle
physiological function
-
a fructose bisphosphatase-negative Corynebacterium glutamicum mutant can be phenotypically complemented with both the chromosome-encoded and the plasmid-encoded isoforms from Bacillus methanolicus
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physiological function
-
cytosolic fructose-1,6-bisphosphatase (FBPase) appears to be a key enzyme in gluconeogenesis and position branch point of carbon partitioning between paramylon and wax ester biosynthesis. Euglena gracilis accumulates the storage polysaccharide paramylon, a beta-1,3-glucan, under aerobic conditions. Under anaerobic conditions, the cells degrade paramylon and synthesize wax esters. The activity of EgFBPaseIII is not regulated by AMP or reversible redox modulation
-
physiological function
-
fructose-1,6-bisphophatase catalyzes the breakdown of fructose 1,6-bisphosphate to fructose 6-phosphate and phosphate. Two FBPase isoenzymes are identified in photosynthetic eukaryotic cells: a cytosolic form, a key enzyme in gluconeogenesis, and a chloroplastic form, a rate-limiting enzyme involved in the Calvin cycle
-
physiological function
-
the enzyme regulates the intracellular balance of NAD(H) and NADP(H)
-
physiological function
-
class II fructose-1,6-bisphosphatase enzyme in Mycobacterium tuberculosis is an essential enzyme for pathogenesis
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physiological function
-
class II fructose-1,6-bisphosphatase enzyme in Mycobacterium tuberculosis is an essential enzyme for pathogenesis
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physiological function
-
fructose-1,6-bisphosphatase is a highly regulated key enzyme in gluconeogenesis and glyconeogenesis (glycogen synthesis from gluconeogenic precursors). The enzyme catalyses the hydrolysis of fructose-1,6-bisphosphate to fructose 6-phosphate and phosphate in the presence of divalent metal cations. In vitro protein-protein interaction analysis between liver fructose 1,6-bisphosphate aldolase B and liver FBPase-1 shows a specific and regulable interaction between them, whereas aldolase A (muscle isozyme) and FBPase-1 show no interaction, by real-time interaction analysis by surface plasmon resonance. The interaction between aldolase B and FBPase-1 is specific and reversible. The affinity of the aldolase B and FBPase-1 complex is modulated by intermediate metabolites, but only in the presence of K+. A decreased association constant is observed in the presence of adenosine monophosphate, fructose-2,6-bisphosphate, fructose-6-phosphate and inhibitory concentrations of fructose-1,6-bisphosphate. Conversely, the association constant of the complex increases in the presence of dihydroxyacetone phosphate (DHAP) and non-inhibitory concentrations of fructose-1,6-bisphosphate
-
physiological function
-
expression of enzyme in Euglena gracilis cells to enhance its photosynthetic activity. The cell volume of the transgenic cell line is significantly larger than that of wild-type cells under normal growth conditions and the photosynthetic activity is significantly higher than that of wild type under high light and high CO2, resulting in enhanced biomass production. The accumulation of paramylon is increased. Transgenic cell lines grown under high light and high CO2 and placed on anaerobiosis show approximately 13- to 100fold higher productivity of wax esters than in wild-type cells
-
physiological function
-
overexpression of fructose 1,6-bisphosphatase has a detrimental effect on growth
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additional information
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active site structures, overview
additional information
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active site structures, overview
additional information
Thermosynechococcus vestitus
active-site residue are Asp33, Glu57, Glu100, Thr102, Tyr131, Lys134, Arg176, Arg178, Asp198, Asp200, and Glu225
additional information
cytosolic EgFBPaseIII is identical to the neutral FBPase
additional information
-
cytosolic EgFBPaseIII is identical to the neutral FBPase
additional information
redox pattern displayed by cFBP1, overview
additional information
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redox pattern displayed by cFBP1, overview
additional information
sequence comparisons of human and porcine FBPase 1, overview. Residue L56 coordinates the (4-[3-(6,7-diethoxy-quinazolin-4-ylamino)-phenyl]-thiazol-2-yl)-methanol (PFE) inhibitor ligand, as does residue L73, both of which exhibit hydrophobic interactions with the ligand in the PFE-binding site. In addition, L73 and L56 are part of a network that leads from the allosteric binding site to the active site of the enzyme. Residue M248 is positioned near the triad of acidic residues co-ordinating manganese and is found in the active site to co-ordinate D-fructose 6-phosphate
additional information
sequence comparisons of human and porcine FBPase 1, overview. The M177 and Y164 interfacial residues are positioned between the AMP-binding site and active sites
additional information
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sequence comparisons of human and porcine FBPase 1, overview. The M177 and Y164 interfacial residues are positioned between the AMP-binding site and active sites
additional information
the active site of enzyme Pcal_0111 contains a lysine residue which makes Schiff base with carbonyl group of the substrate
additional information
the apoform of enzyme LmFBPase is a homotetramer in which the dimer of dimers adopts a planar conformation with disordered dynamic loops. The structure of LmFBPase, complexed with manganese and the catalytic product phosphate, shows the dynamic loops locked into the active sites. The dynamic loop (residues 52-71), which has been shown to be catalytically important in mammalian FBPases, is in a similar position in LmFBPase but shows functionally important sequence differences and has two insertions (Tyr57 and Gln61) compared with mammalian and bacterial sequences. Enzyme structure analysis and structure-function relationship, modeling, overview. Conformational variability of the FBPase active site
additional information
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the apoform of enzyme LmFBPase is a homotetramer in which the dimer of dimers adopts a planar conformation with disordered dynamic loops. The structure of LmFBPase, complexed with manganese and the catalytic product phosphate, shows the dynamic loops locked into the active sites. The dynamic loop (residues 52-71), which has been shown to be catalytically important in mammalian FBPases, is in a similar position in LmFBPase but shows functionally important sequence differences and has two insertions (Tyr57 and Gln61) compared with mammalian and bacterial sequences. Enzyme structure analysis and structure-function relationship, modeling, overview. Conformational variability of the FBPase active site
additional information
-
the FBP active site works by stabilizing the FBPase, and the allosteric site impairs the activity of FBPase through its binding of a nonsubstrate molecule. Competitive inhibition of AMP, fructose 1,6-bisphosphate, or fructose 6-phosphate binding to FBPase with fluorescent AMP analogue, 2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate (TNP-AMP)-binding FBPase
additional information
the transition from the inactive, AMP-associated T state towards the active R state involves a reversible refolding of a key helix that is part of the allosteric centre of muscle FBPase
additional information
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the transition from the inactive, AMP-associated T state towards the active R state involves a reversible refolding of a key helix that is part of the allosteric centre of muscle FBPase
additional information
Thr84 in MtFBPaseII protein (Thr90 in Escherichia coli) is a conserved residue in the active site as shown in other FBPases
additional information
-
cytosolic EgFBPaseIII is identical to the neutral FBPase
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additional information
-
Thr84 in MtFBPaseII protein (Thr90 in Escherichia coli) is a conserved residue in the active site as shown in other FBPases
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additional information
-
Thr84 in MtFBPaseII protein (Thr90 in Escherichia coli) is a conserved residue in the active site as shown in other FBPases
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additional information
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the active site of enzyme Pcal_0111 contains a lysine residue which makes Schiff base with carbonyl group of the substrate
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additional information
-
the active site of enzyme Pcal_0111 contains a lysine residue which makes Schiff base with carbonyl group of the substrate
-
additional information
-
the active site of enzyme Pcal_0111 contains a lysine residue which makes Schiff base with carbonyl group of the substrate
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C157S
-
slightly more active than wild type enzyme
C157S/C174S
-
activity remains unchanged
C174S
-
mildly less active than wild type enzyme
C174S/C179S
-
slightly more active than wild type enzyme
C174S/C307S
-
activity remains unchanged
C179S
-
slightly more active than wild type enzyme
C307S
-
activity remains unchanged
C53S
-
mildly less active than wild type enzyme
C53S/C174S
-
mildly less active than wild type enzyme
C96S
-
slightly more active than wild type enzyme
D186A
Km (mM) (D-fructose 1,6-bisphosphate): 0.2 (wild-type: 0.07 mM), kcat (1/sec)(D-fructose 1,6-bisphosphate): 1.2 (wild-type: 5.7/sec)
E59A
Km (mM) (D-fructose 1,6-bisphosphate): 0.1 (wild-type: 0.07 mM), kcat (1/sec)(D-fructose 1,6-bisphosphate): 1.1 (wild-type: 5.7/sec)
K239A
Km (mM) (D-fructose 1,6-bisphosphate): 0.1 (wild-type: 0.07 mM), kcat (1/sec)(D-fructose 1,6-bisphosphate): 7.5 (wild-type: 5.7/sec)
K29A
Km (mM) (D-fructose 1,6-bisphosphate): 0.06 (wild-type: 0.07 mM), kcat (1/sec)(D-fructose 1,6-bisphosphate): 14 (wild-type: 5.7/sec)
L54A
-
enzymic activity similar to wild-type, but much less sensitive to inhibition by AMP. Crystallization data in presence of AMP
R235A
Km (mM) (D-fructose 1,6-bisphosphate): 0.2 (wild-type: 0.07 mM), kcat (1/sec)(D-fructose 1,6-bisphosphate): 5.4 (wild-type: 5.7/sec)
Delta1
-
deletion of the first and the first two N-terminal amino acids of FBPase affects neither the kinetic properties of the enzyme nor its association with aldolase
DELTA10
-
deletion of the first 10 amino acids: affinity to aldolase is significantly reduced, cooperativitiy of Mg2+ activation is abolished and results in biphasic inhibition of the enzyme by AMP. Truncation lowers affinity of muscle FBPase to aldolase about 14times, making it resemble the liver isozyme, Km (D-fructose 1,6-bisphosphate) similar to wild-type
DELTA2
-
deletion of the first and the first two N-terminal amino acids of FBPase affects neither the kinetic properties of the enzyme nor its association with aldolase
DELTA3
-
deletion of the first 3 amino acids: kinetic properties similar to wild-type, affinity to aldolase is significantly reduced, Km (D-fructose 1,6-bisphosphate) similar to wild-type
DELTA4
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deletion of the first 4 amino acids: kinetic properties similar to wild-type, affinity to aldolase is significantly reduced, mutant shows a lower sensitivity to inhibition by AMP and a little weaker activation by Mg2+, Km (D-fructose 1,6-bisphosphate) similar to wild-type
DELTA5
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deletion of the first 5 amino acids: mutant is significantly weaker inhibited by AMP than wild-tpye, affinity to aldolase is significantly reduced, kcat and activation by Mg2+ are significantly reduced, Km (D-fructose 1,6-bisphosphate) similar to wild-type
DELTA6
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deletion of the first 6 amino acids: mutant is significantly weaker inhibited by AMP than wild-tpye, affinity to aldolase is significantly reduced, kcat and activation by Mg2+ are significantly reduced, Km (D-fructose 1,6-bisphosphate) similar to wild-type
DELTA7
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deletion of the first 7 amino acids: mutant is significantly weaker inhibited by AMP than wild-tpye, affinity to aldolase is significantly reduced, kcat and activation by Mg2+ are significantly reduced, Km (D-fructose 1,6-bisphosphate) similar to wild-type
DELTA8
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deletion of the first 8 amino acids: mutant is significantly weaker inhibited by AMP than wild-tpye, affinity to aldolase is significantly reduced, kcat significantly reduced, Km (D-fructose 1,6-bisphosphate) similar to wild-type
E20K
liver enzyme, mutation towards the muscle enzyme
E20K/M177T/C179Q
liver enzyme, mutation towards the muscle enzyme
K203E
-
mutation results in a noticeable drop in the amount of cells having nuclear FBPase
K204E
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mutation results in a noticeable drop in the amount of cells having nuclear FBPase
K205E
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mutation results in a noticeable drop in the amount of cells having nuclear FBPase
K207E
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mutation results in a noticeable drop in the amount of cells having nuclear FBPase
K20E
muscle enzyme, mutation towards the liver enzyme
K20E/T177M/Q179C
muscle enzyme, mutation towards the liver enzyme
M177T/C179Q
liver enzyme, mutation towards the muscle enzyme
Q32R
conentration of AMP required for 50% inhibition of the Q32R mutant is increased 19fold, and the cooperativity of both AMP and Mg2+ is abolished or decreased. The mutation affects the conformations of both N-terminal residues and the dynamic loop 5272
T177M/Q179C
muscle enzyme, mutation towards the liver enzyme
H20A
-
the mutant shows reduced activity compared to the wild type enzyme
H20N
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the mutant shows reduced activity compared to the wild type enzyme
H20Q
-
the mutant shows reduced activity compared to the wild type enzyme
K76A
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the mutant shows reduced activity compared to the wild type enzyme
T16P
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the mutant shows reduced activity compared to the wild type enzyme
D40N
-
almost complete loss of both inositol monophosphatase and fructose 1,6-bisphosphatase activity
D94N
-
almost complete loss of both inositol monophosphatase and fructose 1,6-bisphosphatase activity
L71A
-
no loss of either of the activities, activity toward inositol is more resisitant to inhibition by calcium than wild-type
D40N
-
almost complete loss of both inositol monophosphatase and fructose 1,6-bisphosphatase activity
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L71A
-
no loss of either of the activities, activity toward inositol is more resisitant to inhibition by calcium than wild-type
-
D221A
loss of 60-70% of activity for both FBPase and IMPase activities
G94A/T95A
mutations partially restore the IMPase activity compared to the single mutants
T95A
about 60% loss of both FBPase and IMPase activities
T95S
about 35% loss of both FBPase and IMPase activities
W220A
loss of 60-70% of activity for both FBPase and IMPase activities
W220A/D221A
mutations reduces both FBPase and IMPase activity drastically
E69Q
-
mutation of E69Q results in a 500fold increase of muscle isozyme I0.5 versus Ca2+
C153S
site-directed mutagenesis
C173S/C178S
site-directed mutagenesis
K115Q
-
Km (D-fructose 1,6-bisphosphate) and Ki (D-fructose 2,6-bisphosphate) comparable to wild-type, IC50 (AMP): 5.8 mM
Y116Q
-
Km (D-fructose 1,6-bisphosphate) and Ki (D-fructose 2,6-bisphosphate) comparable to wild-type, IC50 (AMP): 15.9 mM
D233N
mutant protein is impaired in both aldolase and phosphatase activity
E357Q
mutation abolishes phosphatase activity, no effect on aldolase activity
K232R
mutation abolishes aldolase activity, phosphatase activity is enhanced
Y229F
mutation abolishes aldolase activity, phosphatase activity is slightly reduced
Y358F
mutation abolishes phosphatase activity, no effect on aldolase activity
E99A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
H13A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
H178A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
H244A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
H268A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
R181A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
R69A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
S11A
-
properties are closely similar compared to wild type enzyme
S11D
-
properties are closely similar compared to wild type enzyme
S19A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
S65A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
W131A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
Y24A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
G20D
-
kcat for fructose 1,6-bisphosphate is 1.62fold lower than wild-type enzyme, Km-value for fructose 1,6-diphosphate is 1.86fold higherr than wild-type enzyme
T23I
-
kcat for fructose 1,6-bisphosphate is 1.2fold lower than wild-type enzyme, Km-value for fructose 1,6-diphosphate is 1.3fold lower than wild-type enzyme
T91I
-
kcat for fructose 1,6-bisphosphate is 1.1fold higher than wild-type enzyme, Km-value for fructose 1,6-diphosphate is 1.14fold lower than wild-type enzyme
Y229F
the kcat/Km-value of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) for D-fructose 1,6-bisphosphate is 1.1fold higher than the wild-type value, no fructose-bisphosphate aldolase activity
Y348F
the kcat/Km-value of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) for D-fructose 1,6-bisphosphate is 3.5fold lower than the wild-type value, the kcat/Km-value for the fructose-bisphosphate aldolase reaction of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) in the anabolic direction is 16fold lower than wild-type value
Y229F
-
the kcat/Km-value of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) for D-fructose 1,6-bisphosphate is 1.1fold higher than the wild-type value, no fructose-bisphosphate aldolase activity
-
Y348F
-
the kcat/Km-value of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) for D-fructose 1,6-bisphosphate is 3.5fold lower than the wild-type value, the kcat/Km-value for the fructose-bisphosphate aldolase reaction of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) in the anabolic direction is 16fold lower than wild-type value
-
A51P
The mutation has little effect on the binding affinity of AMP, but increases the KI value. The KM value is unchanged.
D118A
mutant tetramer with one wild-type subunit and three mutant subunits. Kinetic parameters similar to wild-type, kcat-value is about one-fourth that of wild-type
D121A
mutant tetramer with one wild-type subunit and three mutant subunits. Kinetic parameters similar to wild-type, kcat-value is about one-fourth that of wild-type
D68E
-
mutation shifts the pH-optimum from pH 7.0 for the wild type enzyme to pH 8.5 for the mutant enzyme, decreased binding affinity for Mg2+ compared to wild type enzyme
D74A
-
50000fold reduced turnover number relative to wild type enzyme
D74E
-
mutation shifts the pH-optimum from pH 7.0 for the wild type enzyme to pH 8.5 for the mutant enzyme, decreased binding affinity for Mg2+ compared to wild type enzyme, no AMP cooperativity, kinetic mechanism of AMP inhibition with respect to Mg2+ is changed from competitive to noncompetitive
D74N
-
2000fold reduced turnover number relative to wild type enzyme
E280Q
-
K+ loses the ability to activate and became a noncompetitive inhibitor
E97A
mutant tetramer with one wild-type subunit and three mutant subunits. Kinetic parameters similar to wild-type, kcat-value is about one-fourth that of wild-type
F16W
mutant FBPases exhibits identical electrophoretic mobility as FBPase isolated from pig kidney. Mutation does not affect catalytic properties significantly, except the loss of AMP cooperativity
F89W
mutant FBPases exhibits identical electrophoretic mobility as FBPase isolated from pig kidney. Mutation does not affect catalytic properties significantly
G191A
decreased Km-value for fructose 1,6-diphosphate, decreased inhibition constant for fructose 1,6-diphosphate and decreased Mg2+ affinity compared to the wild type enzyme. The 50% inhibiting concentration of AMP is increased over 2000fold relative to the wild type enzyme, loss of AMP cooperativity, mechanism of AMP inhibition changes from competitive to noncompetitive
I10D
mutation introduces an electrostatic charge that destabilizes the R and T states. Structure and molcular dynamic simulation show that the AMP/Mg2+ and AMP/Zn2+ complexes of mutant I10D are in intermediate quaternary conformations completing 12° of the subunit-pair rotation, but the complex with Zn2+ provides an engaged loop in a near-T quaternary state. The 12° subunit-pair rotation generates close contacts involving the hinges, residues 50-57 and hairpin turns, residues 58-72, of the engaged loops. Additional subunit-pair rotation toward the T state would make such contacts unfavorable
I190T
decreased Km-value for fructose 1,6-diphosphate, decreased inhibition constant for fructose 1,6-diphosphate decreased Mg2+ affinity compared to the wild type enzyme. The 50% inhibiting concentration of AMP is increased over 2000fold relative to the wild type enzyme, loss of AMP cooperativity, mechanism of AMP inhibition changes from competitive to noncompetitive
K42E
decreased Km-value for fructose 1,6-diphosphate, decreased inhibition constant for fructose 1,6-diphosphate and decreased Mg2+ affinity compared to the wild type enzyme. The 50% inhibiting concentration of AMP is increased over 2000fold relative to the wild type enzyme, loss of AMP cooperativity
K42T
decreased Km-value for fructose 1,6-diphosphate, decreased inhibition constant for fructose 1,6-diphosphate decreased Mg2+ affinity compared to the wild type enzyme. The 50% inhibiting concentration of AMP is increased over 2000fold relative to the wild type enzyme, loss of AMP cooperativity, mechanism of AMP inhibition changes from competitive to noncompetitive
K50P
The mutation has little effect on the binding affinity of AMP, but increases the KI value. The KM value is unchanged, but 40fold loss if specific activity in comparison of wild-type enzyme, the Hill coefficients of Mg2+ are significantly reduced
K50P/Y57W
the KI value of AMP is increased, the mutant displays a biphasic bahavior toward AMP, the KM value is unchanged
K71A
-
mutation shifts the pH-optimum from pH 7.0 for the wild type enzyme to pH 7.5 for the mutant enzyme
K71M/K72M
-
mutation shifts the pH-optimum from pH 7.0 for the wild type enzyme to pH 7.5 for the mutant enzyme, 175fold increased inhibition constant for AMP, 2fold increased affinity for Mg2+
N64A
-
mutation shifts the pH-optimum from pH 7.0 for the wild type enzyme to pH 8.5 for the mutant enzyme, decreased binding affinity for Mg2+ compared to wild type enzyme, no AMP cooperativity, kinetic mechanism of AMP inhibition with respect to Mg2+ is changed from competitive to noncompetitive
N64Q
-
mutation shifts the pH-optimum from pH 7.0 for the wild type enzyme to pH 8.5 for the mutant enzyme, decreased binding affinity for Mg2+ compared to wild type enzyme
Q32L
decreased Km-value for fructose 1,6-diphosphate and decreased inhibition constant for fructose 1,6-diphosphate compared to the wild type enzyme. 1.7fold increase in turnover number, 8fold increase in Mg2+ affinity. 8fold increase in 50% inhibiting concentration of AMP
R49C
-
less thermostable than wild type enzyme, wild type values for turnover number and Km-value
R49D
-
less thermostable than wild type enzyme, wild type values for turnover number and Km-value, increased inhibition constant for fructose 2,6-diphosphate. Mechanism of AMP inhibition with respect to fructose 1,6-diphosphate changes from noncompetitive, wild type, to competitive. Mechanism of AMP inhibition with respect to fructose 1,6-diphosphate changes from noncompetitive, wild type, to uncompetitive. Loss of AMP cooperativity
R49L
-
less thermostable than wild type enzyme, wild type values for turnover number and Km-value, increased inhibition constant for fructose 2,6-diphosphate. Mechanism of AMP inhibition with respect to fructose 1,6-diphosphate changes from noncompetitive, wild type, to competitive. Loss of AMP cooperativity
R49M
-
enzyme is more thermostable than wild type enzyme, kinetic properties are similar to the wild type enzyme. Loss of AMP cooperativity
D198H
more than 10fold reduction in kcat value, reduction in IC50 value of AMP
D200A
simultaneous decrease in substrate affinity and kcat value
D97A
almost complete loss of activity
E100A
almost complete loss of activity
E225A
almost complete loss of activity
E57A
almost complete loss of activity
F309A
greatly reduced activity
H215A
greatly reduced activity
K134A
greatly reduced activity, reduction in IC50 value of AMP
K29A
2fold increase in activity
N213A
greatly reduced activity
R164A
greatly reduced activity
R176A
simultaneous decrease in substrate affinity and kcat value
R178G
greatly reduced activity
R307A
greatly reduced activity
R314A
greatly reduced activity
T102A
more than 10fold reduction in kcat value, reduction in IC50 value of AMP
Y131A
greatly reduced activity
K274L
-
site-directed mutagenesis, active site mutant. The residue K274 is very important for AMP analogue TNP-AMP to bind to the active site of FBPase
K274L
-
equivalent activity to the wild-type enzyme. Wild-type and mutant FBPases behaved identically throughout expression and purification. When the residue K274 is mutated to L274, 2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate can not bind to the active site, but can bind to the allosteric site
T84A
inactive mutant enzyme
T84A
site-directed mutagenesis, catalytically inactive active-site mutant
T84A
site-directed mutagenesis, the codon ACC for Thr84 is replaced by GCA for alanine, the active site mutant shows fully abolished enzyme activity while retaining substrate binding affinity
T84A
mutantion fully abolishes enzyme activity while retaining substrate binding affinity
T84S
site-directed mutagenesis, active-site mutant, the mutant shows reduced activity compared to wild-type. One Mg2+ ion is found in T84S MtFBPaseII, coordinated to a glycerol molecule and to Asp79, Asp82, and Glu208 near the cleaved 1-phosphate group of the substrate
T84S
site-directed mutagenesis, the codon ACC for Thr84 is replaced by AGC for serine, the active site mutant retains some activity having a 10times reduction in Vmax and exhibit similar sensitivity to lithium when compared to the wild-type enzyme
T84S
lower catalytic activity than wild-type enzyme
T84S
mutantion retains some activity having a 10 times reduction in Vmax and exhibits similar sensitivity to lithium when compared to the wild-type enzyme. Homology modeling using the Escherichia coli enzyme structure suggests that the replacement of the critical nucleophile OH- in the Thr84 residue of the wild-type enzyme by Ser84 results in subtle alterations of the position and orientation that reduces the catalytic efficiency. This mutant can be used to trap reaction intermediates, through crystallographic methods, facilitating the design of potent inhibitors via structure-based drug design
T84A
-
site-directed mutagenesis, catalytically inactive active-site mutant
-
T84A
-
site-directed mutagenesis, the codon ACC for Thr84 is replaced by GCA for alanine, the active site mutant shows fully abolished enzyme activity while retaining substrate binding affinity
-
T84A
-
mutantion fully abolishes enzyme activity while retaining substrate binding affinity
-
T84S
-
site-directed mutagenesis, active-site mutant, the mutant shows reduced activity compared to wild-type. One Mg2+ ion is found in T84S MtFBPaseII, coordinated to a glycerol molecule and to Asp79, Asp82, and Glu208 near the cleaved 1-phosphate group of the substrate
-
T84S
-
site-directed mutagenesis, the codon ACC for Thr84 is replaced by AGC for serine, the active site mutant retains some activity having a 10times reduction in Vmax and exhibit similar sensitivity to lithium when compared to the wild-type enzyme
-
T84S
-
mutantion retains some activity having a 10 times reduction in Vmax and exhibits similar sensitivity to lithium when compared to the wild-type enzyme. Homology modeling using the Escherichia coli enzyme structure suggests that the replacement of the critical nucleophile OH- in the Thr84 residue of the wild-type enzyme by Ser84 results in subtle alterations of the position and orientation that reduces the catalytic efficiency. This mutant can be used to trap reaction intermediates, through crystallographic methods, facilitating the design of potent inhibitors via structure-based drug design
-
T84A
-
site-directed mutagenesis, the codon ACC for Thr84 is replaced by GCA for alanine, the active site mutant shows fully abolished enzyme activity while retaining substrate binding affinity
-
T84A
-
mutantion fully abolishes enzyme activity while retaining substrate binding affinity
-
T84S
-
site-directed mutagenesis, the codon ACC for Thr84 is replaced by AGC for serine, the active site mutant retains some activity having a 10times reduction in Vmax and exhibit similar sensitivity to lithium when compared to the wild-type enzyme
-
T84S
-
mutantion retains some activity having a 10 times reduction in Vmax and exhibits similar sensitivity to lithium when compared to the wild-type enzyme. Homology modeling using the Escherichia coli enzyme structure suggests that the replacement of the critical nucleophile OH- in the Thr84 residue of the wild-type enzyme by Ser84 results in subtle alterations of the position and orientation that reduces the catalytic efficiency. This mutant can be used to trap reaction intermediates, through crystallographic methods, facilitating the design of potent inhibitors via structure-based drug design
-
C155S
-
lowest Mg2+ requirement, when the regulatory site disulfide is opened by mutation, in comparison to wild-type enzyme and mutant C179S
C174S
-
lowest Mg2+ requirement, when the regulatory site disulfide is opened by mutation, in comparison to wild-type enzyme and mutant C179S
C174S
-
mutant is active and can be inactivated by oxidation
C179S
-
mutant is inactive
C179S
-
mutant significantly decreases the Mg2+ requirement of the oxidized enzyme, mutant is more easily activated by thioredoxin f in comparison to wild-type enzyme
F219W
mutant FBPases exhibits identical electrophoretic mobility as FBPase isolated from pig kidney. Mutation does not affect catalytic properties significantly
F219W
-
mutation introduced to allow for fluorescence measurements. At concentrations near the Km value, the substrate fructose 1,6-bispohosphate causes a 15% increase in the intrinsic fluorescence of the mutant
F232W
mutant FBPases exhibits identical electrophoretic mobility as FBPase isolated from pig kidney. Mutation does not affect catalytic properties significantly
F232W
-
mutation introduced to allow for fluorescence measurements. The fluorescence emission of the mutant is not altered significantly by the substrate
K112A
site-directed mutagenesis, mutation in the AMP-binding site to eliminate AMP hydrogen bonding to amino acids in the binding pocket
K112A
mutations in the AMP-binding site demonstrates an eight to nine-fold decrease in AMP inhibition
L56A
site-directed mutagenesis, interfacial mutant, that displays an about 5fold increased Ki for D-fructose 2,6-bisphosphate compared to wild-type
L56A
mutant enzyme (interfacial mutant) exhibits an increase in Ki for fructose-2,6-bisphosphate by approximately 5fold
L73A
site-directed mutagenesis, interfacial mutant, that displays an about 5fold increased Ki for D-fructose 2,6-bisphosphate compared to wild-type
L73A
mutant enzyme (interfacial mutant) exhibits an increase in Ki for fructose-2,6-bisphosphate by approximately 5fold
M177A
site-directed mutagenesis, the mutant data correlates with clinical data
M177A
mutation reveals an approximate two to three-fold decrease in inhibitory constants (Ki's) for natural inhibitors AMP and fructose-2,6-bisphosphate compared with the wild-type enzyme
M248D
site-directed mutagenesis, active site mutant, that displays an about 7fold increase in Ki for D-fructose 2,6-bisphosphate, a 4fold decrease in its apparent Km, and a 6fold increase in catalytic efficiency as compared to wild-type. The M248 residue is mutated to aspartic acid in an attempt to activate the enzyme as a means to enhance its binding affinity to the activating metals manganese and magnesium
M248D
the active site mutant enzyme displays an approximate 7fold increase in Ki for fructose-2,6-bisphosphate. The mutant enzyme displays a four-fold decrease in its apparent Michelis constant, and a six-fold increase in catalytic efficiency
Y113A
site-directed mutagenesis, mutation in the AMP-binding site to eliminate AMP hydrogen bonding to amino acids in the binding pocket
Y113A
mutations in the AMP-binding site demonstrates an eight to nine-fold decrease in AMP inhibition
Y164A
site-directed mutagenesis, the mutant data correlates with clinical data
Y164A
mutation reveals an approximate two to three-fold decrease in inhibitory constants (Ki's) for natural inhibitors AMP and fructose-2,6-bisphosphate compared with the wild-type enzyme
additional information
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reduction of expression level by corresponding Pisum sativum antisense construct. Reduction of foliar enzyme activity in transformants T2and T3 generation ranges from 20% to 42% and correlates with lower levels of protein. Antisense plants display different phenotypes with a clear increase in leaf fresh weight, a shift in sucrose-to-starch ratio reaching a maximum of 0.99
additional information
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fusion of C-terminal half of Beta vulgaris with C-terminal half of Pisum sativum enzyme, or insertion of cysteine-rich light regulatory sequence of Pisum sativum enzyme into corresponding site of Beta vulgaris enzyme. Both mutants show a decrease in pH-optimum, decrease in sensitivity to AMP, increase in sensitivity to substrate fructose 1,6-bisphosphate and negligible activation by thioredoxin f
additional information
EgFBPaseI gene suppression by by RNAi gene silencing
additional information
EgFBPaseI gene suppression by by RNAi gene silencing
additional information
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EgFBPaseI gene suppression by by RNAi gene silencing
additional information
EgFBPaseII gene suppression by by RNAi gene silencing
additional information
EgFBPaseII gene suppression by by RNAi gene silencing
additional information
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EgFBPaseII gene suppression by by RNAi gene silencing
additional information
silencing of EgFBPaseIII by RNAi
additional information
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silencing of EgFBPaseIII by RNAi
additional information
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silencing of EgFBPaseIII by RNAi
-
additional information
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EgFBPaseII gene suppression by by RNAi gene silencing
-
additional information
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EgFBPaseI gene suppression by by RNAi gene silencing
-
additional information
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fusion of C-terminal half of Beta vulgaris with C-terminal half of Pisum sativum enzyme, or insertion of cysteine-rich light regulatory sequence of Pisum sativum enzyme into corresponding site of Beta vulgaris enzyme. Both mutants show a decrease in pH-optimum, decrease in sensitivity to AMP, increase in sensitivity to substrate fructose 1,6-bisphosphate
additional information
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deletion of the first and the first two N-terminal amino acids of FBPase affects neither the kinetic properties of the enzyme not its association with aldolase. The kinetic properties of the mutant with deletion of the first three N-terminal amino acids are entirely the same as these of the wild-type muscle enzyme, its affinity to aldolase is significanltly reduced. The same affinity reduction is observed for the FPase construct lacking the first four N-terminal residues. This protein shows a slight perturbation of its kinetics, a lower sensitivity to inhibition by AMP and a little weaker activation by Mg2+
additional information
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to determine the role of upregulated liver FBPase in glucose homeostasis human liver FBPase transgenic mice under the control of the transthyretin promoter are generated, expressing the transgene specifically in liver. Hemizygous transgenic mice have an approximately 3fold increase in total liver FBPase mRNA with concomitant increases in FBPase protein and enzyme activity levels. After high-fat feeding, hemizygous transgenics are glucose intolerant compared to wild-type. Homozygous chow-fed transgenic mice show a 5.5fold increase in liver FBPase levels and are glucose intolerant with a significantly higher rate of endogenous glucose production
additional information
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transgenic mouse lines overexpressing huFBPase gene specifically in pancreatic islet beta-cells are generated to determine whether a specific increase in islet beta-cell FBPase can result in reduced glucose-mediated insulin secretion. FBPase transgenic mice show reduced insulin secretion in response to an intravenous glucose bolus. Pancreatic beta-cell lines (MIN6) stably overexpressing huFBPase show a decreased cell proliferation rate and significantly depressed glucose-induced insulin secretion. These defects are associated with a decrease in the rate of glucose utilization, resulting in reduced cellular ATP levels
additional information
deletion of first 7 N-terminal amino acids of isoform FBP2 markedly impairs colocalization of the enzyme with mitochondria in the presence of GSK3 inhibitor. Deletion of the next 3 residues further enhanced this effect
additional information
genetic silencing of fructose-1,6-bisphosphatase (FBP1), FBP1 downregulation enhances the activity of Wnt/beta-catenin pathway and increases the level of its downstream targets, including c-Myc and MMP7
additional information
genetic silencing of fructose-1,6-bisphosphatase (FBP1), FBP1 downregulation enhances the activity of Wnt/beta-catenin pathway and increases the level of its downstream targets, including c-Myc and MMP7
additional information
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enzyme null-mutant, unable to grow in the absence of hexose, null mutant promastigotes are internalized by macrophages and differentiate into amastigotes but are unable to replicate in the macrophage phagolysosome. Mutant persists in mice but fails to generate normal lesions
additional information
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OscFBP1 mutants (mutant allele oscfbp1-1 containing a Tos17 insertion in the second exon, and mutant allele oscfbp1-2 harbouring a T-DNA insertion in the third intron) exhibit markedly decreased photosynthetic rates and severe growth retardation with reduced chlorophyll content, which results in plant death. Analysis of primary carbon metabolites reveals both significantly reduced levels of sucrose, glucose, fructose and starch in leaves of these mutants, and a high accumulation of sucrose to starch in leaves of rice plants. In the oscfbp1 mutants, products of glycolysis and the TCA cycle are significantly increased. A partitioning experiment of 14C-labelled photoassimilates reveals altered carbon distributions including a slight increase in the insoluble fraction representing transitory starch, a significant decrease in the neutral fraction corresponding to soluble sugars and a high accumulation of phosphorylated intermediates and carboxylic acid fractions in the oscfbp1 mutants
additional information
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enzyme deletion mutant, reduced sensitivity to alkylating agent methymethane sulfonate and reduced production of reactive oxygen species. Overexpression of enzyme increases sensitivity to methymethane sulfonate, shortens life span and increases induction of RNR2 gene
additional information
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to avoid the decrease in accumulation of a foreign protein in the chloroplasts caused by excess expression of FBP/SBPase for enhancing plant growth, transplastomic tobacco plants are generated carrying a S.7942 fbp/sbp transgene with a different promoter in the plastid genome. Analyses of the photosynthetic parameters and the metabolites of transformants indicates that a 2 to 3fold increase in levels of FBPase and SBPase activity is sufficient to increase the final amount of dry matter by up to 1.8fold relative to the wild-type plants
additional information
overexpression of bifunctional fructose-1,6-bisphosphatase/sedoheptulose-1,7-bisphosphatase (BiBPase) alters the carbon partitioning to extracellular carbohydrate. It induces carbohydrate partitioning which is significantly different from that in the wild-type and more towards extracellular carbohydrate and less towards glycogen. The activities of aldolase and ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) are enhanced by overexpression of BiBPase compared to wild-type, while glucose 6-phosphate dehydrogenase activity is decreased. Overexpression of BiBPase leads to enhanced cell size and photosynthetic O2 evolution. Overexpression of BiBPase in Synechococcus sp. PCC 7002 confers faster growth under elevated [CO2] and light conditions, but not under conditions where the amount of either light or CO2 is limiting
additional information
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overexpression of bifunctional fructose-1,6-bisphosphatase/sedoheptulose-1,7-bisphosphatase (BiBPase) alters the carbon partitioning to extracellular carbohydrate. It induces carbohydrate partitioning which is significantly different from that in the wild-type and more towards extracellular carbohydrate and less towards glycogen. The activities of aldolase and ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) are enhanced by overexpression of BiBPase compared to wild-type, while glucose 6-phosphate dehydrogenase activity is decreased. Overexpression of BiBPase leads to enhanced cell size and photosynthetic O2 evolution. Overexpression of BiBPase in Synechococcus sp. PCC 7002 confers faster growth under elevated [CO2] and light conditions, but not under conditions where the amount of either light or CO2 is limiting
-
additional information
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overexpression of bifunctional fructose-1,6-bisphosphatase/sedoheptulose-1,7-bisphosphatase (BiBPase) alters the carbon partitioning to extracellular carbohydrate. It induces carbohydrate partitioning which is significantly different from that in the wild-type and more towards extracellular carbohydrate and less towards glycogen. The activities of aldolase and ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) are enhanced by overexpression of BiBPase compared to wild-type, while glucose 6-phosphate dehydrogenase activity is decreased. Overexpression of BiBPase leads to enhanced cell size and photosynthetic O2 evolution. Overexpression of BiBPase in Synechococcus sp. PCC 7002 confers faster growth under elevated [CO2] and light conditions, but not under conditions where the amount of either light or CO2 is limiting
-
additional information
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to avoid the decrease in accumulation of a foreign protein in the chloroplasts caused by excess expression of FBP/SBPase for enhancing plant growth, transplastomic tobacco plants are generated carrying a S.7942 fbp/sbp transgene with a different promoter in the plastid genome. Analyses of the photosynthetic parameters and the metabolites of transformants indicates that a 2 to 3fold increase in levels of FBPase and SBPase activity is sufficient to increase the final amount of dry matter by up to 1.8fold relative to the wild-type plants
-
additional information
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a mutant defective in photoautotrophic growth is isolated from a random insertion mutant library. The interrupted gene is identified to be slr2094 (fbp1), which encodes the FBPase/sedoheptulose-1,7-biphosphatase bifunctional enzyme. Two other independently constructed slr2094 mutants by targeted insertion show an identical phenotype. The FBPase activity is found to be virtually lacking in an slr2094 mutant, which is sensitive to light under mixotrophic growth conditions
additional information
a Yarrowia lipolytica strain with two different disrupted versions of YlFBP1 is constructed. The mutant strain grows much slower than the wild type in gluconeogenic carbon sources but growth is not abolished due to the existance of an alternative phosphatase with a high Km for fructose-1,6-bisphosphate
additional information
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a Yarrowia lipolytica strain with two different disrupted versions of YlFBP1 is constructed. The mutant strain grows much slower than the wild type in gluconeogenic carbon sources but growth is not abolished due to the existance of an alternative phosphatase with a high Km for fructose-1,6-bisphosphate
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