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D-fructose 6-phosphate
D-glucose 6-phosphate
D-fructose 6-phosphate
D-mannose 6-phosphate
D-galactose
D-tagatose
-
-
-
-
?
D-glucose 6-phosphate
D-fructose 6-phosphate
D-Mannose 6-phosphate
D-Fructose 6-phosphate
fructose 6-phosphate
D-glucose 6-phosphate
-
-
r
Fructose 6-phosphate
Glucose 6-phosphate
Glucose 6-phosphate
Fructose 6-phosphate
L-talose
L-tagatose
best aldose substrate
-
-
?
malonic dialdehyde
methylglyoxal
-
-
-
-
r
additional information
?
-
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
?
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
?
D-fructose 6-phosphate
D-glucose 6-phosphate
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
-
?
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
?
D-fructose 6-phosphate
D-glucose 6-phosphate
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
-
?
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
Cassia coluteoides
-
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
?
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
?
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
?
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
?
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
?
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
?
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
?
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
the isomerization occurrs by a cis-enediol intermediate involving C-1 pro-R hydrogen of D-fructose 6-phosphate. The presence of metal electrophile to activate the carbonyl group is required not only for the hydride shift mechanism but also for the operation of an enediol process
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
r
D-fructose 6-phosphate
D-mannose 6-phosphate
-
-
-
r
D-fructose 6-phosphate
D-mannose 6-phosphate
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
?
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
Cassia coluteoides
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
?
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
?
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
?
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
?
D-glucose 6-phosphate
D-fructose 6-phosphate
multistep catalytic mechanism is proposed: first the enzyme catalyzes ring opening to yield the open chain form of the substrate. Then isomerization proceeds via proton transfer between C2 and C1 of a cis-enediol(ate) intermediate to yield the open chain form of the product. His388 promotes ring opening by protonating the ring oxygen. Glu216 helps to position His388, and a water molecule that is held in position by Lys518 and Thr214 accepts a proton from the hydroxyl group at C2
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
the active site residues Lys58 and His388 might be involved in catalytic mechanism
-
?
D-glucose 6-phosphate
D-fructose 6-phosphate
in the cytoplasm, it catalyzes the second step in glycolysis. Outside the cell, it serves as a nerve growth factor and cytokine
-
?
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
?
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
?
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
in hydride shift mechanism of catalysis Fe2+ is responsible for proton transfer between O1 and O2, and the hydride shift between C1 and C2 is favored by a markedly hydrophobic environment in the active site. The absence of any obvious enzymatic machinery for catalyzing ring opening of the sugar substrates suggests that the pyrococcal enzyme has a preference for straight chain substrates. The metabolism in extreme thermophiles may use sugars in both ring and straight chain forms. At the extreme temperatures in which Pyrococcus furiosus exists, the equilibrium would increasingly favor the open chain forms
-
-
?
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
?
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
the glucose 6-phosphate molecule is bound in an extended conformation in the active site of PGI, substrate binding structure, overview
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
the glucose 6-phosphate molecule is bound in an extended conformation in the active site of PGI, substrate binding structure, overview
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
r
Fructose 6-phosphate
Glucose 6-phosphate
-
r
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
r
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
-
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
-
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
-
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
-
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
-
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
r
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
r
-
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
r
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
r
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
-
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
-
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
r
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
-
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
r
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
-
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
-
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
r
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
r
-
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
r
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
r
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
r
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
-
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
-
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
r
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
r
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
-
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
-
-
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
r
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
r
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
r
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
-
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
-
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
r
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
-
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
r
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
-
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
-
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
r
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
r
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
r
-
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
r
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
r
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
r
-
?
additional information
?
-
-
the multifunctional protein GPI shows specific and competitive inhibitory activity toward a myofibril-bound serine proteinase, MBSP, from Carassius auratus with a Ki of 320 nM, inhibition kinetics, while no inhibitory activity is identified toward other serine proteinases, such as white croaker MBSP and crucian carp trypsin, overview
-
-
?
additional information
?
-
-
the formation of phosphoglucose isomerase is under respiratory control, during anaerobiosis the enzyme is derepressed parallely with other glycolytic enzymes
-
-
?
additional information
?
-
-
the formation of phosphoglucose isomerase is under respiratory control, during anaerobiosis the enzyme is derepressed parallely with other glycolytic enzymes
-
-
?
additional information
?
-
the enzyme has cell-motility-stimulating activity on mouse colon cancer cells
-
?
additional information
?
-
-
the enzyme has cell-motility-stimulating activity on mouse colon cancer cells
-
?
additional information
?
-
the enzyme plays a central role in both the glycolysis and the gluconeogenesis pathways
-
?
additional information
?
-
-
the enzyme plays a central role in both the glycolysis and the gluconeogenesis pathways
-
?
additional information
?
-
-
PGI/AMF stimulates beta-catenin expression and is involved in E-cadherin and beta-catenin expression regulation, overview
-
-
?
additional information
?
-
the enzyme can also act as an autocrine motility factor, neuroleukin, and maturation factor
-
-
?
additional information
?
-
-
the enzyme can also act as an autocrine motility factor, neuroleukin, and maturation factor
-
-
?
additional information
?
-
the enzyme plays important roles in glycolysis and gluconeogenesis
-
?
additional information
?
-
-
the enzyme plays important roles in glycolysis and gluconeogenesis
-
?
additional information
?
-
-
the enzyme is part of the glycolytic pathway
-
?
additional information
?
-
glucose-6-phosphate isomerase catalyzes the interconversion between two different aldoses and ketose for pentoses and hexoses via two isomerization reactions. Activity order as follows: aldose substrates with hydroxyl groups oriented in the same direction at C2, C3, and C4 better than C2 and C4 better than C2 and C3 better than C3 and C4. L-Talose and D-ribulose exhibit the most preferred substrates among the aldoses and ketoses, respectively, substrate specificity, overview
-
-
?
additional information
?
-
-
glucose-6-phosphate isomerase catalyzes the interconversion between two different aldoses and ketose for pentoses and hexoses via two isomerization reactions. Activity order as follows: aldose substrates with hydroxyl groups oriented in the same direction at C2, C3, and C4 better than C2 and C4 better than C2 and C3 better than C3 and C4. L-Talose and D-ribulose exhibit the most preferred substrates among the aldoses and ketoses, respectively, substrate specificity, overview
-
-
?
additional information
?
-
enzyme does not convert mannose 6-phosphate to fructose 6-phosphate
-
-
?
additional information
?
-
-
enzyme does not convert mannose 6-phosphate to fructose 6-phosphate
-
-
?
additional information
?
-
-
glycolytic enzyme
-
-
?
additional information
?
-
-
enzyme of the oxidative pentose phosphate cycle
-
-
?
additional information
?
-
-
the isomerization occurs by a cis-enediol intermediate involving the C-1 pro-R hydrogen atom of fructose 6-phosphate. The presence of a metal electrophile to activate the carbonyl group is required not only for the hydride shift mechanism but also for the operation of an enediol process
-
-
?
additional information
?
-
the isomerization occurs by a cis-enediol intermediate involving the C-1 pro-R hydrogen atom of fructose 6-phosphate. The presence of a metal electrophile to activate the carbonyl group is required not only for the hydride shift mechanism but also for the operation of an enediol process
-
-
?
additional information
?
-
-
probable role of the enzyme in starch biosynthesis in amyloplasts
-
-
?
additional information
?
-
-
glycolytic enzyme
-
-
?
additional information
?
-
-
glycolytic enzyme
-
-
?
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1,5-Anhydroglucitol 6-phosphate
-
-
2-amino-2-deoxy-D-glucitol 6-phosphate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
2-amino-2-deoxy-D-glucitol 6-phosphate dimethyl ester
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
2-amino-2-deoxy-D-mannitol 6-phosphate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
2-Deoxy-D-glucitol 6-phosphate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
2-deoxyglucose 6-phosphate
-
-
5-deoxy-5-malonate-D-arabinonohydroxamic acid
-
-
5-phospho-D-arabinoamide
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
5-phospho-D-arabinoate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
5-phospho-D-arabinohydroxamate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
5-phospho-D-arabinonohydroxamate
competitive, stable analogue of putative cis-endiol intermediate
5-phospho-D-arabinonohydroxamic acid
-
-
5-phosphoarabinonhydroxamic acid
6-phospho-2-deoxygluconate
Cassia coluteoides
-
glucose 6-phosphate as substrate
6-phospho-D-gluconate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
6-phospho-D-gluconoamide
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
6-Phosphomannonate
Cassia coluteoides
-
with glucose 6-phosphate as substrate
Ca2+
slight inhibition at 1.5 mM
Co2+
10 mM, 59% inhibition, D-fructose 6-phosphate as substrate
D-fructose 1,6-bisphosphate
D-glucitol 6-phosphate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
dihydroxyacetone phosphate
-
-
Erythritol 4-phosphate
-
-
erythrose-4-phosphate
-
-
gluconate 6-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
GTP
-
competitive inhibitor, also compromises the autocrine motility factor function of the enzyme. The GTP-binding site partially overlaps with the catalytic site. In addition,GTP stabilizes the structure of PGI against heat- and detergent-induced denaturation. GTP is bound in a syn-conformation with the gamma-phosphate group located near the phosphate-binding loop and the ribose moiety positioned away from the active-site residues
insulin-like growth factor binding protein-3
-
both glycosylated and unglycosylated, binding and inhibition of enzyme
-
K+
10 mM, 18% inhibition, D-fructose 6-phosphate as substrate
L-Sorbose 6-phosphate
-
-
L-xylulose 5-phosphate
-
-
Maleate
-
10 mM, 50% inhibition
malonate
-
10 mM, 15% inhibition
mannitol 1-phosphate
Cassia coluteoides
-
glucose 6-phosphate as substrate
N,2,3,4,5-pentahydroxypentanamide
-
-
N-acetyl-2-amino-2-deoxy-D-glucitol 6-phosphate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
N-bromoacetylethanolamine phosphate
-
oxaloacetate
-
10 mM, 25% inhibition
oxoglutarate
-
10 mM, 20% inhibition
sedoheptulose 7-phosphate
5-phospho-D-arabinonate
-
5-phospho-D-arabinonate
-
5-phospho-D-arabinonate
competitive
5-phosphoarabinonhydroxamic acid
-
-
5-phosphoarabinonhydroxamic acid
competitive inhibition
6-phosphogluconate
-
6-phosphogluconate
Cassia coluteoides
-
glucose 6-phosphate as substrate
6-phosphogluconate
-
0.2 mM, 52% inhibition
6-phosphogluconate
-
competitive
6-phosphogluconate
-
pH 7.6, 25°C
6-phosphogluconate
-
competitive
Agaricic acid
-
-
Agaricic acid
irreversible inhibition
Cd2+
10 mM, 96% inhibition, D-fructose 6-phosphate as substrate
Cu2+
-
1 mM, about 40% inhibition
Cu2+
10 mM, 96% inhibition, D-fructose 6-phosphate as substrate
D-fructose 1,6-bisphosphate
10 mM, residual activities are 41% and 53% in the direction of fructose 6-phosphate and glucose 6-phosphate formation, respectively
D-fructose 1,6-bisphosphate
-
D-Fructose 1-phosphate
2 mM, residual activities are 50% and 69% in the direction of fructose 6-phosphate and glucose 6-phosphate formation, respectively
D-gluconate 6-phosphate
-
D-gluconate 6-phosphate
-
D-mannose 6-phosphate
1.25 mM, residual activities are 18% and 38% in the direction of fructose 6-phosphate and glucose 6-phosphate formation, respectively
EDTA
-
-
EDTA
100fold excess, complete loss of activity within 10 min. 93% of activity may be recovered by additon of 1000fold excess of Zn2+
EDTA
-
the enzyme activity is completely diminished when the enzyme is heated at 70°C in the presence of 10 mM EDTA. Complete restoration of the enzyme activity is observed when the enzyme is incubated at room temperature in the presence of Zn2+
EDTA
10 mM, 78% inhibition, D-fructose 6-phosphate as substrate
erythrose 4-phosphate
-
erythrose 4-phosphate
Cassia coluteoides
-
glucose 6-phosphate as substrate
erythrose 4-phosphate
-
0.02 mM, 58% inhibition
erythrose 4-phosphate
-
activates enzyme form B with ribose 5-phosphate as substrate, inhibits activity of enzyme form A and B with glucose 6-phosphate as substrate, inhibits activity of enzyme form A with glucose 6-phosphate as substrate
erythrose 4-phosphate
-
competitive
erythrose 4-phosphate
-
-
erythrose 4-phosphate
-
-
erythrose 4-phosphate
-
-
erythrose 4-phosphate
-
competitive
fructose 1,6-diphosphate
-
1 mM, 4% inhibition
fructose 1,6-diphosphate
-
-
fructose 1-phosphate
-
1 mM, 10% inhibition
Hg2+
-
1 mM, about 50% inhibition
Mn2+
10 mM, 18% inhibition, D-fructose 6-phosphate as substrate
Ni2+
10 mM, 84% inhibition, D-fructose 6-phosphate as substrate
phosphate
-
-
ribose 5-phosphate
-
1 mM, 12% inhibition
ribulose 5-phosphate
-
0.5 mM, 48% inhibition
sedoheptulose 7-phosphate
-
1 mM, 10% inhibition
sedoheptulose 7-phosphate
-
-
sorbitol-6-phosphate
-
-
suramin
-
no inhibition
suramin
an anti-trypanosomal drug
Zn2+
-
plastid enzyme is completely inhibited by 5 mM, activity of cytosolic isoenzyme is reduced to 49% of untreated control
Zn2+
10 mM, 89% inhibition, D-fructose 6-phosphate as substrate
additional information
-
no inhibition by PCMB and iodoacetate
-
additional information
-
screening for thiazolide inhibitors, diverse compounds, mode of action of thiazolides and structure-activity relationship, overview
-
additional information
-
not inhibitory: EDTA
-
additional information
activity is not affected by addition of 10 mM EDTA. The addition of fructose, glucose, mannose, galactose (10 mM), pyruvate, phosphoenolpyruvate (10 mM), AMP, ADP, or ATP (3.5 mM), does not show any effect on the activity neither in the fructose 6-phosphate formation, nor in the glucose 6-phosphate formation
-
additional information
-
activity is not affected by addition of 10 mM EDTA. The addition of fructose, glucose, mannose, galactose (10 mM), pyruvate, phosphoenolpyruvate (10 mM), AMP, ADP, or ATP (3.5 mM), does not show any effect on the activity neither in the fructose 6-phosphate formation, nor in the glucose 6-phosphate formation
-
additional information
-
no inhibition by suramin, an anti-trypanosomal drug, and agaricic acid
-
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0.031 - 170
D-fructose 6-phosphate
1.029
D-galactose
-
pH 8.0, 40°C
0.084 - 267.4
D-glucose 6-phosphate
0.25 - 1.1
D-mannose 6-phosphate
0.01 - 0.74
fructose 6-phosphate
0.03 - 8
glucose 6-phosphate
133
L-talose
pH 7.0, 95°C
additional information
additional information
-
0.031
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant S278L
0.034
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant I525T
0.037
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant wild-type enzyme
0.038
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant R347H
0.038
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant R75G
0.039
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant L487F
0.04
D-fructose 6-phosphate
-
50°C, pH 6.3
0.045
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant A300P
0.045
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant L339P
0.046
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant R347C
0.046
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant T375R
0.05
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant E495K
0.06
D-fructose 6-phosphate
-
pH 7.4, 80°C
0.061
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant R83W
0.063
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant T195I
0.063
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant V101M
0.068
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant R472H
0.14
D-fructose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI I from germinating seeds
0.1425
D-fructose 6-phosphate
-
-
0.147
D-fructose 6-phosphate
-
22°C, pH 7.4
0.18
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme Y95K
0.19
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme H136A
0.2
D-fructose 6-phosphate
80°C, pH 7.4
0.21
D-fructose 6-phosphate
50°C, pH 7.4
0.22
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme T63A
0.23
D-fructose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI II from developing seeds
0.25
D-fructose 6-phosphate
pH 7.4, 70°C, wild-type enzyme
0.27
D-fructose 6-phosphate
-
pH 7.6, 25°C
0.3
D-fructose 6-phosphate
-
pH 7.4, 50°C
0.318
D-fructose 6-phosphate
-
pH 7.6, 22°C
0.35
D-fructose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI II from germinating seeds
0.36
D-fructose 6-phosphate
-
pH 8.0
0.36
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme Y95F
0.39
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme H80D
0.42
D-fructose 6-phosphate
50°C, pH 7.0, recombinant enzyme
0.44
D-fructose 6-phosphate
80°C, pH 7.4
0.46
D-fructose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI I from developing seeds
0.5
D-fructose 6-phosphate
50°C
0.5
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme G79A
0.59
D-fructose 6-phosphate
50°C, pH 7.5, mutant enzyme E89V
0.6
D-fructose 6-phosphate
-
pH 7.4, 50°C
0.6 - 3
D-fructose 6-phosphate
pH 7.0, 50°C
0.63
D-fructose 6-phosphate
50°C, pH 7.0, native enzyme
0.7
D-fructose 6-phosphate
-
pH 7.6, 37°C
0.8
D-fructose 6-phosphate
-
pH 7.4, 50°C
1
D-fructose 6-phosphate
-
80°C, pH 7.0, native enzyme
1.2
D-fructose 6-phosphate
-
80°C, pH 7.0, recombinant enzyme
1.4
D-fructose 6-phosphate
50°C, pH 7.5, mutant enzyme H137A
1.4
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme Y160F
1.7
D-fructose 6-phosphate
50°C, pH 7.5, wild-type enzyme
2
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme G79L
2
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme H82A
2.1
D-fructose 6-phosphate
50°C, pH 7.5, mutant enzyme H91A
2.2
D-fructose 6-phosphate
-
at pH 6.0 and 37°C
2.9
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme E93D
3
D-fructose 6-phosphate
-
pH 7.2, 37°C
3.5
D-fructose 6-phosphate
50°C, pH 7.5, mutant enzyme H89A
4
D-fructose 6-phosphate
-
80°C, pH not specified in the publication
20.3
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme H80A
169
D-fructose 6-phosphate
-
wild-type, 37°C, pH 8.0
170
D-fructose 6-phosphate
-
mutant A346H, 37°C, pH 8.0
0.084
D-glucose 6-phosphate
-
in 50 mM HEPES buffer, pH 7.1, at 25°C
0.11
D-glucose 6-phosphate
-
ZR-82 cells, 22°C
0.18
D-glucose 6-phosphate
mutant enzyme D511N, at 21°C in 20 mM HEPES buffer (pH 7.5)
0.2 - 1
D-glucose 6-phosphate
mutant enzyme H100L, at 21°C in 20 mM HEPES buffer (pH 7.5)
0.23
D-glucose 6-phosphate
mutant enzyme E495Q, at 21°C in 20 mM HEPES buffer (pH 7.5)
0.28
D-glucose 6-phosphate
-
22°C, pH 7.4
0.29
D-glucose 6-phosphate
mutant enzyme H396L, at 21°C in 20 mM HEPES buffer (pH 7.5)
0.29
D-glucose 6-phosphate
wild type enzyme, at 21°C in 20 mM HEPES buffer (pH 7.5)
0.3
D-glucose 6-phosphate
mutant enzyme Y274F, at 21°C in 20 mM HEPES buffer (pH 7.5)
0.3
D-glucose 6-phosphate
mutant enzyme Y341F, at 21°C in 20 mM HEPES buffer (pH 7.5)
0.4
D-glucose 6-phosphate
-
pH 7.4, 50°C
0.5
D-glucose 6-phosphate
mutant enzyme Q388A, at 21°C in 20 mM HEPES buffer (pH 7.5)
0.6
D-glucose 6-phosphate
-
pH 7.4, 50°C
0.72
D-glucose 6-phosphate
80°C, pH 7.4
0.73
D-glucose 6-phosphate
mutant enzyme S185A, at 21°C in 20 mM HEPES buffer (pH 7.5)
0.78
D-glucose 6-phosphate
mutant enzyme N386A, at 21°C in 20 mM HEPES buffer (pH 7.5)
0.83
D-glucose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI II from germinating seeds
1
D-glucose 6-phosphate
-
pH 7.6, 37°C
1
D-glucose 6-phosphate
-
pH 7.2, 37°C
1
D-glucose 6-phosphate
-
50°C, pH 6.3
1.02
D-glucose 6-phosphate
-
cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37°C
1.04
D-glucose 6-phosphate
mutant enzyme N154Q, at 21°C in 20 mM HEPES buffer (pH 7.5)
1.1
D-glucose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI I from germinating seeds
1.3
D-glucose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI II from developing seeds
1.5
D-glucose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI I from developing seeds
1.53
D-glucose 6-phosphate
-
avicel-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37°C
1.65
D-glucose 6-phosphate
-
avicel-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60°C
1.86
D-glucose 6-phosphate
-
cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60°C
1.9
D-glucose 6-phosphate
-
pH 7.4, 80°C
1.9
D-glucose 6-phosphate
-
free enzyme, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37°C
1.99
D-glucose 6-phosphate
pH 7.0, 50°C
1.99
D-glucose 6-phosphate
50°C, pH 7.0, native enzyme
2
D-glucose 6-phosphate
50°C, pH 7.0, recombinant enzyme
2.11
D-glucose 6-phosphate
-
immobilized-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37°C
2.43
D-glucose 6-phosphate
-
immobilized-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60°C
2.58
D-glucose 6-phosphate
-
mutant GroD1 cells, 22°C
2.7
D-glucose 6-phosphate
-
pH 7.4, 50°C
2.89
D-glucose 6-phosphate
-
free enzyme, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60°C
3.5
D-glucose 6-phosphate
80°C, pH 7.4
7.9
D-glucose 6-phosphate
-
80°C, pH 7.0, recombinant enzyme
8.7
D-glucose 6-phosphate
-
80°C, pH 7.0, native enzyme
11.7
D-glucose 6-phosphate
50°C, pH 7.5, wild-type enzyme
221
D-glucose 6-phosphate
-
wild-type, 37°C, pH 8.0
267.4
D-glucose 6-phosphate
-
mutant A346H, 37°C, pH 8.0
0.25
D-mannose 6-phosphate
80°C, pH 7.4
1.1
D-mannose 6-phosphate
80°C, pH 7.4
0.01 - 0.17
fructose 6-phosphate
-
muscle enzyme, values of 0.01 mM, 0.12 mM and 0.17 mM are determined by different authors
0.0186
fructose 6-phosphate
-
isomerase a
0.0205
fructose 6-phosphate
-
isomerase c
0.0213
fructose 6-phosphate
-
isomerase b
0.048
fructose 6-phosphate
-
-
0.0596
fructose 6-phosphate
-
mutant enzyme Thr224 to Met
0.0635
fructose 6-phosphate
-
native enzyme
0.0657
fructose 6-phosphate
-
mutant enzyme Thr5 to Ile
0.07
fructose 6-phosphate
-
mammary gland enzyme
0.071
fructose 6-phosphate
-
-
0.0734
fructose 6-phosphate
-
mutant enzyme Asp539 to Asn
0.0769
fructose 6-phosphate
-
mutant enzyme Gln343 to Arg
0.09
fructose 6-phosphate
-
isozyme 1 and isozyme 2
0.1
fructose 6-phosphate
-
-
0.1
fructose 6-phosphate
-
-
0.1
fructose 6-phosphate
-
-
0.1
fructose 6-phosphate
-
-
0.1
fructose 6-phosphate
-
fructose 6-phosphate, isozyme 4
0.1
fructose 6-phosphate
-
glucose 6-phosphate, soluble enzyme
0.11
fructose 6-phosphate
-
isozyme 3
0.11 - 0.23
fructose 6-phosphate
-
values of 0.11 mM, 0.15 mM and 0.23 mM are determined by different autors
0.116
fructose 6-phosphate
-
-
0.119
fructose 6-phosphate
-
-
0.12
fructose 6-phosphate
-
-
0.12
fructose 6-phosphate
-
liver enzyme
0.12
fructose 6-phosphate
-
fructose 6-phosphate, enzyme form PGI II
0.12
fructose 6-phosphate
-
fructose 6-phosphate, at pH 8.6
0.12
fructose 6-phosphate
-
glucose 6-phosphate
0.122
fructose 6-phosphate
-
-
0.167
fructose 6-phosphate
-
-
0.17
fructose 6-phosphate
-
enzyme form PGI I
0.18
fructose 6-phosphate
-
-
0.2
fructose 6-phosphate
-
glucose 6-phosphate, immobilized enzyme
0.2
fructose 6-phosphate
-
enzyme forms PGI I and PGI II
0.21
fructose 6-phosphate
-
erythrocyte enzyme, wild-type
0.228 - 0.278
fructose 6-phosphate
-
-
0.3
fructose 6-phosphate
-
isozyme 1 and 2
0.46
fructose 6-phosphate
-
glucose 6-phosphate, isozyme 2
0.48
fructose 6-phosphate
-
chloroplastic isoenzyme
0.74
fructose 6-phosphate
-
erythrocyte enzyme, mutant B9
0.03 - 0.8
glucose 6-phosphate
-
muscle enzyme, values of 0.03 mM, 0.31 mM and 0.8 mM are determined by different authors
0.12 - 0.57
glucose 6-phosphate
-
mammary gland enzyme, values of 0.12 mM and 0.57 mM are determined by different authors
0.25
glucose 6-phosphate
-
-
0.27
glucose 6-phosphate
-
-
0.3 - 1.5
glucose 6-phosphate
-
values of 0.27 mM, 0.3 mM, 0.7 mM, 0.8 mM and 1.5 mM are determined by different authors
0.351
glucose 6-phosphate
-
mutant enzyme Thr224 to Met
0.36
glucose 6-phosphate
-
-
0.44
glucose 6-phosphate
-
glucose 6-phosphate
0.44
glucose 6-phosphate
-
glucose 6-phosphate, enzyme form PGI I and PGI II
0.44
glucose 6-phosphate
-
at pH 8.6
0.445
glucose 6-phosphate
-
native enzyme
0.449
glucose 6-phosphate
-
mutant enzyme Thr5 to Ile
0.45
glucose 6-phosphate
-
isozyme 4
0.505
glucose 6-phosphate
-
mutant enzyme Asp539 to Asn
0.51
glucose 6-phosphate
-
isozyme 1
0.573
glucose 6-phosphate
-
mutant enzyme Gln343 to Arg
0.58
glucose 6-phosphate
-
isozyme 3
0.58
glucose 6-phosphate
-
fructose 6-phosphate, cytosolic isoenzame
0.6
glucose 6-phosphate
-
liver enzyme
2
glucose 6-phosphate
-
-
2
glucose 6-phosphate
-
-
5.9
glucose 6-phosphate
-
isozyme 2
8
glucose 6-phosphate
-
isozyme 1
8
glucose 6-phosphate
-
glucose 6-phosphate, cytosolic and chloroplastic isoenzyme
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
the pH-value has a great influence on the Km-value for fructose 6-phosphate
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
kinetics for aldose substrates, overview
-
additional information
additional information
-
kinetics for aldose substrates, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0003 - 650
D-fructose 6-phosphate
0.04 - 2765
D-glucose 6-phosphate
3330
fructose 6-phosphate
-
isomerase a
475.5
L-talose
pH 7.0, 95°C
0.0003
D-fructose 6-phosphate
50°C, pH 7.5, mutant enzyme E98V
0.021
D-fructose 6-phosphate
50°C, pH 7.5, mutant enzyme H89A
0.06
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme E93D
0.07
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme G79L
0.22
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme Y95F
0.32
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme G79A
0.34
D-fructose 6-phosphate
50°C, pH 7.5, mutant enzyme H137A
0.42
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme H80D
0.43
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme H80A
0.5
D-fructose 6-phosphate
50°C, pH 7.5, mutant enzyme H91A
0.6
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant S278L
0.68
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme Y95K
1.9
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme T63A
5
D-fructose 6-phosphate
-
at pH 6.0 and 37°C
8
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme H82A
8.4
D-fructose 6-phosphate
50°C
11.6
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme Y160F
15
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant L339P
18
D-fructose 6-phosphate
-
pH 8.0
19
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant L487F
26
D-fructose 6-phosphate
50°C, pH 7.5, wild-type enzyme
30.8
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme H136A
32.4
D-fructose 6-phosphate
pH 7.4, 70°C, wild-type enzyme
42
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant R347H
75
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant T375R
76
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant I525T
93
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant R75G
100
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant A300P
150
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant R347C
160
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant V101M
190
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant R472H
190
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant R83W
300
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant T195I
420
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant mutant E495K
650
D-fructose 6-phosphate
pH 7.5, 30°C, recombinant wild-type enzyme
0.04
D-glucose 6-phosphate
kcat below 0.04 s-1,mutant enzyme K362A, at 21°C in 20 mM HEPES buffer (pH 7.5)
0.04
D-glucose 6-phosphate
kcat below 0.04 s-1mutant enzyme H389L, at 21°C in 20 mM HEPES buffer (pH 7.5)
0.3
D-glucose 6-phosphate
pH 7.5, 30°C, recombinant mutant S278L
0.6
D-glucose 6-phosphate
mutant enzyme H100L, at 21°C in 20 mM HEPES buffer (pH 7.5)
1.3
D-glucose 6-phosphate
mutant enzyme D511N, at 21°C in 20 mM HEPES buffer (pH 7.5)
1.6
D-glucose 6-phosphate
mutant enzyme E495Q, at 21°C in 20 mM HEPES buffer (pH 7.5)
4 - 5
D-glucose 6-phosphate
mutant enzyme Q388A, at 21°C in 20 mM HEPES buffer (pH 7.5)
17
D-glucose 6-phosphate
pH 7.5, 30°C, recombinant mutant L487F
21
D-glucose 6-phosphate
mutant enzyme H396L, at 21°C in 20 mM HEPES buffer (pH 7.5)
31
D-glucose 6-phosphate
pH 7.5, 30°C, recombinant mutant L339P
42
D-glucose 6-phosphate
50°C, pH 7.5, wild-type enzyme
61
D-glucose 6-phosphate
pH 7.5, 30°C, recombinant mutant A300P
63
D-glucose 6-phosphate
pH 7.5, 30°C, recombinant mutant R347H
80
D-glucose 6-phosphate
pH 7.5, 30°C, recombinant mutant T375R
110
D-glucose 6-phosphate
pH 7.5, 30°C, recombinant mutant I525T
120
D-glucose 6-phosphate
pH 7.5, 30°C, recombinant mutant R83W
130
D-glucose 6-phosphate
pH 7.5, 30°C, recombinant mutant R75G
140
D-glucose 6-phosphate
pH 7.5, 30°C, recombinant mutant V101M
240
D-glucose 6-phosphate
mutant enzyme Y274F, at 21°C in 20 mM HEPES buffer (pH 7.5)
260
D-glucose 6-phosphate
pH 7.5, 30°C, recombinant mutant R472H
340
D-glucose 6-phosphate
mutant enzyme Y341F, at 21°C in 20 mM HEPES buffer (pH 7.5)
350
D-glucose 6-phosphate
pH 7.5, 30°C, recombinant mutant R347C
360
D-glucose 6-phosphate
mutant enzyme S185A, at 21°C in 20 mM HEPES buffer (pH 7.5)
380
D-glucose 6-phosphate
pH 7.5, 30°C, recombinant mutant T195I
470
D-glucose 6-phosphate
mutant enzyme N154Q, at 21°C in 20 mM HEPES buffer (pH 7.5)
470
D-glucose 6-phosphate
mutant enzyme N386A, at 21°C in 20 mM HEPES buffer (pH 7.5)
500
D-glucose 6-phosphate
wild type enzyme, at 21°C in 20 mM HEPES buffer (pH 7.5)
729
D-glucose 6-phosphate
-
cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37°C
750
D-glucose 6-phosphate
pH 7.5, 30°C, recombinant mutant E495K
929
D-glucose 6-phosphate
-
free enzyme, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37°C
946
D-glucose 6-phosphate
-
avicel-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37°C
1000
D-glucose 6-phosphate
pH 7.5, 30°C, recombinant wild-type enzyme
1091
D-glucose 6-phosphate
-
immobilized-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37°C
2009
D-glucose 6-phosphate
-
avicel-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60°C
2198
D-glucose 6-phosphate
-
immobilized-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60°C
2433
D-glucose 6-phosphate
-
cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60°C
2765
D-glucose 6-phosphate
-
free enzyme, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.02 - 162
D-fructose 6-phosphate
2.7 - 1700
D-glucose 6-phosphate
3.58
L-talose
pH 7.0, 95°C
0.02
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme E93D
0.02
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme H80A
0.035
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme G79L
0.61
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme Y95F
0.64
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme G79A
1.1
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme H80D
2.27
D-fructose 6-phosphate
-
at pH 6.0 and 37°C
3.8
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme Y95K
4
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme H82A
8.3
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme Y160F
8.6
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme T63A
11.5
D-fructose 6-phosphate
pH 7.0, 50°C, native enzyme
16.5
D-fructose 6-phosphate
pH 7.0, 50°C, recombinant enzyme
130
D-fructose 6-phosphate
pH 7.4, 70°C, wild-type enzyme
162
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme H136A
2.7
D-glucose 6-phosphate
mutant enzyme H100L, at 21°C in 20 mM HEPES buffer (pH 7.5)
6.2
D-glucose 6-phosphate
pH 7.0, 50°C, native enzyme
6.7
D-glucose 6-phosphate
mutant enzyme E495Q, at 21°C in 20 mM HEPES buffer (pH 7.5)
7.4
D-glucose 6-phosphate
mutant enzyme D511N, at 21°C in 20 mM HEPES buffer (pH 7.5)
8.5
D-glucose 6-phosphate
pH 7.0, 50°C, recombinant enzyme
72
D-glucose 6-phosphate
mutant enzyme H396L, at 21°C in 20 mM HEPES buffer (pH 7.5)
90
D-glucose 6-phosphate
mutant enzyme Q388A, at 21°C in 20 mM HEPES buffer (pH 7.5)
450
D-glucose 6-phosphate
mutant enzyme N154Q, at 21°C in 20 mM HEPES buffer (pH 7.5)
489
D-glucose 6-phosphate
-
free enzyme, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37°C
490
D-glucose 6-phosphate
mutant enzyme S185A, at 21°C in 20 mM HEPES buffer (pH 7.5)
517
D-glucose 6-phosphate
-
immobilized-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37°C
610
D-glucose 6-phosphate
mutant enzyme N386A, at 21°C in 20 mM HEPES buffer (pH 7.5)
618
D-glucose 6-phosphate
-
avicel-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37°C
715
D-glucose 6-phosphate
-
cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37°C
790
D-glucose 6-phosphate
mutant enzyme Y274F, at 21°C in 20 mM HEPES buffer (pH 7.5)
906
D-glucose 6-phosphate
-
immobilized-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60°C
957
D-glucose 6-phosphate
-
free enzyme, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60°C
1100
D-glucose 6-phosphate
mutant enzyme Y341F, at 21°C in 20 mM HEPES buffer (pH 7.5)
1218
D-glucose 6-phosphate
-
avicel-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60°C
1308
D-glucose 6-phosphate
-
cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60°C
1700
D-glucose 6-phosphate
wild type enzyme, at 21°C in 20 mM HEPES buffer (pH 7.5)
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malfunction
deficiency of the enzymatic activity in red blood cells causes nonspherocytic hemolytic anemia
malfunction
-
neuromuscular symptoms are associated with inherited GPI deficiency
malfunction
-
PGI/AMF is correlated with breast cancer and poor prognosis in breast cancer. Inhibition of PGI/AMF expression triggers mesenchymal-to-epithelial transition in aggressive mesenchymal-type breast cancer MD-MB-231 cells
malfunction
enzyme deficiency leads to nonspherocytic hemolytic anemia
metabolism
GPI plays an important role in glycolysis
metabolism
-
key enzyme in the AMF signaling pathway, overview
metabolism
-
PGI is a key enzyme in glycolysis and glycogenesis catalyzing the second step of glycolysis
metabolism
-
PGI is the second enzyme of glycolysis
metabolism
PGI is the second enzyme of glycolysis
metabolism
-
phosphoglucose isomerase is a key enzyme in the glycolysis and glycogenesis pathways
metabolism
-
PGI is the second enzyme of glycolysis
-
metabolism
-
GPI plays an important role in glycolysis
-
physiological function
-
AMF is critical for the migration, invasion, metastasis, and anti-apoptotic effects of malignant tumor cells, and its multiple roles in tumor progression may be mediated by certain downstream pathways and effectors. Phosphoglucose isomerase/autocrine motility factor promotes melanoma cell migration through ERK activation dependent on autocrine production of interleukin-8, overview
physiological function
-
multifunctional protein GPI is an endogenous inhibitor to myofibril-bound serine proteinase, and may play a significant role in the regulation of muscular protein metabolism in vivo
physiological function
-
PGI/AMF is a housekeeping gene product/cytokine that catalyzes a step in glycolysis and gluconeogenesis, and acts as a multifunctional cytokine associated with aggessive tumors. PGI/AMF induces a mesenchymal-like morphologic conversion being a key enzyme for both epithelial-to-mesenchymal transition in the initiating step of cancer metastasis and mesenchymal-to-epithelial transition in the late stage of metastasis during breast cancer progression, overview
physiological function
phosphoglucose isomerase plays a key role in both glycolysis and gluconeogenesis inside the cell, whereas outside the cell it exhibits cytokine properties. The enzyme also acts as an autocrine motility factor, a neuroleukin agent and a differentiation and maturation mediator
physiological function
-
the Pgi activity is limiting in the control BL310 strain during growth on lactose or galactose. The level of Pgi enzyme activity controls the level of production of those UDP-glucose and UDP-galactose in galactose
physiological function
-
the enzyme is involved in the modified Embden-Meyerhof pathway
physiological function
-
autocrine motility factor/phosphoglucose isomerase (AMF/PGI) regulates endoplasmic reticulm (ER) stress and cell death through control of ER calcium release. AMF/PGI also protects against thapsigargin- and tunicamycin-induced ER stress and apoptosis and suppresses cytosolic Ca2+ homeostasis
physiological function
-
the enzyme is involved in glycogen catabolism
physiological function
the enzyme is part of the Pyrococcus furiosus variant of the Embden-Meyerhof pathway
physiological function
-
a leaky mutant expressing PGI1 at a level of 1.9% of the wild type, is able to synthesize the pigment melanin in the presence of 2% glucose. Capsule biosynthesis is remarkably reduced in the mutant, integrity of the cell wall and plasma membrane are impaired. The mutant exhibits hypersensitivity to osmotic stress generated by 2 M NaCl or 1 M KCl and fails to utilize mannose and fructose
physiological function
starch content in leaves completely lacking PGI1 activity is about 10-15% of that of wild type leaves and can be be reverted by the introduction of a sex1 null mutation impeding beta-amylolytic starch breakdown. In mutant strains, starch granules are present in the chloroplasts of mesophyll cells and plastidic and extra-plastidic beta-amylase encoding genes are higly expressed in leaves. Mutant strains display slow growth and reduced photosynthetic capacity phenotypes even under continuous light conditions
physiological function
-
phosphoglucose isomerase plays a key role in both glycolysis and gluconeogenesis inside the cell, whereas outside the cell it exhibits cytokine properties. The enzyme also acts as an autocrine motility factor, a neuroleukin agent and a differentiation and maturation mediator
-
physiological function
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
physiological function
-
a leaky mutant expressing PGI1 at a level of 1.9% of the wild type, is able to synthesize the pigment melanin in the presence of 2% glucose. Capsule biosynthesis is remarkably reduced in the mutant, integrity of the cell wall and plasma membrane are impaired. The mutant exhibits hypersensitivity to osmotic stress generated by 2 M NaCl or 1 M KCl and fails to utilize mannose and fructose
-
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118000
-
isoenzymes 1-4, gel filtration
120000 - 127000
Cassia coluteoides
-
gel filtration, density gradient centrifugation
120000 - 130000
-
low-molecular weight form PGI I, gel filtration, sucrose density gradient centrifugation
135000
-
enzyme form A, gel filtration
145000
-
calculation from sedimentation coefficient and diffusion coefficient
172000
-
sedimentation equilibrium analysis
202000 - 204000
-
gel filtration, electrophoresis of the enzyme cross-linked with dimethyl adipimidate
21500
x * 21476, sequence calculation, x * 21500, SDS-PAGE
220000 - 234000
-
high-molecular weight form PGI II, gel filtration
23500
2 * 23500, SDS-PAGE
24000
-
x * 24000, SDS-PAGE
24675
-
x * 24675, calculated from amino acid sequence
26834
-
2 * 26834, calculated, 2 * 32000, SDS-PAGE
27424
-
1 * 27424, calculated, 1 * 28000, SDS-PAGE
30209
-
1 * 30209, calculated, 1 * 28000, SDS-PAGE
32000
-
2 * 26834, calculated, 2 * 32000, SDS-PAGE
33548
-
2 * 36000, SDS-PAGE, 2 * 33548, calculated
34684
-
2 * 34684, calculated, 2 * 27000, SDS-PAGE
35000
2 * 35000, SDS-PAGE, 2 * 35150, calculated
35150
2 * 35000, SDS-PAGE, 2 * 35150, calculated
36100
2 * 36000, SDS-PAGE, 2 * 36100, calculated
41000
-
native enzyme, gel filtration
49000
-
x * 49000, free enzyme, SDS-PAGE
50000
-
x * 50000, SDS-PAGE
50600
-
4 * 50600, SDS-PAGE
56000
-
x * 56000, enzyme variant C, SDS-PAGE
57000
-
x * 57000, enzyme variant B, SDS-PAGE
61310
-
x * 61310, calculation from nucleotide sequence
61450
-
2 * 61450, mass spectrometry, 2 * 61000, SDS-PAGE
63000
-
2 * 63000, sedimentation velocity ultracentrifugation of enzyme dissociated in 6 M guanidine/HCl
6320
-
1 * 6320, A-type subunit, + 1 * 69800, B-type subunit, isoenzyme 3, SDS-PAGE
63200
-
2 * 63200, A-type subunit, isoenzyme 1 and 2, SDS-PAGE
66000
-
x * 66000, SDS-PAGE
67113
-
x * 67113, calculation from nucleotide sequence
67700
-
enzyme form B, gel filtration
70700
-
2 * 70700, isomerase A, SDS-PAGE
73300
x * 75000, recombinant His-tagged enzyme, SDS-PAGE, x * 73300, about, sequence calculation
75000
x * 75000, recombinant His-tagged enzyme, SDS-PAGE, x * 73300, about, sequence calculation
110000
-
gel filtration
110000
-
sedimentation equilibrium analysis
120000
-
-
120000
-
gel filtration, sucrose density gradient centrifugation
120000
-
isoenzyme A, B and C, sedimentation equilibrium ultracentrifugation, gel electrophoresis
120000
-
isoenzyme 1 and 2, sedimentation velocity centrifugation
125000
-
gel filtration
125000
-
cytosolic isoenzyme, gel filtration
125000
-
cytosolic isoenzyme, gel filtration
125000
-
cytosolic isoenzyme, gel filtration
125000
-
isomerase a, sedimentation equilibrium analysis
132000
-
high speed equilibrium sedimentation
132000
-
sedimentation velocity ultracentrifugation
140000
-
plastidic isoenzyme, gel filtration
140000
-
plastidic isoenzyme, gel filtration
140000
-
plastidic isoenzyme, gel filtration
21476
x * 21476, sequence calculation, x * 21500, SDS-PAGE
21476
2 * 21476, calculated from sequence
23000
-
2 * 23000, SDS-PAGE
23000
2 * 23000, SDS-PAGE
27000
-
analytical ultracentrifugation
27000
-
2 * 34684, calculated, 2 * 27000, SDS-PAGE
28000
-
gel filtration
34000
-
2 * 34000, enzyme form B, gel filtration after equilibration with SDS
34000
-
4 * 34000, enzyme form A, gel filtration after equilibration with SDS
36000
-
2 * 36000, SDS-PAGE, 2 * 33548, calculated
36000
2 * 36000, SDS-PAGE, 2 * 36100, calculated
45000
gel filtration
45000
-
2 * 45000, SDS-PAGE
48000
gel filtration
48000
-
mammary gland, low speed sedimentation without reaching equilibrium
55000
-
x * 55000
55000
-
1 * 55000 + 1 * 65000, SDS-PAGE
59000
-
2 * 59000, isoenzyme 1-5, SDS-PAGE
59000
-
2 * 59000, low-molecular weight form, SDS-PAGE
59000
-
possible 4 * 59000, high-molecular weight form, SDS-PAGE
60000
-
x * 60000, enzyme variant A, SDS-PAGE
60000
-
2 * 60000, SDS-PAGE, gel filtration in 6 M guanidine-HCl
61000
-
2 * 61000, SDS-PAGE
61000
-
2 * 61000, SDS-PAGE
61000
-
2 * 61450, mass spectrometry, 2 * 61000, SDS-PAGE
65000
-
sedimentation equilibrium, analytical ultracentrifugation
65000
-
x * 65000, recombinant enzyme, SDS-PAGE
65000
-
1 * 55000 + 1 * 65000, SDS-PAGE
67000
-
gel filtration
67000
analytical ultracentrifugation
69800
-
2 * 69800, B-type subunit, isoenzyme 4, SDS-PAGE
69800
-
1 * 6320, A-type subunit, + 1 * 69800, B-type subunit, isoenzyme 3, SDS-PAGE
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heterodimer
-
1 * 55000 + 1 * 65000, SDS-PAGE
?
-
x * 49000, free enzyme, SDS-PAGE
?
x * 75000, recombinant His-tagged enzyme, SDS-PAGE, x * 73300, about, sequence calculation
?
-
x * 75000, recombinant His-tagged enzyme, SDS-PAGE, x * 73300, about, sequence calculation
-
?
-
x * 56000, enzyme variant C, SDS-PAGE
?
-
x * 60000, enzyme variant A, SDS-PAGE
?
-
x * 57000, enzyme variant B, SDS-PAGE
?
-
x * 67113, calculation from nucleotide sequence
?
-
x * 65000, recombinant enzyme, SDS-PAGE
?
x * 21476, sequence calculation, x * 21500, SDS-PAGE
?
-
x * 61310, calculation from nucleotide sequence
?
-
x * 24675, calculated from amino acid sequence
dimer
2 * 36000, SDS-PAGE, 2 * 36100, calculated
dimer
-
2 * 59000, isoenzyme 1-5, SDS-PAGE
dimer
-
2 * 59000, low-molecular weight form, SDS-PAGE
dimer
-
2 * 59000, low-molecular weight form, SDS-PAGE
-
dimer
-
2 * 70700, isomerase A, SDS-PAGE
dimer
-
2 * 69800, B-type subunit, isoenzyme 4, SDS-PAGE
dimer
-
2 * 63000, sedimentation velocity ultracentrifugation of enzyme dissociated in 6 M guanidine/HCl
dimer
-
2 * 63200, A-type subunit, isoenzyme 1 and 2, SDS-PAGE
dimer
-
1 * 6320, A-type subunit, + 1 * 69800, B-type subunit, isoenzyme 3, SDS-PAGE
dimer
-
2 * 34000, enzyme form B, gel filtration after equilibration with SDS
dimer
-
2 * 45000, SDS-PAGE
dimer
-
2 * 61450, mass spectrometry, 2 * 61000, SDS-PAGE
dimer
-
2 * 60000-70000, SDS-PAGE, SDS velocity centrifugation, maleic anhydride velocity and equilibrium sedimentation, urea velocity sedimentation, propionic acid velocity sedimentation guanidine-HCl velocity and equilibrium sedimentation
dimer
the enzyme is a dimer with two alpha/beta-sandwich domains in each subunit
dimer
-
2 * 61000, SDS-PAGE
dimer
-
2 * 36000, SDS-PAGE, 2 * 33548, calculated
dimer
-
2 * 23000, SDS-PAGE
dimer
2 * 23000, SDS-PAGE
dimer
-
2 * 60000, SDS-PAGE, gel filtration in 6 M guanidine-HCl
dimer
-
2 * 26834, calculated, 2 * 32000, SDS-PAGE
dimer
-
2 * 34684, calculated, 2 * 27000, SDS-PAGE
dimer
-
2 * 61000, SDS-PAGE
dimer
-
2 * 63000-67000, SDS-PAGE, analytical ultracentrifugation in 6 M guanidine/HCl
dimer
2 * 35000, SDS-PAGE, 2 * 35150, calculated
dimer
structure and active site conformation, overview
dimer
-
structure and active site conformation, overview
-
dimer
-
2 * 60000-67000, SDS-PAGE
homodimer
-
homodimer
x-ray crystallography
homodimer
-
x-ray crystallography
-
homodimer
2 * 23500, SDS-PAGE
homodimer
2 * 21476, calculated from sequence
monomer
-
1 * 27424, calculated, 1 * 28000, SDS-PAGE
monomer
-
1 * 30209, calculated, 1 * 28000, SDS-PAGE
tetramer
-
possible 4 * 59000, high-molecular weight form, SDS-PAGE
tetramer
-
possible 4 * 59000, high-molecular weight form, SDS-PAGE
-
tetramer
-
4 * 34000, enzyme form A, gel filtration after equilibration with SDS
tetramer
-
4 * 50600, SDS-PAGE
additional information
predicted 2D and 3D structures of GPI proteins possess potential active motifs including GEPGTNGQHSFYQLIHQG and VQGFIWGINSFDQWGVELGK, and critical active site residues, such as Ser241, Ser296, Thr298, Thr301, Arg358, Glu444, His475 and Lys600
additional information
-
predicted 2D and 3D structures of GPI proteins possess potential active motifs including GEPGTNGQHSFYQLIHQG and VQGFIWGINSFDQWGVELGK, and critical active site residues, such as Ser241, Ser296, Thr298, Thr301, Arg358, Glu444, His475 and Lys600
additional information
-
predicted 2D and 3D structures of GPI proteins possess potential active motifs including GEPGTNGQHSFYQLIHQG and VQGFIWGINSFDQWGVELGK, and critical active site residues, such as Ser241, Ser296, Thr298, Thr301, Arg358, Glu444, His475 and Lys600
-
additional information
structure homology modelling, overview
additional information
-
structure homology modelling, overview
additional information
-
interaction of enzyme with insulin-like growth factor binding protein-3, both glycosylated and unglycosylated, results in formation of a complex of 80 kDa and in dose-dependent inhibition of enzyme
additional information
-
poly(AFP-ribose)polymerase-14, i.e. PARP-14, is a binding partner of phosphoglucose isomerase/autocrine motility factor. Phosphoglucose isomerase/autocrine motility factor is degraded via the ubiquitin-lysosome system, and PARP-14 inhibits the ubiquitination of the enzyme thus contributing to its stabilization and secretion
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hanging drop vapor diffusion method, crystal strcuture at 2.3 A resolution
hanging drop vapor diffusion method, crystal structure of the enzyme complexed with 5-phospho-D-arabinonate and N-bromoacetylethanolamine phosphate at 2.5 A and 2.3 A resolution, respectively. The inhibitors bind to a region within the domains interface and interact with His306 from the other subunit
molecular modeling and dynamics simulation of GTP binding
-
native enzyme and enzyme lacking N-terminal 47 amino acids. Comparison of data with mammalian enzymes
-
native enzyme and in complex with glucose 6-phosphate or erythrose 4-phosphate
hanging drop vapor diffusion method, using 1.2 M ammonium sulfate pH 8.5 (0.1 M HEPES) and 5% (v/v) glycerol at 10°C
resolution of 2.8 A, space group I212121
-
enzyme complexed with the competitive inhibitor D-gluconate 6-phosphate, X-ray crystallography at 2.5 A resolution
hanging drop vapor diffusion method, X-ray crystal structure of the enzyme complexed with the cyclic form of its substrate, D-fructose 6-phosphate, at 2.1 A resolution
in complex with D-sorbitol 6-phosphate
purified recombinant His-tagged enzyme, hanging drop vapour diffusion method, mixing 0.002 ml of both protein solution and reservoir solution, the latter containing 38% v/v PEG 400 and 0.2 M calcium acetate in 0.1 M sodium cacodylate-HCl, pH 6.5, equilibration over 0.5 ml of reservoir solution, 1 week, X-ray diffraction structure determination and analysis at 1.5 A resolution
-
both in complex with fructose 6-phosphate and with glucose 6-phosphate
both native form and in complex with 5-phosphoarabinonate
1.9 A resolution, crystals belong to the space group P2(1)
hanging-drop method of vapour diffusion using 1.6 M sodium citrate as the precipitant at pH 6.5. Maximum resolution of 1.92 A on a single selenomethionine-incorporated crystal. Crystal belongs to space group C2, with approximate unit-cell parameters a = 84.7, b = 42.4, c = 57.3 A, beta = 120.6° and a monomer in the asymmetric unit
-
in presence of bound zinc, substrate D-fructose 6-phosphate and several competitive inhibitors
native form and in comlex with 5-phospho-D-arabinonate, in presence and absence of Mn2+
structure is determined by X-ray diffraction to 2 A resolution
-
vapor diffusion using the hanging drop method, crystal structure of the enzyme in native form and in complex with two active site ligands, 5-phosphoarabinonate and gluconate 6-phosphate
enzyme complexed with glucose 6-phosphate, X-ray diffraction structure determination and analysis at 1.6 A resolution
-
purified recombinant His-tagged enzyme complexed with glucose 6-phosphate, by hanging drop vapor diffusion method at room temperature, 0.004 ml of protein solution with 28.4 mg/ml protein and 5 mM fructose 6-phosphate is mixed with 0.002 ml of reservoir solution containing 10% PEG 3350, 50 mM sodium citrate, and 50 mM dithiothreitol, a few days, X-ray diffraction structure determination and analysis at 1.6 A resolution. Although fructose 6-phosphate is added to the crystallization mixture, the enzyme shows bound gluose 6-phosphate at its active site in the crystals
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E93A
Ni2+ content and apparent Ni2+ binding ability is reduced
E93D
catalytic efficiency is reduced by more than 100fold. Ni2+ content and apparent Ni2+ binding ability is reduced
G79A
mutant enzyme exhibits a lower thermostability, catalytic efficiency is reduced by more than 100fold
G79L
mutant enzyme exhibits a lower thermostability, catalytic efficiency is reduced by more than 100fold
H136A
catalytic efficiency remains about the same compared to wild-type activity
H80A
catalytic efficiency is reduced by more than 100fold. Ni2+ content and apparent Ni2+ binding ability is reduced
H80D
catalytic efficiency is reduced by more than 100fold. Ni2+ content and apparent Ni2+ binding ability is reduced
H82A
catalytic efficiency is reduced by more than 15fold, catalytic efficiency is reduced by more than 15fold. Ni2+ content and apparent Ni2+ binding ability is reduced
T63A
catalytic efficiency is reduced by more than 15fold
Y160F
catalytic efficiency is reduced by more than 15fold
Y95F
mutant enzyme exhibits a lower thermostability, catalytic efficiency is reduced by more than 100fold
Y95K
catalytic efficiency is reduced by more than 15fold
G189E
-
GroD1 enzyme mutant cells show 87% reduced enzyme activity and defects in glycerolipid biosynthesis, overview. The phenotype comprises profound reduction in the synthesis of phosphatidylcholine, phosphatidylethanolamine, and triglycerides but high levels of phosphatidic acid and normal levels of phosphatidylinositol synthesis, accompanied by a reduction in phosphatidate phosphatase 1 activity. Expression of wild-type hamster GPI restores GPI activity, glycerolipid biosynthesis, and PAP1 activity in GroD1
A300P
the mutation may affect the folding efficiency of the enzyme protein, the mutant shows reduced expression level and barely detectable activity
A346H
-
mutation identified in a patient suffering from chronic nonspherocytic hemolytic anemia. Loss of 82% of enzyme activity, loss of enzyme capability to dimerize. Mutation results in significant changes in erythrocyte metabolism
D511N
the mutant shows 0.44% activity compared to the wild type enzyme
E495Q
the mutant shows 0.39% activity compared to the wild type enzyme
H100L
the mutant shows 0.16% activity compared to the wild type enzyme
H389R
the mutation at or near the active site highly affects the catalytic efficiency of the enzyme, the mutant shows barely detectable activity
H396L
the mutant shows 4.2% activity compared to the wild type enzyme
L487F
the mutation decreases the enzyme tolerance to heat or SDS by mechanisms of decreasing packing efficiency
N154Q
the mutant shows 26% activity compared to the wild type enzyme
N386A
the mutant shows 36% activity compared to the wild type enzyme
Q343R
-
mutant enzymes Thr5 to Ile exhibits marked thermal instability. Mutant Thr224 to Met shows normal substrate affinity in spite of slight decrease in both specific activity and thermostability. Mutant Gln343 to Arg and Asp539 to Asn show impaired substrate affinity
Q388A
the mutant shows 5.3% activity compared to the wild type enzyme
R273H
the mutation at or near the active site highly affects the catalytic efficiency of the enzyme, the mutant shows barely detectable activity
R472H
the mutation weakens network bonding of the enzyme
R539N
-
mutant enzymes Thr5 to Ile exhibits marked thermal instability. Mutant Thr224 to Met shows normal substrate affinity in spite of slight decrease in both specific activity and thermostability. Mutant Gln343 to Arg and Asp539 to Asn show impaired substrate affinity
R75G
the mutation weakens network bonding of the enzyme
R83W
the mutation increases the water-accessible hydrophobic surface
S185A
the mutant shows 29% activity compared to the wild type enzyme
T224M
-
mutant enzymes Thr5 to Ile exhibits marked thermal instability. Mutant Thr224 to Met shows normal substrate affinity in spite of slight decrease in both specific activity and thermostability. Mutant Gln343 to Arg and Asp539 to Asn show impaired substrate affinity
T375R
the mutation decreases the enzyme tolerance to heat or SDS by mechanisms of decreasing packing efficiency
T5I
-
mutant enzymes Thr5 to Ile exhibits marked thermal instability. Mutant Thr224 to Met shows normal substrate affinity in spite of slight decrease in both specific activity and thermostability. Mutant Gln343 to Arg and Asp539 to Asn show impaired substrate affinity
V101M
the mutation decreases the enzyme tolerance to heat or SDS by mechanisms of decreasing packing efficiency
Y274F
the mutant shows 46% activity compared to the wild type enzyme
Y341F
the mutant shows 65% activity compared to the wild type enzyme
G157Y
the mutation results in a complete loss of activity
T211A
the mutant shows decreased activity with higher Km compared with that of the wild type protein
G157Y
-
the mutation results in a complete loss of activity
-
T211A
-
the mutant shows decreased activity with higher Km compared with that of the wild type protein
-
E98V
the ratio of turnover number and Km-value is 31373fold lower than that of the wild-type enzyme. The absorption maximum at 420 nm as found in wild-type enzyme is completely lost. Mutant enzyme does not contain iron or zinc or other metal
H137A
the ratio of turnover number and Km-value is 66.7fold lower than that of the wild-type enzyme. The absorption maximum at 420 nm as found in wild-type enzyme is completely lost. Mutant enzyme does not contain iron or zinc or other metal
H89A
the ratio of turnover number and Km-value is 2712fold lower than that of the wild-type enzyme. The absorption maximum at 420 nm as found in wild-type enzyme is completely lost. Mutant enzyme does not contain iron or zinc or other metal
H91A
the ratio of turnover number and Km-value is 66.7fold lower than that of the wild-type enzyme. The absorption maximum at 420 nm as found in wild-type enzyme is completely lost. Mutant enzyme does not contain iron or zinc or other metal
E495K
the mutation may affect the folding efficiency of the enzyme protein, the mutant shows reduced expression level and barely detectable activity
E495K
the mutation weakens network bonding of the enzyme
I525T
the mutation decreases the enzyme tolerance to heat or SDS by mechanisms of decreasing packing efficiency
I525T
the mutation destabilizes the ternary structure of the enzyme
L339P
the mutation decreases the enzyme tolerance to heat or SDS by mechanisms of decreasing packing efficiency
L339P
the mutation may affect the folding efficiency of the enzyme protein, the mutant shows reduced expression level and barely detectable activity
R347C
the mutation destabilizes the ternary structure of the enzyme
R347C
the mutation weakens network bonding of the enzyme
R347H
the mutation destabilizes the ternary structure of the enzyme
R347H
the mutation weakens network bonding of the enzyme
S278L
the mutation at or near the active site highly affects the catalytic efficiency of the enzyme
S278L
the mutation decreases the enzyme tolerance to heat or SDS by mechanisms of decreasing packing efficiency
T195I
the mutation decreases the enzyme tolerance to heat or SDS by mechanisms of decreasing packing efficiency
T195I
the mutation destabilizes the ternary structure of the enzyme
additional information
-
mutant with point mutation in enzyme gene shows abnormal development after germination by extending a primary germ tube that quickly reverts to siotropic growth and results in an enlarged, swollen apex with pronounced wall thickenings. Mutant is unable to conidiate due to a block in conidiophore development at vesicle formation
additional information
-
independently isolated GPI-deficient mutants displayed similar phenotypes like G189E with respect to PAP1 activity and glycerolipid biosynthesis
additional information
identification of 33 single nucleotide polymorphisms and 14 insertion/deletion sites in the strain and EtG6-PI coding sequence
additional information
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identification of 33 single nucleotide polymorphisms and 14 insertion/deletion sites in the strain and EtG6-PI coding sequence
additional information
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downregulation of enzyme expression by siRNA results in increased sensitivity to oxidative stress and oxidative stress-induced cellular senescence. The senscence pathway involving p21 cyclin-dependent kinase inhibitor is up-regulated in enzyme knock-down cells
additional information
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ectopic expression of PGI/AMF induces epithelial-to-mesenchymal transition in MCF10A epithelial breast cancer cells. Inhibition of PGI/AMF expression triggers mesenchymal-to-epithelial transition in aggressive mesenchymal-type breast cancer MD-MB-231 cells
additional information
thermoinactivation of GPI genetic variants, phenotypes, overview
additional information
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thermoinactivation of GPI genetic variants, phenotypes, overview
additional information
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recombinant enzyme carrying His-tag shows enzymatic acitivity equal to native enzyme
additional information
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recombinant enzyme carrying His-tag shows enzymatic acitivity equal to native enzyme
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54.8
the melting temperature of the mutant is 54.8°C
75
purified native enzyme, half-life is 41 h
77
Tm-value of mutant enzyme G79L
85
purified native enzyme, half-life is 19 h
87
Tm-value of mutant enzyme G79A
98
Tm-value of wild-type enzyme and mutant enzymes T63A, H80A, H80D, H82A, E93A, E93D, Y95K and Y160F
100
melting temperature above 100°C
100
-
3 min, complete loss of activity
100
-
melting temperature for thermal unfolding, 60 min, 50% residual activity
100
-
pH 7.0, 180 min, about 60% loss of activity
45
-
soluble enzyme, t1/2: 42 min. Immobilized enzyme, t1/2: 82 min
45
-
presence of Mn2+, 45 min, 55% loss of activity
45
-
15 min, enzyme form PGI I, 50% loss of activity
50
-
7 h, stable
50
-
30 min, no loss of activity
50
-
soluble enzyme, t1/2: 12 min. Immobilized enzyme, t1/2: 10 min
55
-
stable up to
55
-
30 min, complete inactivation
55
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soluble enzyme, t1/2: 2 min. Immobilized enzyme, t1/2: 1 min
55
-
15 min, 50% loss of activity
55
-
15 min, complete loss of activity
55
-
50% loss of activity, enzyme form PGI II
60
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free phosphoglucose isomerase is stable at a high protein concentration of 0.1 g/l (half-life of 180 h at 60°C) but deactivates rapidly at low concentrations (half-life at 60°C is 2.4 h at 0.001 g/l). Immobilized cellulose-binding module-phosphoglucose isomerase at a low concentration of 0.001 g/l has a half-life of 190 h, approximately 80fold of that of free phosphoglucose isomerase. Immobilized cellulose-binding module-phosphoglucose isomerase on regenerated amorphous cellulose is extremely stable at about 60°C, nearly independent of its mass concentration in bulk solution
60
-
15 min, 90% loss of activity
65
-
25% loss of activity after 1 h
65
purified native enzyme, half-life is 170 h
70
-
pH 7.0, 180 min, about 10% loss of activity
70
purified native enzyme, half-life is 68 h
80
-
120 min, stable
80
-
pH 7.0, 180 min, about 20% loss of activity
80
purified native enzyme, half-life is 25 h
90
-
120 min, about 40% loss of activity
90
-
pH 7.0, 180 min, about 50% loss of activity
90
purified native enzyme, half-life is 11 h
90
-
the enzyme exhibits a half-life of 40 min at 90°C
95
-
120 min, about 90% loss of activity
95
purified native enzyme, half-life is 7.9 h
97
-
melting temperature
97
Tm-value of mutant enzyme H136A
additional information
thermoinactivation of GPI genetic variants, overview
additional information
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thermoinactivation of GPI genetic variants, overview
additional information
thermal inactivation follows first-order kinetics
additional information
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thermal inactivation follows first-order kinetics
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DNA and amino acid sequence determination and analysis, GPI expression analysis, recombinant expression of the enzyme in Escherichia coli strain BL21
DNA and amino acid sequence determination and analysis, sequence comparisons, phylogeneitic analysis, and genotyping for polymorphisms
DNA and amino acid sequence determination, PGI genotyping for polymorphisms, influence of environmental conditions and geographic genetic structuring, modeling, overview
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expressed in Escherichia coli BL21 Star (DE3) cells
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expressed in Escherichia coli BL21-CodonPlus(DE3)-RIL cells
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expression in Agrobacterium tumefaciens
expression in Escherichia coli
expression in Escherichia coli BL21
expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
expression of wild-type and mutant enzymes in Escherichia coli strain DF2145
functionally expressed in Escherichia coli BL21(DE3)
genotyping and polymorphisms, overview
GPI gene, DNA and amino acid sequence determination and analysis, phylogenetic tree and expression analysis by real time quantitative RT-PCR, recombinant expression of His-tagged enzyme in Escherichia coli
isozyme A and B overexpressed in Escherichia coli
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native enzyme and mutant enzymes T5I, T224M, Q343R, D539N
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overexpressed in Escherichia coli
-
overexpression in Escherichia coli
overexpression of His-tagged enzyme in Escherichia coli strain BL21 (DE3)
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PGI, expression analysis in cells from healthy and colon cancer individuals
-
-
-
expression in Escherichia coli
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expression in Escherichia coli
-
genotyping and polymorphisms, overview
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genotyping and polymorphisms, overview
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genotyping and polymorphisms, overview
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overexpression in Escherichia coli
-
overexpression in Escherichia coli
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analysis
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Pgi is an adaptive marker, rather than providing insights into individual genetic health, Pgi appears to have a role in conservation genetics by providing insights into gene by environment interactions, local adaptation and evolutionary significant units, and potentially even morphologically cryptic dispersal phenotypes, method development, overview
analysis
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Pgi is an adaptive marker, rather than providing insights into individual genetic health, Pgi appears to have a role in conservation genetics by providing insights into gene by environment interactions, local adaptation and evolutionary significant units, and potentially even morphologically cryptic dispersal phenotypes, method development, overview
analysis
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Pgi is an adaptive marker, rather than providing insights into individual genetic health, Pgi appears to have a role in conservation genetics by providing insights into gene by environment interactions, local adaptation and evolutionary significant units, and potentially even morphologically cryptic dispersal phenotypes, method development, overview
analysis
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phosphoglucose isomerase variability of Cerastoderma glaucum as a model for testing the influence of environmental conditions and dispersal patterns through quantitative ecology approaches, overview. The PGI locus is an appropriate marker for revealing the spatial distribution of genetic variation and for establishing the relationships between allelic composition and the environmental influencing variables
analysis
development of a bioautographic assay based on thin layer chromatography for inhibition of PDI by phosphoenolpyruvate. The detection limit for phosphoenolpyruvate as an inhibitor of PGI is 226 microg per spot/zone
drug development
PGI might be a good target for species-specific drug design
drug development
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the enzyme is a target for development of specific inhibitors against Echinococcus multilocularismetacestodes and disease alveolar echinococcosis, overview
drug development
the enzyme is a valid drug target against protozoa in coccidiosis
drug development
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PGI might be a good target for species-specific drug design
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medicine
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use as a diagnostic tool in medicine
medicine
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frequency of enzyme variants in healthy control subjects with anti-glucoes 6-phosphate antibodies is significantly higher than in antibody-negative healthy subjects. Frequency of enzyme variants in anti-glucose 6-phosphate antibody positive patients suffering from rheumatoid arthritis is more significantly higher than in antibody-negative patients
medicine
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mutation A346H is identified in a patient suffering fromchronic nonspherocytic hemolytic anemia. Mutation results in loss of 82% of enzyme activity, loss of enzyme capability to dimerize, and in significant changes in erythrocyte metabolism
medicine
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enzyme expression is detected in a major proportion of lung carcinomas, and enzyme may play a part in proliferation and/or progression of the tumours as well as possibly in the differentiation of squamous cell carcinoma. higher enzyme mRNA expression may be related to the high metastatic potential of non-small cell lung carcinomas and to increased protein secretion
medicine
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sera and synovial fluids from patients with immune-based inflammatory arthritis contain significantly higher levels of enzyme activity and of enzyme protein both in inactive and active form than healthy control or patients with non-immune based inflammatory arthritis