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hydroxypyruvate + D-glyceraldehyde 3-phosphate
D-xylulose 5-phosphate + CO2
-
7.2% of the activity with pyruvate
-
-
?
pyruvate + 1-methyl-2-nitrosobenzene
N-hydroxy-N-(2-methylphenyl)acetamide + CO2
-
-
-
?
pyruvate + 1-nitrosonaphthalen-2-ol
N-hydroxy-N-(2-hydroxynaphthalen-1-yl)acetamide + CO2
-
-
-
?
pyruvate + 2-hydroxy-4,6-dinitrobenzaldehyde
? + CO2
-
-
-
?
pyruvate + 3,5-dimethyl-4-nitroso-1-(propan-2-yl)-1H-pyrazole
N-[3,5-dimethyl-1-(propan-2-yl)-1H-pyrazol-4-yl]-N-hydroxyacetamide + CO2
-
-
-
?
pyruvate + 6-bromo-1-nitrosonaphthalen-2-ol
N-(6-bromo-2-hydroxynaphthalen-1-yl)-N-hydroxyacetamide + CO2
-
-
-
?
pyruvate + 6-hydroxy-5-nitrosonaphthalene-2-sulfonamide
N-hydroxy-N-(2-hydroxy-6-sulfamoylnaphthalen-1-yl)acetamide + CO2
-
-
-
?
pyruvate + 7-methoxy-1-nitrosonaphthalen-2-ol
N-hydroxy-N-(2-hydroxy-7-methoxynaphthalen-1-yl)acetamide + CO2
-
-
-
?
pyruvate + D-erythrose
1-deoxy-D-fructose + CO2
-
17% of the activity with D-glyceraldehyde
-
-
?
pyruvate + D-erythrose 4-phosphate
1-deoxy-D-fructose 6-phosphate + CO2
pyruvate + D-glyceraldehyde
1-deoxy-D-xylulose + CO2
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
pyruvate + D-ribose 5-phosphate
1-deoxy-D-sedoheptulose 7-phosphate + CO2
pyruvate + DL-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
pyruvate + glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
pyruvate + glycolaldehyde
1-deoxy-L-erythrulose + CO2
-
71% of the activity with D-glyceraldehyde
-
-
?
pyruvate + L-glyceraldehyde
1-deoxy-D-xylulose + CO2
-
-
-
-
?
pyruvate + N,N-dimethyl-4-nitrosoaniline
N-[4-(dimethylamino)phenyl]-N-hydroxyacetamide + CO2
-
-
-
?
pyruvate + nitrosobenzene
? + CO2
-
-
-
?
pyruvate + nitrosobenzene
N-hydroxy-N-phenylacetamide + CO2
-
-
-
?
additional information
?
-
pyruvate + D-erythrose 4-phosphate
1-deoxy-D-fructose 6-phosphate + CO2
-
-
-
-
?
pyruvate + D-erythrose 4-phosphate
1-deoxy-D-fructose 6-phosphate + CO2
-
84% of the activity with D-glyceraldehyde
-
-
?
pyruvate + D-erythrose 4-phosphate
1-deoxy-D-fructose 6-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde
1-deoxy-D-xylulose + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde
1-deoxy-D-xylulose + CO2
-
-
-
?
pyruvate + D-glyceraldehyde
1-deoxy-D-xylulose + CO2
-
the reaction product, 1-deoxy-D-xylulose 5-phosphate, is a precursor to isoprenoids and vitamins
-
-
?
pyruvate + D-glyceraldehyde
1-deoxy-D-xylulose + CO2
-
as active as D-glyceraldehyde 3-phosphate
-
-
?
pyruvate + D-glyceraldehyde
1-deoxy-D-xylulose + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde
1-deoxy-D-xylulose + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde
1-deoxy-D-xylulose + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
plastidic isoprenoid synthesis in plants, catalyses one of the rate-limiting steps
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
the enzyme expression is decreased during degreening and natural color break, which is delayed by gibberellin and nitrate, 2C-methyl-D-erythritol-4-phosphate, MEP, pathway and regulation, as part of the plastidial isoprenoid pathway, overview
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
the enzyme is crucial in the isoprenoid pathway, catalyzing the first step of the 2C-methyl-D-erythritol-4-phosphate, MEP, DXS is also a crucial enzyme for the biosynthesis of isopentenyl diphosphate, thiamine, and pyridoxol
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
the enzyme is involved in the 2C-methyl-D-erythritol-4-phosphate, MEP, pathway performing the initial step
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
the enzyme is crucial in the isoprenoid pathway, catalyzing the first step of the 2C-methyl-D-erythritol-4-phosphate, MEP, DXS is also a crucial enzyme for the biosynthesis of isopentenyl diphosphate, thiamine, and pyridoxol
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
the enzyme is important in the plastidic pathway of isoprenoid biosynthesis, including the 2C-methyl-D-erythritol-4-phosphate, MEP, pathway, in plants and shows a regulatory role catalyzing the initial step, overview
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
D-glyceraldehyde and pyruvate bind reversibly and independently
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
the enzyme catalyzes the first committed step in the 2C-methyl-D-erythritol-4-phosphate, MEP, pathway which leads to the biosynthesis of gingkolides, in which the enzyme expression level might play a regulatory role
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
the enzyme catalyzes the first committed step in the 2C-methyl-D-erythritol-4-phosphate, MEP, pathway which leads to the biosynthesis of gingkolides, overview, gingkolides are synthesized in roots and then translocated to the leaves
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
the enzyme is involved in the plastidial 2C-methyl-D-erythritol-4-phosphate, MEP, pathway and plays a crucial role in monoterpene precursor biosynthesis for the production of essential oils in leaves and flowers, overview
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
potential importance of DXS1 in many housekeeping functions, hypothetical role of DXS2 in the biosynthesis of secondary isoprenoids
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
the enzyme catalyzes the first step of the methyl-D-erythritol 4-phosphate pathway. Antraquinone biosynthesis is regulated at the transcriptional level of the DXS gene
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
the enzyme catalyzes the first step in the 2C-methyl-D-erythritol-4-phosphate, MEP, pathway, with differential expression of genes dxs1, dxs2, and dxs3, overview
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-ribose 5-phosphate
1-deoxy-D-sedoheptulose 7-phosphate + CO2
-
-
-
-
?
pyruvate + D-ribose 5-phosphate
1-deoxy-D-sedoheptulose 7-phosphate + CO2
-
-
-
-
?
pyruvate + DL-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + DL-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
additional information
?
-
-
no activity with D-glucose 6-phosphate, D-galactose 6-phosphate and free aldoses such as D-threose, D-xylose, D-arabinose or D-glucose
-
-
?
additional information
?
-
gingkolides are diterpenoids and potent platelet-activating factor antagonists
-
-
?
additional information
?
-
-
gingkolides are diterpenoids and potent platelet-activating factor antagonists
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pyruvate + D-glyceraldehyde
1-deoxy-D-xylulose + CO2
-
the reaction product, 1-deoxy-D-xylulose 5-phosphate, is a precursor to isoprenoids and vitamins
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
additional information
?
-
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
plastidic isoprenoid synthesis in plants, catalyses one of the rate-limiting steps
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
the enzyme expression is decreased during degreening and natural color break, which is delayed by gibberellin and nitrate, 2C-methyl-D-erythritol-4-phosphate, MEP, pathway and regulation, as part of the plastidial isoprenoid pathway, overview
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
the enzyme is crucial in the isoprenoid pathway, catalyzing the first step of the 2C-methyl-D-erythritol-4-phosphate, MEP, DXS is also a crucial enzyme for the biosynthesis of isopentenyl diphosphate, thiamine, and pyridoxol
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
the enzyme is involved in the 2C-methyl-D-erythritol-4-phosphate, MEP, pathway performing the initial step
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
the enzyme is crucial in the isoprenoid pathway, catalyzing the first step of the 2C-methyl-D-erythritol-4-phosphate, MEP, DXS is also a crucial enzyme for the biosynthesis of isopentenyl diphosphate, thiamine, and pyridoxol
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
the enzyme is important in the plastidic pathway of isoprenoid biosynthesis, including the 2C-methyl-D-erythritol-4-phosphate, MEP, pathway, in plants and shows a regulatory role catalyzing the initial step, overview
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
the enzyme catalyzes the first committed step in the 2C-methyl-D-erythritol-4-phosphate, MEP, pathway which leads to the biosynthesis of gingkolides, in which the enzyme expression level might play a regulatory role
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
the enzyme catalyzes the first committed step in the 2C-methyl-D-erythritol-4-phosphate, MEP, pathway which leads to the biosynthesis of gingkolides, overview, gingkolides are synthesized in roots and then translocated to the leaves
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
the enzyme is involved in the plastidial 2C-methyl-D-erythritol-4-phosphate, MEP, pathway and plays a crucial role in monoterpene precursor biosynthesis for the production of essential oils in leaves and flowers, overview
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
potential importance of DXS1 in many housekeeping functions, hypothetical role of DXS2 in the biosynthesis of secondary isoprenoids
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
the enzyme catalyzes the first step of the methyl-D-erythritol 4-phosphate pathway. Antraquinone biosynthesis is regulated at the transcriptional level of the DXS gene
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
the enzyme catalyzes the first step in the 2C-methyl-D-erythritol-4-phosphate, MEP, pathway, with differential expression of genes dxs1, dxs2, and dxs3, overview
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
1-deoxy-D-xylulose 5-phosphate + CO2
-
-
-
-
?
additional information
?
-
gingkolides are diterpenoids and potent platelet-activating factor antagonists
-
-
?
additional information
?
-
-
gingkolides are diterpenoids and potent platelet-activating factor antagonists
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(1E,1'E)-O,O'-(ethane-1,2-diyl)bis[2,4,5-trihydroxybenzaldehyde oxime]
-
-
(1E,7E)-1-(2,4,5-trihydroxyphenyl)-3,6-dioxa-2,7-diazanona-1,7-dien-9-oate
-
-
(2R)-2-(4-[2-[(acetylphosphinato)oxy]ethyl]-1H-1,2,3-triazol-1-yl)-3-(4-hydroxyphenyl)propanoate
-
-
(2R)-2-(4-[2-[(acetylphosphinato)oxy]ethyl]-1H-1,2,3-triazol-1-yl)-3-phenylpropanoate
-
most potent selective inhibitor
(2R)-2-(4-[2-[(acetylphosphinato)oxy]ethyl]-1H-1,2,3-triazol-1-yl)propanoate
-
-
(2S)-2-(4-[2-[(acetylphosphinato)oxy]ethyl]-1H-1,2,3-triazol-1-yl)-3-(4-hydroxyphenyl)propanoate
-
-
(2S)-2-(4-[2-[(acetylphosphinato)oxy]ethyl]-1H-1,2,3-triazol-1-yl)-3-phenylpropanoate
-
-
(2S)-2-(4-[2-[(acetylphosphinato)oxy]ethyl]-1H-1,2,3-triazol-1-yl)propanoate
-
-
(E)-2,4,5-trihydroxybenzaldehyde O-benzyl oxime
-
-
(E)-2,4,5-trihydroxybenzaldehyde O-methyl oxime
-
-
(E)-2,4,5-trihydroxybenzaldehyde oxime
-
-
(E)-2,4-dihydroxybenzaldehyde O-methyl oxime
-
-
(E)-2,5-dihydroxybenzaldehyde O-methyl oxime
-
-
(E)-2-fluoro-4,5-dihydroxybenzaldehyde O-methyl oxime
-
-
(E)-2-fluoro-4,5-dimethoxybenzaldehyde O-methyl oxime
-
-
(E)-2-hydroxy-3-nitrobenzaldehyde O-methyl oxime
-
-
(E)-2-hydroxybenzaldehyde O-methyl oxime
-
-
(E)-3,4,5-trihydroxybenzaldehyde O-methyl oxime
-
-
(E)-3,4-dihydroxy-5-methoxybenzaldehyde O-methyl oxime
-
-
(E)-4,5-difluoro-2-hydroxybenzaldehyde O-methyl oxime
-
-
(E)-4-hydroxy-3-nitrobenzaldehyde O-methyl oxime
-
-
(E)-5-[(2-methylhydrazono)methyl]benzene-1,2,4-triol
-
-
(E)-uracil-6-carbaldehyde O-methyl oxime
-
-
(E,Z)-2,4,5-trimethoxybenzaldehyde O-methyl oxime
-
-
(E,Z)-3,4-dihydroxybenzaldehyde O-methyl oxime
-
-
1-deoxy-D-xylulose 5-phosphate
competitive inhibition with respect to pyruvate, non-competitive inhibition with respect to D-glyceraldehyde 3-phosphate
1-methyl-2-nitrosobenzene
weak inhibitory activity
1-nitrosonaphthalen-2-ol
weak inhibitory activity
2,3-diphospho-D-glyceric acid
-
0.1 mM, 50% inhibition
2-(1-benzyl-1H-1,2,3-triazol-4-yl)ethyl acetylphosphonate
-
-
2-(1-cyclohexyl-1H-1,2,3-triazol-4-yl)ethyl acetylphosphonate
-
-
2-(1-pentyl-1H-1,2,3-triazol-4-yl)ethyl acetylphosphonate
-
-
2-(1-[(2S)-1-[methyl(4-methylbenzene-1-sulfonyl)amino]-1-oxo-3-phenylpropan-2-yl]-1H-1,2,3-triazol-4-yl)ethyl acetylphosphonate
-
-
2-(1-[2-[methyl(methylsulfonyl)amino]-2-oxoethyl]-1H-1,2,3-triazol-4-yl)ethyl acetylphosphonate
-
-
2-methyl-3,5-diphenyl-6-propylpyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
2-methyl-3,5-diphenylpyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
2-methyl-5-naphthalen-2-yl-3-phenylpyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
2-[1-(2-hydroxyethyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
-
2-[1-(2-hydroxyphenyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
-
2-[1-(2-methoxy-2-oxoethyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
-
2-[1-(2-nitrobenzyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
-
2-[1-(2-phenylethyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
-
2-[1-(2-[methyl[(4-methylphenyl)sulfonyl]amino]-2-oxoethyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
-
2-[1-(3-hydroxyphenyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
-
2-[1-(4-hydroxyphenyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
-
2-[1-(4-nitrobenzyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
-
2-[1-(carboxymethyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
-
2-[1-(prop-2-en-1-yl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
-
2-[1-[4-(methoxycarbonyl)benzyl]-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
-
3,5-bis(4-methoxyphenyl)-2-methylpyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
3,5-dimethyl-4-nitroso-1-(propan-2-yl)-1H-pyrazole
weak inhibitory activity
3,5-diphenyl-2-(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
3-(4-bromophenyl)-5-(2-methoxyphenyl)-2-methylpyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
3-(4-bromophenyl)-5-methyl-2-(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
3-(4-chlorophenyl)-2-ethyl-5-(4-methoxyphenyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
3-(4-chlorophenyl)-2-methyl-5-phenylpyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
3-(4-chlorophenyl)-2-methyl-5-[[(1-phenyl-1H-tetrazol-5-yl)sulfanyl]methyl]pyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
3-(4-chlorophenyl)-5-(4-methoxyphenyl)-2-methylpyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
3-(4-chlorophenyl)-5-(methoxymethyl)-2-methylpyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
3-(4-chlorophenyl)-5-(methoxymethyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
3-(4-chlorophenyl)-5-methyl-2-(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
3-(4-chlorophenyl)-5-methylpyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
3-(4-chlorophenyl)-5-[[(4-chlorophenyl)sulfanyl]methyl]-2-methylpyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
3-(4-fluorophenyl)-5-(4-methoxyphenyl)-2-methylpyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
3-(4-methoxyphenyl)-2-methyl-5-phenylpyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
3-(4-methoxyphenyl)-5-phenyl-2-(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
3-Fluoropyruvate
competitive with respect to pyruvate
5-(chloromethyl)-3-phenylpyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
5-benzyl-3-(4-chlorophenyl)-2-(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
5-benzyl-3-(4-chlorophenyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
5-benzyl-3-phenyl-2-(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
5-[(methoxyamino)methyl]benzene-1,2,4-triol
-
-
5-[[(4-chlorophenyl)sulfanyl]methyl]-2-methyl-3-phenylpyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
6-benzyl-3-(4-chlorophenyl)-5-methyl-2-(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
-
-
6-bromo-1-nitrosonaphthalen-2-ol
weak inhibitory activity
6-hydroxy-5-nitrosonaphthalene-2-sulfonamide
weak inhibitory activity
7-methoxy-1-nitrosonaphthalen-2-ol
weak inhibitory activity
beta-Glycerophosphate
-
0.3 mM, 40% inhibition
butyl acetyl phosphonate
-
-
butylacetylphosphonate
-
-
D-3-phosphoglyceric acid
-
0.16 mM, 23% inhibition
D-glyceraldehyde
-
competitive inhibition with respect to pyruvate
D-glyceraldehyde 3-phosphate
-
substrate inhibition
dimethylallyl diphosphate
-
competitive inhibitor
DL-alpha-glycerophosphate
-
0.29 mM, 50% inhibition
ethyl (5-methyl-7-oxo-3-phenyl-4,7-dihydropyrazolo[1,5-a]pyrimidin-6-yl)acetate
-
-
ethyl acetylphosphonate
-
-
Fluoropyruvate
-
recombinant protein, 50% inhibition at 0.4 mM, fluoropyruvate is supposed to bind covalently to the active site
hexyl acetylphosphonate
-
-
isopentenyl diphosphate
-
competitive inhibitor
isopropylacetylphosphonate
-
weak inhibition
lithium but-3-yn-1-yl acetylphosphonate
-
-
methyl acetylphosphonate
-
-
methyl [3-(4-bromophenyl)-7-oxo-2-(trifluoromethyl)-4,7-dihydropyrazolo[1,5-a]pyrimidin-5-yl]acetate
-
-
N,N-dimethyl-4-nitrosoaniline
weak inhibitory activity
nitrosobenzene
weak inhibitory activity
octyl acetylphosphonate
-
-
pentyl acetylphosphonate
-
-
phosphonoacetohydroxamate
-
0.1 mM, 25% inhibition
phosphonopropionohydroxamate
-
0.1 mM, 10% inhibition
propyl acetylphosphonate
-
-
pyruvate
-
substrate inhibition
3-fluoro-2-oxopropanoate
-
competitive inhibition with respect to pyruvate
3-fluoro-2-oxopropanoate
-
competitive inhibition with respect to pyruvate
3-fluoro-2-oxopropanoate
-
competitive, 0.1 mM, up to 57% inhibition
benzylacetylphosphonate
competitive inhibitor
benzylacetylphosphonate
-
-
beta-fluoropyruvate
competitive inhibition with respect to pyruvate, non-competitive inhibition with respect to D-glyceraldehyde 3-phosphate
beta-fluoropyruvate
-
dead-end inhibitor for pyruvate
EDTA
completely active after dialysis against EDTA. Incubation of the enzyme with saturated ammonium sulfate and 5.0mM EDTA at pH 3.5 leads to the complete loss of DXScc activity, with only a 25% recovery of activity upon the addition of Mg(II)
EDTA
-
recombinant protein
Methylacetylphosphonate
-
-
Methylacetylphosphonate
-
competitive inhibition with respect to pyruvate
Methylacetylphosphonate
-
competitive inhibition with respect to pyruvate
additional information
protein is feedback regulated in response to the inhibition of the pathway flow; protein is feedback regulated in response to the inhibition of the pathway flow
-
additional information
protein is feedback regulated in response to the inhibition of the pathway flow; protein is feedback regulated in response to the inhibition of the pathway flow
-
additional information
-
protein is feedback regulated in response to the inhibition of the pathway flow; protein is feedback regulated in response to the inhibition of the pathway flow
-
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0.099
1-methyl-2-nitrosobenzene
at pH 8.0 and 37°C
0.041
1-nitrosonaphthalen-2-ol
at pH 8.0 and 37°C
0.512
2-hydroxy-4,6-dinitrobenzaldehyde
at pH 8.0 and 37°C
0.387
3,5-dimethyl-4-nitroso-1-(propan-2-yl)-1H-pyrazole
at pH 8.0 and 37°C
0.024
6-bromo-1-nitrosonaphthalen-2-ol
at pH 8.0 and 37°C
0.018
6-hydroxy-5-nitrosonaphthalene-2-sulfonamide
at pH 8.0 and 37°C
0.063
7-methoxy-1-nitrosonaphthalen-2-ol
at pH 8.0 and 37°C
0.12
D-erythrose 4-phosphate
-
pH 7.9, 37°C
5.6 - 38
D-glyceraldehyde
0.0015 - 12
D-glyceraldehyde 3-phosphate
4.5
L-glyceraldehyde
-
pH 7.9, 37°C
0.054
N,N-dimethyl-4-nitrosoaniline
at pH 8.0 and 37°C
5.6
D-glyceraldehyde
-
pH 7.9, 37°C
10
D-glyceraldehyde
-
recombinant isoenzyme B
14
D-glyceraldehyde
-
recombinant isoenzyme A
33
D-glyceraldehyde
-
pH 7.4, 37°C
35
D-glyceraldehyde
-
recombinant protein
0.0015
D-glyceraldehyde 3-phosphate
-
apparent value, mutant enzyme H299N, at pH 8.0 and 25-28°C
0.0016
D-glyceraldehyde 3-phosphate
-
mutant enzyme R478A, at pH 8.0 and 37°C
0.0033
D-glyceraldehyde 3-phosphate
-
apparent value, mutant enzyme H299A, at pH 8.0 and 25-28°C
0.0061
D-glyceraldehyde 3-phosphate
-
pH 7.9, 37°C
0.0142
D-glyceraldehyde 3-phosphate
-
apparent value, wild type enzyme, at pH 8.0 and 25-28°C
0.016
D-glyceraldehyde 3-phosphate
-
apparent value, at pH 7.0 and 37°C
0.0162
D-glyceraldehyde 3-phosphate
-
apparent value, mutant enzyme H49A, at pH 8.0 and 25-28°C
0.0185
D-glyceraldehyde 3-phosphate
-
at pH 8.0 and 37°C
0.019
D-glyceraldehyde 3-phosphate
pH and temperature not specified in the publication
0.023
D-glyceraldehyde 3-phosphate
-
pH 8.0, 37°C
0.0232
D-glyceraldehyde 3-phosphate
-
0.0235
D-glyceraldehyde 3-phosphate
-
wild type enzyme, at pH 8.0 and 37°C
0.026
D-glyceraldehyde 3-phosphate
-
apparent value, at pH 7.0 and 37°C
0.029
D-glyceraldehyde 3-phosphate
-
apparent value, mutant enzyme H49N, at pH 8.0 and 25-28°C
0.03
D-glyceraldehyde 3-phosphate
apparent value, mutant enzyme H82A, at pH 8.0 and 37°C
0.03
D-glyceraldehyde 3-phosphate
apparent value, mutant enzyme N181A, at pH 8.0 and 37°C
0.03
D-glyceraldehyde 3-phosphate
mutant enzyme H82A, at pH 8.0 and 37°C
0.042
D-glyceraldehyde 3-phosphate
-
wild type enzyme, at pH 8.0 and 37°C
0.05
D-glyceraldehyde 3-phosphate
wild type enzyme, at pH 8.0 and 37°C
0.05
D-glyceraldehyde 3-phosphate
apparent value, wild type enzyme, at pH 8.0 and 37°C
0.054
D-glyceraldehyde 3-phosphate
-
pH and temperature not specified in the publication
0.068
D-glyceraldehyde 3-phosphate
-
pH 7.4, 37°C
0.08
D-glyceraldehyde 3-phosphate
apparent value, mutant enzyme H304A, at pH 8.0 and 37°C
0.08
D-glyceraldehyde 3-phosphate
mutant enzyme H304A, at pH 8.0 and 37°C
0.12
D-glyceraldehyde 3-phosphate
-
recombinant protein
0.12
D-glyceraldehyde 3-phosphate
-
recombinant isoenzyme B
0.12
D-glyceraldehyde 3-phosphate
apparent value, mutant enzyme D430A, at pH 8.0 and 37°C
0.12
D-glyceraldehyde 3-phosphate
mutant enzyme D430A, at pH 8.0 and 37°C
0.15
D-glyceraldehyde 3-phosphate
-
recombinant isoenzyme A
0.158
D-glyceraldehyde 3-phosphate
-
pH 8.5, 40°C
0.21
D-glyceraldehyde 3-phosphate
-
mutant enzyme Y392F, at pH 8.0 and 37°C
0.226
D-glyceraldehyde 3-phosphate
-
-
0.23
D-glyceraldehyde 3-phosphate
apparent value, mutant enzyme H434A, at pH 8.0 and 37°C
0.23
D-glyceraldehyde 3-phosphate
mutant enzyme H434A, at pH 8.0 and 37°C
0.24
D-glyceraldehyde 3-phosphate
-
0.47
D-glyceraldehyde 3-phosphate
pH 7.8, 32°C
0.59
D-glyceraldehyde 3-phosphate
apparent value, mutant enzyme Y395A, at pH 8.0 and 37°C
0.6
D-glyceraldehyde 3-phosphate
apparent value, mutant enzyme R423K, at pH 8.0 and 37°C
0.67
D-glyceraldehyde 3-phosphate
apparent value, wild type enzyme, at pH 8.0 and 37°C
0.87
D-glyceraldehyde 3-phosphate
pH 7.8, 32°C
1
D-glyceraldehyde 3-phosphate
pH 7.8, 32°C
1.67
D-glyceraldehyde 3-phosphate
-
mutant K284N, pH 8.0, 37°C
1.78
D-glyceraldehyde 3-phosphate
-
wild-type, pH 8.0, 37°C
2.3
D-glyceraldehyde 3-phosphate
-
mutant enzyme R478A, at pH 8.0 and 37°C
7.7
D-glyceraldehyde 3-phosphate
apparent value, mutant enzyme Y395F, at pH 8.0 and 37°C
12
D-glyceraldehyde 3-phosphate
apparent value, mutant enzyme R423A, at pH 8.0 and 37°C
0.0011
pyruvate
-
-
0.011
pyruvate
-
pH and temperature not specified in the publication
0.04
pyruvate
-
pH 7.9, 37°C
0.0442
pyruvate
-
apparent value, wild type enzyme, at pH 8.0 and 25-28°C
0.049
pyruvate
-
pH 8.0, 37°C
0.049
pyruvate
-
wild type enzyme, at pH 8.0 and 37°C
0.05
pyruvate
apparent value, mutant enzyme H434K, at pH 8.0 and 37°C
0.054
pyruvate
-
mutant enzyme R478A, at pH 8.0 and 37°C
0.06
pyruvate
apparent value, mutant enzyme R423K, at pH 8.0 and 37°C
0.065
pyruvate
-
recombinant protein
0.073
pyruvate
-
mutant enzyme Y392F, at pH 8.0 and 37°C
0.0878
pyruvate
-
at pH 8.0 and 37°C
0.107
pyruvate
DXR-coupled assay, at pH 8.0 and 37°C
0.111
pyruvate
-
pH 8.5, 40°C
0.123
pyruvate
HPLC method, at pH 8.0 and 37°C
0.16
pyruvate
apparent value, mutant enzyme Y395A, at pH 8.0 and 37°C
0.17
pyruvate
apparent value, mutant enzyme N181A, at pH 8.0 and 37°C
0.19
pyruvate
apparent value, mutant enzyme Y395F, at pH 8.0 and 37°C
0.23
pyruvate
apparent value, mutant enzyme H82A, at pH 8.0 and 37°C
0.23
pyruvate
mutant enzyme H82A, at pH 8.0 and 37°C
0.28
pyruvate
wild type enzyme, at pH 8.0 and 37°C
0.28
pyruvate
apparent value, wild type enzyme, at pH 8.0 and 37°C
0.44
pyruvate
-
pH 7.4, 37°C, cosubstrate: D-glyceraldehyde 3-phosphate
0.52
pyruvate
apparent value, mutant enzyme D430A, at pH 8.0 and 37°C
0.52
pyruvate
mutant enzyme D430A, at pH 8.0 and 37°C
0.585
pyruvate
-
mutant K284N, pH 8.0, 37°C
0.61
pyruvate
-
recombinant isoenzyme A, cosubstrate D-glyceraldehyde 3-phosphate
0.64
pyruvate
-
apparent value, at pH 7.0 and 37°C
0.661
pyruvate
-
wild-type, pH 8.0, 37°C
0.72
pyruvate
pH 7.8, 32°C
0.75
pyruvate
pH 7.8, 32°C
0.87
pyruvate
pH and temperature not specified in the publication
1.07
pyruvate
-
apparent value, mutant enzyme H49A, at pH 8.0 and 25-28°C
1.08
pyruvate
-
apparent value, mutant enzyme H299N, at pH 8.0 and 25-28°C
1.09
pyruvate
-
apparent value, at pH 7.0 and 37°C
1.1
pyruvate
-
apparent value, mutant enzyme H299A, at pH 8.0 and 25-28°C
1.61
pyruvate
-
apparent value, mutant enzyme H49N, at pH 8.0 and 25-28°C
1.7
pyruvate
apparent value, mutant enzyme H304A, at pH 8.0 and 37°C
1.7
pyruvate
mutant enzyme H304A, at pH 8.0 and 37°C
1.7
pyruvate
mutant enzyme H434A, at pH 8.0 and 37°C
1.8
pyruvate
pH 7.8, 32°C
1.9
pyruvate
-
pH 7.4, 37°C, cosubstrate: D-glyceraldehyde
3
pyruvate
-
recombinant isoenzyme B, cosubstrate D-glyceraldehyde 3-phosphate
4.3
pyruvate
-
recombinant isoenzyme A, cosubstrate D-glyceraldehyde
14
pyruvate
-
recombinant isoenzyme B, cosubstrate D-glyceraldehyde
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6
1-methyl-2-nitrosobenzene
at pH 8.0 and 37°C
0.045
1-nitrosonaphthalen-2-ol
at pH 8.0 and 37°C
0.06
3,5-dimethyl-4-nitroso-1-(propan-2-yl)-1H-pyrazole
at pH 8.0 and 37°C
1.3
6-bromo-1-nitrosonaphthalen-2-ol
at pH 8.0 and 37°C
1.1
6-hydroxy-5-nitrosonaphthalene-2-sulfonamide
at pH 8.0 and 37°C
0.35
7-methoxy-1-nitrosonaphthalen-2-ol
at pH 8.0 and 37°C
0.035
D-glyceraldehyde
-
-
0.03 - 570
D-glyceraldehyde 3-phosphate
0.28
N,N-dimethyl-4-nitrosoaniline
at pH 8.0 and 37°C
0.03
D-glyceraldehyde 3-phosphate
-
mutant enzyme R420A, at pH 8.0 and 37°C
0.14
D-glyceraldehyde 3-phosphate
apparent value, mutant enzyme R423A, at pH 8.0 and 37°C
2.3
D-glyceraldehyde 3-phosphate
-
mutant enzyme R478A, at pH 8.0 and 37°C
4.2
D-glyceraldehyde 3-phosphate
mutant enzyme H434A, at pH 8.0 and 37°C
5.8
D-glyceraldehyde 3-phosphate
apparent value, mutant enzyme Y395A, at pH 8.0 and 37°C
6.1
D-glyceraldehyde 3-phosphate
-
apparent value, at pH 7.0 and 37°C
6.6
D-glyceraldehyde 3-phosphate
mutant enzyme D430A, at pH 8.0 and 37°C
10
D-glyceraldehyde 3-phosphate
apparent value, mutant enzyme Y395F, at pH 8.0 and 37°C
10.8
D-glyceraldehyde 3-phosphate
-
apparent value, mutant enzyme H299N, at pH 8.0 and 25-28°C
11
D-glyceraldehyde 3-phosphate
apparent value, mutant enzyme H304A, at pH 8.0 and 37°C
11
D-glyceraldehyde 3-phosphate
apparent value, mutant enzyme R423K, at pH 8.0 and 37°C
11
D-glyceraldehyde 3-phosphate
mutant enzyme H304A, at pH 8.0 and 37°C
13
D-glyceraldehyde 3-phosphate
apparent value, mutant enzyme H82A, at pH 8.0 and 37°C
13
D-glyceraldehyde 3-phosphate
mutant enzyme H82A, at pH 8.0 and 37°C
13.67
D-glyceraldehyde 3-phosphate
-
-
14
D-glyceraldehyde 3-phosphate
apparent value, mutant enzyme N181A, at pH 8.0 and 37°C
15
D-glyceraldehyde 3-phosphate
-
apparent value, mutant enzyme H299A, at pH 8.0 and 25-28°C
15.1
D-glyceraldehyde 3-phosphate
-
mutant enzyme Y392F, at pH 8.0 and 37°C
18.8
D-glyceraldehyde 3-phosphate
-
apparent value, mutant enzyme H49N, at pH 8.0 and 25-28°C
27.3
D-glyceraldehyde 3-phosphate
-
apparent value, mutant enzyme H49A, at pH 8.0 and 25-28°C
42
D-glyceraldehyde 3-phosphate
apparent value, mutant enzyme H434A, at pH 8.0 and 37°C
66
D-glyceraldehyde 3-phosphate
apparent value, mutant enzyme D430A, at pH 8.0 and 37°C
95
D-glyceraldehyde 3-phosphate
-
apparent value, wild type enzyme, at pH 8.0 and 25-28°C
113.3
D-glyceraldehyde 3-phosphate
-
wild type enzyme, at pH 8.0 and 37°C
150
D-glyceraldehyde 3-phosphate
wild type enzyme, at pH 8.0 and 37°C
150
D-glyceraldehyde 3-phosphate
apparent value, wild type enzyme, at pH 8.0 and 37°C
240
D-glyceraldehyde 3-phosphate
-
apparent value, at pH 7.0 and 37°C
570
D-glyceraldehyde 3-phosphate
pH and temperature not specified in the publication
0.037
pyruvate
-
apparent value, mutant enzyme H299A, at pH 8.0 and 25-28°C
0.173
pyruvate
-
apparent value, mutant enzyme H299N, at pH 8.0 and 25-28°C
0.417
pyruvate
-
apparent value, mutant enzyme H49N, at pH 8.0 and 25-28°C
0.422
pyruvate
-
apparent value, mutant enzyme H49A, at pH 8.0 and 25-28°C
0.58
pyruvate
apparent value, mutant enzyme H304A, at pH 8.0 and 37°C
0.58
pyruvate
mutant enzyme H304A, at pH 8.0 and 37°C
0.59
pyruvate
apparent value, mutant enzyme H434K, at pH 8.0 and 37°C
1.7
pyruvate
apparent value, mutant enzyme H82A, at pH 8.0 and 37°C
1.7
pyruvate
mutant enzyme H82A, at pH 8.0 and 37°C
5.9
pyruvate
mutant enzyme H434A, at pH 8.0 and 37°C
6.5
pyruvate
-
apparent value, at pH 7.0 and 37°C
11
pyruvate
pH and temperature not specified in the publication
14
pyruvate
apparent value, mutant enzyme D430A, at pH 8.0 and 37°C
14
pyruvate
mutant enzyme D430A, at pH 8.0 and 37°C
16
pyruvate
apparent value, mutant enzyme Y395F, at pH 8.0 and 37°C
19
pyruvate
apparent value, mutant enzyme N181A, at pH 8.0 and 37°C
22
pyruvate
apparent value, mutant enzyme Y395A, at pH 8.0 and 37°C
26
pyruvate
wild type enzyme, at pH 8.0 and 37°C
26
pyruvate
apparent value, wild type enzyme, at pH 8.0 and 37°C
32.2
pyruvate
-
apparent value, wild type enzyme, at pH 8.0 and 25-28°C
53.3
pyruvate
-
wild type enzyme, at pH 8.0 and 37°C
65
pyruvate
apparent value, mutant enzyme R423K, at pH 8.0 and 37°C
110
pyruvate
-
wild-type, pH 8.0, 37°C
210
pyruvate
-
mutant K284N, pH 8.0, 37°C
250
pyruvate
-
apparent value, at pH 7.0 and 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.001
(1E,1'E)-O,O'-(ethane-1,2-diyl)bis[2,4,5-trihydroxybenzaldehyde oxime]
-
at pH 8.0 and 37°C
0.0184
(1E,7E)-1-(2,4,5-trihydroxyphenyl)-3,6-dioxa-2,7-diazanona-1,7-dien-9-oate
-
at pH 8.0 and 37°C
0.00033
(2R)-2-(4-[2-[(acetylphosphinato)oxy]ethyl]-1H-1,2,3-triazol-1-yl)-3-(4-hydroxyphenyl)propanoate
-
at pH 8.0 and 37°C
0.00009
(2R)-2-(4-[2-[(acetylphosphinato)oxy]ethyl]-1H-1,2,3-triazol-1-yl)-3-phenylpropanoate
-
at pH 8.0 and 37°C
0.0029
(2R)-2-(4-[2-[(acetylphosphinato)oxy]ethyl]-1H-1,2,3-triazol-1-yl)propanoate
-
at pH 8.0 and 37°C
0.001
(2S)-2-(4-[2-[(acetylphosphinato)oxy]ethyl]-1H-1,2,3-triazol-1-yl)-3-(4-hydroxyphenyl)propanoate
-
at pH 8.0 and 37°C
0.0021
(2S)-2-(4-[2-[(acetylphosphinato)oxy]ethyl]-1H-1,2,3-triazol-1-yl)-3-phenylpropanoate
-
at pH 8.0 and 37°C
0.0013
(2S)-2-(4-[2-[(acetylphosphinato)oxy]ethyl]-1H-1,2,3-triazol-1-yl)propanoate
-
at pH 8.0 and 37°C
0.0091
(E)-2,4,5-trihydroxybenzaldehyde O-benzyl oxime
-
at pH 8.0 and 37°C
0.0039
(E)-2,4,5-trihydroxybenzaldehyde O-methyl oxime
-
at pH 8.0 and 37°C
0.0026
(E)-2,4,5-trihydroxybenzaldehyde oxime
-
at pH 8.0 and 37°C
0.2
(E)-2,4-dihydroxybenzaldehyde O-methyl oxime
-
Ki above 0.2 mM, at pH 8.0 and 37°C
0.2
(E)-2,5-dihydroxybenzaldehyde O-methyl oxime
-
Ki above 0.2 mM, at pH 8.0 and 37°C
0.0151
(E)-2-fluoro-4,5-dihydroxybenzaldehyde O-methyl oxime
-
at pH 8.0 and 37°C
0.2
(E)-2-fluoro-4,5-dimethoxybenzaldehyde O-methyl oxime
-
Ki above 0.2 mM, at pH 8.0 and 37°C
0.0478
(E)-2-hydroxy-3-nitrobenzaldehyde O-methyl oxime
-
at pH 8.0 and 37°C
0.2
(E)-2-hydroxybenzaldehyde O-methyl oxime
-
Ki above 0.2 mM, at pH 8.0 and 37°C
0.0294
(E)-3,4,5-trihydroxybenzaldehyde O-methyl oxime
-
at pH 8.0 and 37°C
0.2
(E)-3,4-dihydroxy-5-methoxybenzaldehyde O-methyl oxime
-
Ki above 0.2 mM, at pH 8.0 and 37°C
0.2
(E)-4,5-difluoro-2-hydroxybenzaldehyde O-methyl oxime
-
Ki above 0.2 mM, at pH 8.0 and 37°C
0.2
(E)-4-hydroxy-3-nitrobenzaldehyde O-methyl oxime
-
Ki above 0.2 mM, at pH 8.0 and 37°C
0.075
(E)-5-[(2-methylhydrazono)methyl]benzene-1,2,4-triol
-
Ki above 0.075 mM, at pH 8.0 and 37°C
0.2
(E)-uracil-6-carbaldehyde O-methyl oxime
-
Ki above 0.2 mM, at pH 8.0 and 37°C
0.1
(E,Z)-2,4,5-trimethoxybenzaldehyde O-methyl oxime
-
Ki above 0.1 mM, at pH 8.0 and 37°C
0.2
(E,Z)-3,4-dihydroxybenzaldehyde O-methyl oxime
-
Ki above 0.2 mM, at pH 8.0 and 37°C
0.13 - 0.83
1-deoxy-D-xylulose 5-phosphate
0.008
2-(1-benzyl-1H-1,2,3-triazol-4-yl)ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.00044
2-(1-cyclohexyl-1H-1,2,3-triazol-4-yl)ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.003
2-(1-pentyl-1H-1,2,3-triazol-4-yl)ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.00083
2-(1-[(2S)-1-[methyl(4-methylbenzene-1-sulfonyl)amino]-1-oxo-3-phenylpropan-2-yl]-1H-1,2,3-triazol-4-yl)ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.00052
2-(1-[2-[methyl(methylsulfonyl)amino]-2-oxoethyl]-1H-1,2,3-triazol-4-yl)ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.001
2-[1-(2-hydroxyethyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.00011
2-[1-(2-hydroxyphenyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.0013
2-[1-(2-methoxy-2-oxoethyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.0054
2-[1-(2-nitrobenzyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.008
2-[1-(2-phenylethyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.00047
2-[1-(2-[methyl[(4-methylphenyl)sulfonyl]amino]-2-oxoethyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.00032
2-[1-(3-hydroxyphenyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.006
2-[1-(4-hydroxyphenyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.0027
2-[1-(4-nitrobenzyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.00084
2-[1-(carboxymethyl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.006
2-[1-(prop-2-en-1-yl)-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.008
2-[1-[4-(methoxycarbonyl)benzyl]-1H-1,2,3-triazol-4-yl]ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.035 - 0.043
3-fluoro-2-oxopropanoate
0.2
3-Fluoropyruvate
pH and temperature not specified in the publication
0.075
5-[(methoxyamino)methyl]benzene-1,2,4-triol
-
Ki above 0.075 mM, at pH 8.0 and 37°C
0.0104
benzylacetylphosphonate
at pH 8.0 and 37°C
0.0033 - 0.057
beta-fluoropyruvate
0.0056
butyl acetyl phosphonate
-
at pH 8.0 and 37°C
0.0026 - 0.0056
butylacetylphosphonate
3.2
D-glyceraldehyde
-
pH 8.0, 37°C
0.0813
dimethylallyl diphosphate
-
at pH 8.0 and 37°C
0.00671
ethyl acetylphosphonate
-
at pH 8.0 and 37°C
0.0089
hexyl acetylphosphonate
-
at pH 8.0 and 37°C
0.0654
isopentenyl diphosphate
-
at pH 8.0 and 37°C
0.075
ketoclomazone
-
at pH 8.0 and 37°C
0.00047
lithium but-3-yn-1-yl acetylphosphonate
-
at pH 8.0 and 37°C
0.001
methyl acetylphosphonate
-
at pH 8.0 and 37°C
0.00324 - 1.08
Methylacetylphosphonate
0.0014
octyl acetylphosphonate
-
at pH 8.0 and 37°C
0.0017
pentyl acetylphosphonate
-
at pH 8.0 and 37°C
0.0071
propyl acetylphosphonate
-
at pH 8.0 and 37°C
0.13
1-deoxy-D-xylulose 5-phosphate
inhibition with respect to pyruvate, at pH 8.0 and 37°C
0.83
1-deoxy-D-xylulose 5-phosphate
inhibition with respect to D-glyceraldehyde 3-phosphate, at pH 8.0 and 37°C
0.035
3-fluoro-2-oxopropanoate
-
apparent value, at pH 7.0 and 37°C
0.043
3-fluoro-2-oxopropanoate
-
apparent value, at pH 7.0 and 37°C
0.0033
beta-fluoropyruvate
inhibition with respect to pyruvate, at pH 8.0 and 37°C
0.057
beta-fluoropyruvate
inhibition with respect to D-glyceraldehyde 3-phosphate, at pH 8.0 and 37°C
0.0026
butylacetylphosphonate
-
at pH 8.0 and 37°C
0.0056
butylacetylphosphonate
-
at pH 8.0 and 37°C
0.00324
Methylacetylphosphonate
-
wild type enzyme, at pH 8.0 and 25-28°C
0.046
Methylacetylphosphonate
-
apparent value, at pH 7.0 and 37°C
0.075
Methylacetylphosphonate
-
apparent value, at pH 7.0 and 37°C
0.125
Methylacetylphosphonate
-
mutant enzyme H49A, at pH 8.0 and 25-28°C
0.167
Methylacetylphosphonate
-
mutant enzyme H49N, at pH 8.0 and 25-28°C
0.24
Methylacetylphosphonate
-
mutant enzyme H299N, at pH 8.0 and 25-28°C
1.08
Methylacetylphosphonate
-
mutant enzyme H299A, at pH 8.0 and 25-28°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.291
1-methyl-2-nitrosobenzene
Escherichia coli
at pH 8.0 and 37°C
1.065
1-nitrosonaphthalen-2-ol
Escherichia coli
at pH 8.0 and 37°C
0.0719
2-methyl-3,5-diphenyl-6-propylpyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.0306
2-methyl-3,5-diphenylpyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.0195
2-methyl-5-naphthalen-2-yl-3-phenylpyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.0424
3,5-bis(4-methoxyphenyl)-2-methylpyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
2
3,5-dimethyl-4-nitroso-1-(propan-2-yl)-1H-pyrazole
Escherichia coli
IC50 above 2.0 mM, at pH 8.0 and 37°C
0.023
3,5-diphenyl-2-(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.0535
3-(4-bromophenyl)-5-(2-methoxyphenyl)-2-methylpyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.2
3-(4-bromophenyl)-5-methyl-2-(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
value above
0.0197
3-(4-chlorophenyl)-2-ethyl-5-(4-methoxyphenyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.0342
3-(4-chlorophenyl)-2-methyl-5-phenylpyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.0551
3-(4-chlorophenyl)-2-methyl-5-[[(1-phenyl-1H-tetrazol-5-yl)sulfanyl]methyl]pyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.0109
3-(4-chlorophenyl)-5-(4-methoxyphenyl)-2-methylpyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.2
3-(4-chlorophenyl)-5-(methoxymethyl)-2-methylpyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
value above
0.2
3-(4-chlorophenyl)-5-(methoxymethyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
value above
0.0984
3-(4-chlorophenyl)-5-methyl-2-(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.2
3-(4-chlorophenyl)-5-methylpyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
value above
0.0411
3-(4-chlorophenyl)-5-[[(4-chlorophenyl)sulfanyl]methyl]-2-methylpyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.0106
3-(4-fluorophenyl)-5-(4-methoxyphenyl)-2-methylpyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.0907
3-(4-methoxyphenyl)-2-methyl-5-phenylpyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.0202 - 0.2
3-(4-methoxyphenyl)-5-phenyl-2-(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
0.2
5-(chloromethyl)-3-phenylpyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
value above
0.014
5-benzyl-3-(4-chlorophenyl)-2-(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.1141
5-benzyl-3-(4-chlorophenyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.0711
5-benzyl-3-phenyl-2-(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.0637
5-[[(4-chlorophenyl)sulfanyl]methyl]-2-methyl-3-phenylpyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.2
6-benzyl-3-(4-chlorophenyl)-5-methyl-2-(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
value above
0.522
6-bromo-1-nitrosonaphthalen-2-ol
Escherichia coli
at pH 8.0 and 37°C
0.354
6-hydroxy-5-nitrosonaphthalene-2-sulfonamide
Escherichia coli
at pH 8.0 and 37°C
2
7-methoxy-1-nitrosonaphthalen-2-ol
Escherichia coli
IC50 above 2.0 mM, at pH 8.0 and 37°C
0.2
ethyl (5-methyl-7-oxo-3-phenyl-4,7-dihydropyrazolo[1,5-a]pyrimidin-6-yl)acetate
Mycobacterium tuberculosis
-
value above
0.073
methyl [3-(4-bromophenyl)-7-oxo-2-(trifluoromethyl)-4,7-dihydropyrazolo[1,5-a]pyrimidin-5-yl]acetate
Mycobacterium tuberculosis
-
-
0.0018 - 10
Methylacetylphosphonate
0.844
N,N-dimethyl-4-nitrosoaniline
Escherichia coli
at pH 8.0 and 37°C
0.208
nitrosobenzene
Escherichia coli
at pH 8.0 and 37°C
0.0202
3-(4-methoxyphenyl)-5-phenyl-2-(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
-
0.2
3-(4-methoxyphenyl)-5-phenyl-2-(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-7(4H)-one
Mycobacterium tuberculosis
-
value above
0.0018
Methylacetylphosphonate
Escherichia coli
-
wild type enzyme, at pH 8.0 and 37°C
0.005
Methylacetylphosphonate
Escherichia coli
-
mutant enzyme R478A, at pH 8.0 and 37°C
0.01
Methylacetylphosphonate
Escherichia coli
-
wild type enzyme, in the presence of 0.08 mM pyruvate, at pH 8.0 and 25-28°C
0.0319
Methylacetylphosphonate
Escherichia coli
-
wild type enzyme, in the presence of 2 mM pyruvate, at pH 8.0 and 25-28°C
0.38
Methylacetylphosphonate
Escherichia coli
-
mutant enzyme H49A, in the presence of 0.08 mM pyruvate, at pH 8.0 and 25-28°C
0.52
Methylacetylphosphonate
Escherichia coli
-
mutant enzyme H49N, in the presence of 0.08 mM pyruvate, at pH 8.0 and 25-28°C
0.78
Methylacetylphosphonate
Escherichia coli
-
mutant enzyme H299N, in the presence of 0.08 mM pyruvate, at pH 8.0 and 25-28°C
1.06
Methylacetylphosphonate
Escherichia coli
-
mutant enzyme H49A, in the presence of 2 mM pyruvate, at pH 8.0 and 25-28°C
1.7
Methylacetylphosphonate
Escherichia coli
-
mutant enzyme H49N, in the presence of 2 mM pyruvate, at pH 8.0 and 25-28°C
2.84
Methylacetylphosphonate
Escherichia coli
-
mutant enzyme H299N, in the presence of 2 mM pyruvate, at pH 8.0 and 25-28°C
3.2
Methylacetylphosphonate
Escherichia coli
-
mutant enzyme H299A, in the presence of 0.08 mM pyruvate, at pH 8.0 and 25-28°C
10
Methylacetylphosphonate
Escherichia coli
-
mutant enzyme H299A, in the presence of 2 mM pyruvate, at pH 8.0 and 25-28°C
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Altincicek, B.; Hintz, M.; Sanderbrand, S.; Wiesner, J.; Beck, E.; Jomaa, H.
Tools for discovery of inhibitors of the 1-deoxy-D-xylulose 5-phosphate (DXP) synthase and DXP reductoisomerase: an approach with enzymes from the pathogenic bacterium Pseudomonas aeruginosa
FEMS Microbiol. Lett.
190
329-333
2000
Pseudomonas aeruginosa
brenda
Kuzuyama, T.; Takagi, M.; Takahashi, S.; Seto, H.
Cloning and characterization of 1-deoxy-D-xylulose 5-phosphate synthase from Streptomyces sp. strain CL190, which uses both the mevalonate and nonmevalonate pathways for isopentenyl diphosphate biosynthesis
J. Bacteriol.
182
891-897
2000
Streptomyces sp., Escherichia coli (P77488), Escherichia coli
brenda
Lois, L.M.; Campos, N.; Putra, S.R.; Danielsen, K.; Rohmer, M.; Boronat, A.
Cloning and characterization of a gene from Escherichia coli encoding a transketolase-like enzyme that catalyzes the synthesis of D-1-deoxyxylulose 5-phosphate, a common precursor for isoprenoid, thiamin, and pyridoxol biosynthesis
Proc. Natl. Acad. Sci. USA
95
2105-2110
1998
Escherichia coli (P77488)
brenda
Harker, M.; Bramley, P.M.
Expression of prokaryotic 1-deoxy-D-xylulose-5-phosphatases in Escherichia coli increases carotenoid and ubiquinone biosynthesis
FEBS Lett.
448
115-119
1999
Synechocystis sp., Bacillus subtilis, Bacillus subtilis PY79
brenda
Hahn, F.M.; Eubanks, L.M.; Testa, C.A.; Blagg, B.S.J.; Baker, J.A.; Poulter, C.D.
1-Deoxy-D-xylulose 5-phosphate synthase, the gene product of open reading frame (ORF) 2816 and ORF 2895 in Rhodobacter capsulatus
J. Bacteriol.
183
1-11
2001
Rhodobacter capsulatus
brenda
Estevez, J.M.; Cantero, A.; Reindl, A.; Reichler, S.; Leon, P.
1-Deoxy-D-xylulose-5-phosphate synthase, a limiting enzyme for plastidic isoprenoid biosynthesis in plants
J. Biol. Chem.
276
22901-22909
2001
Arabidopsis thaliana
brenda
Querol, J.; Rodriguez-Concepcion, M.; Boronat, A.; Imperial, S.
Essential role of residue H49 for activity of Escherichia coli 1-deoxy-D-xylulose 5-phosphate synthase, the enzyme catalyzing the first step of the 2-C-methyl-D-erythritol 4-phosphate pathway for isoprenoid synthesis
Biochem. Biophys. Res. Commun.
289
155-160
2001
Escherichia coli (P77488), Escherichia coli
brenda
Lois, L.M.; Rodriguez-Concepcion, M.; Gallego, F.; Campos, N.; Boronat, A.
Carotenoid biosynthesis during tomato fruit development: Regulatory role of 1-deoxy-D-xylulose 5-phosphate synthase
Plant J.
22
503-513
2000
Solanum lycopersicum
brenda
Lange, B.M.; Wildung, M.R.; McCaskill, D.; Croteau, R.
A family of transketolases that directs isoprenoid biosynthesis via a mevalonate-independent pathway
Proc. Natl. Acad. Sci. USA
95
2100-2104
1998
Mentha x piperita
brenda
Eubanks, L.M.; Poulter, C.D.
Rhodobacter capsulatus 1-deoxy-D-xylulose 5-phosphate synthase: steady-state kinetics and substrate binding
Biochemistry
42
1140-1149
2003
Rhodobacter capsulatus
brenda
Bailey, A.M.; Mahapatra, S.; Brennan, P.J.; Crick, D.C.
Identification, cloning, purification, and enzymatic characterization of Mycobacterium tuberculosis 1-deoxy-D-xylulose 5-phosphate synthase
Glycobiology
12
813-820
2002
Mycobacterium tuberculosis
brenda
Schrmann, M.; Schrmann, M.; Sprenger, G.A.
Fructose 6-phosphate aldolase and 1-deoxy-D-xylulose 5-phosphate synthase from Escherichia coli as tools in enzymatic synthesis of 1-deoxysugars
J. Mol. Catal. B
19-20
247-252
2002
Escherichia coli
-
brenda
Walter, M.H.; Hans, J.; Strack, D.
Two distantly related genes encoding 1-deoxy-d-xylulose 5-phosphate synthases: differential regulation in shoots and apocarotenoid-accumulating mycorrhizal roots
Plant J.
31
243-254
2002
Medicago truncatula
brenda
Han, Y.S.; Roytrakul, S.; Verberne, M.C.; van der Heijden, R.; Linthorst, H.J.M.; Verpoorte, R.
Cloning of a cDNA encoding 1-deoxy-D-xylulose 5-phosphate synthase from Morinda citrifolia and analysis of its expression in relation to anthraquinone accumulation
Plant Sci.
164
911-917
2003
Morinda citrifolia
-
brenda
Querol, J.; Grosdemange-Billiard, C.; Rohmer, M.; Boronat, A.; Imperial, S.
Enzymatic synthesis of 1-deoxysugar-phosphates using E. coli 1-deoxy-D-xylulose 5-phosphate synthase
Tetrahedron Lett.
43
8265-8268
2002
Escherichia coli
-
brenda
Kim, B.R.; Kim, S.U.; Chang, Y.J.
Differential expression of three 1-deoxy-D-xylulose-5-phosphate synthase genes in rice
Biotechnol. Lett.
27
997-1001
2005
Oryza sativa
brenda
Alos, E.; Cercos, M.; Rodrigo, M.J.; Zacarias, L.; Talon, M.
Regulation of color break in citrus fruits. Changes in pigment profiling and gene expression induced by gibberellins and nitrate, two ripening retardants
J. Agric. Food Chem.
54
4888-4895
2006
Citrus clementina
brenda
Xiang, S.; Usunow, G.; Lange, G.; Busch, M.; Tong, L.
Crystal structure of 1-deoxy-D-xylulose 5-phosphate synthase, a crucial enzyme for isoprenoids biosynthesis
J. Biol. Chem.
282
2676-2682
2007
Deinococcus radiodurans, Escherichia coli
brenda
Lee, J.K.; Oh, D.K.; Kim, S.Y.
Cloning and characterization of the dxs gene, encoding 1-deoxy-d-xylulose 5-phosphate synthase from Agrobacterium tumefaciens, and its overexpression in Agrobacterium tumefaciens
J. Biotechnol.
128
555-566
2007
Agrobacterium tumefaciens, Agrobacterium tumefaciens (Q5QKF8), Agrobacterium tumefaciens KCCM 10413
brenda
Morris, W.L.; Ducreux, L.J.; Hedden, P.; Millam, S.; Taylor, M.A.
Overexpression of a bacterial 1-deoxy-D-xylulose 5-phosphate synthase gene in potato tubers perturbs the isoprenoid metabolic network: implications for the control of the tuber life cycle
J. Exp. Bot.
57
3007-3018
2006
Escherichia coli
brenda
Munoz-Bertomeu, J.; Arrillaga, I.; Ros, R.; Segura, J.
Up-regulation of 1-deoxy-D-xylulose-5-phosphate synthase enhances production of essential oils in transgenic spike lavender
Plant Physiol.
142
890-900
2006
Lavandula latifolia, Arabidopsis thaliana (Q38854)
brenda
Khemvong, S.; Suvachittanont, W.
Molecular cloning and expression of a cDNA encoding 1-deoxy-D-xylulose-5-phosphate synthase from oil palm Elaeis guineensis Jacq.
Plant Sci.
169
571-578
2005
Elaeis guineensis (Q6IZE6), Elaeis guineensis (Q6PRU5)
brenda
Kim, S.; Kuzuyama, T.; Chang, Y.; Song, K.; Kim, S.
Identification of class 2 1-deoxy-D-xylulose 5-phosphate synthase and 1-deoxy-D-xylulose 5-phosphate reductoisomerase genes from Ginkgo biloba and their transcription in embryo culture with respect to ginkgolide biosynthesis
Planta Med.
72
234-240
2006
Ginkgo biloba (Q5J7B4), Ginkgo biloba
brenda
Gong, Y.F.; Liao, Z.H.; Guo, B.H.; Sun, X.F.; Tang, K.X.
Molecular cloning and expression profile analysis of Ginkgo biloba DXS gene encoding 1-deoxy-D-xylulose 5-phosphate synthase, the first committed enzyme of the 2-C-methyl-D-erythritol 4-phosphate pathway
Planta Med.
72
329-335
2006
Ginkgo biloba (Q5J5B3), Ginkgo biloba
brenda
Wungsintaweekul, J.; Sirisuntipong, T.; Kongduang, D.; Losuphanporn, T.; Ounaroon, A.; Tansakul, P.; De-Eknamkul, W.
Transcription profiles analysis of genes encoding 1-deoxy-D-xylulose 5-phosphate synthase and 2C-methyl-D-erythritol 4-phosphate synthase in plaunotol biosynthesis from Croton stellatopilosus
Biol. Pharm. Bull.
31
852-856
2008
Croton stellatopilosus (A7BKB8), Croton stellatopilosus
brenda
Seo, M.; Im, E.; Nam, J.; Kim, S.
Increase of CoQ10 production level by the coexpression of decaprenyl diphosphate synthase and 1-deoxy-D-xylulose 5-phosphate synthase isolated from Rhizobium radiobacter ATCC 4718 in recombinant Escherichia coli
J. Microbiol. Biotechnol.
17
1045-1048
2007
Agrobacterium tumefaciens (Q0GGQ3)
brenda
Zhang, M.; Li, K.; Zhang, C.; Gai, J.; Yu, D.
Identification and characterization of class 1 DXS gene encoding 1-deoxy-D: -xylulose-5-phosphate synthase, the first committed enzyme of the MEP pathway from soybean
Mol. Biol. Rep.
36
879-887
2008
Glycine max
brenda
Floss, D.S.; Hause, B.; Lange, P.R.; Kuester, H.; Strack, D.; Walter, M.H.
Knock-down of the MEP pathway isogene 1-deoxy-D-xylulose 5-phosphate synthase 2 inhibits formation of arbuscular mycorrhiza-induced apocarotenoids, and abolishes normal expression of mycorrhiza-specific plant marker genes
Plant J.
56
86-100
2008
Medicago truncatula
brenda
Phillips, M.A.; Walter, M.H.; Ralph, S.G.; Dabrowska, P.; Luck, K.; Uros, E.M.; Boland, W.; Strack, D.; Rodriguez-Concepcion, M.; Bohlmann, J.; Gershenzon, J.
Functional identification and differential expression of 1-deoxy-D-xylulose 5-phosphate synthase in induced terpenoid resin formation of Norway spruce (Picea abies)
Plant Mol. Biol.
65
243-257
2007
Picea abies
brenda
Cordoba, E.; Salmi, M.; Leon, P.
Unravelling the regulatory mechanisms that modulate the MEP pathway in higher plants
J. Exp. Bot.
60
2933-2943
2009
Escherichia coli, Ginkgo biloba, Solanum lycopersicum, Oryza sativa, Solanum tuberosum, Zea mays, Picea abies (A7LA00), Picea abies (A7LA01), Picea abies (A7LA02), Arabidopsis thaliana (Q38854), Medicago truncatula (Q8L692), Medicago truncatula (Q8L693)
brenda
Kim, Y.B.; Kim, S.M.; Kang, M.K.; Kuzuyama, T.; Lee, J.K.; Park, S.C.; Shin, S.C.; Kim, S.U.
Regulation of resin acid synthesis in Pinus densiflora by differential transcription of genes encoding multiple 1-deoxy-D-xylulose 5-phosphate synthase and 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase genes
Tree Physiol.
29
737-749
2009
Pinus densiflora (B9U4U0), Pinus densiflora (B9U4U6), Pinus densiflora
brenda
Mao, J.; Eoh, H.; He, R.; Wang, Y.; Wan, B.; Franzblau, S.G.; Crick, D.C.; Kozikowski, A.P.
Structure-activity relationships of compounds targeting mycobacterium tuberculosis 1-deoxy-D-xylulose 5-phosphate synthase
Bioorg. Med. Chem. Lett.
18
5320-5323
2008
Mycobacterium tuberculosis
brenda
Sitthithaworn, W.; Wungsintaweekul, J.; Sirisuntipong, T.; Charoonratana, T.; Ebizuka, Y.; De-Eknamkul, W.
Cloning and expression of 1-deoxy-d-xylulose 5-phosphate synthase cDNA from Croton stellatopilosus and expression of 2C-methyl-d-erythritol 4-phosphate synthase and geranylgeranyl diphosphate synthase, key enzymes of plaunotol biosynthesis
J. Plant Physiol.
167
292-300
2010
Croton stellatopilosus (A7BKB8), Croton stellatopilosus
brenda
Brammer, L.A.; Meyers, C.F.
Revealing substrate promiscuity of 1-deoxy-D-xylulose 5-phosphate synthase
Org. Lett.
11
4748-4751
2009
Escherichia coli
brenda
Battilana, J.; Costantini, L.; Emanuelli, F.; Sevini, F.; Segala, C.; Moser, S.; Velasco, R.; Versini, G.; Stella Grando, M.
The 1-deoxy-D: -xylulose 5-phosphate synthase gene co-localizes with a major QTL affecting monoterpene content in grapevine
Theor. Appl. Genet.
118
653-669
2009
Vitis vinifera
brenda
Quevedo, C.; Perassolo, M.; Alechine, E.; Corach, D.; Giulietti, A.M.; Talou, J.R.
Increasing anthraquinone production by overexpression of 1-deoxy-D: -xylulose-5-phosphate synthase in transgenic cell suspension cultures of Morinda citrifolia
Biotechnol. Lett.
32
997-1003
2010
Catharanthus roseus
brenda
Handa, S.; Ramamoorthya, D.; Spradlinga, T.J.; Guidaa, W.C.; Adamsb, J.H.; Bendinskasc, K.G.; Merkler, D.J.
Production of recombinant 1-deoxy-D-xylulose-5-phosphate synthase from Plasmodium vivax in Escherichia coli
FEBS Open Bio
3
124-129
2013
Plasmodium vivax (A5K817), Plasmodium vivax
brenda
Brammer, L.A.; Smith, J.M.; Wade, H.; Meyers, C.F.
1-Deoxy-D-xylulose 5-phosphate synthase catalyzes a novel random sequential mechanism
J. Biol. Chem.
286
36522-36531
2011
Escherichia coli
brenda
Cordoba, E.; Porta, H.; Arroyo, A.; San Roman, C.; Medina, L.; Rodriguez-Concepcion, M.; Leon, P.
Functional characterization of the three genes encoding 1-deoxy-D-xylulose 5-phosphate synthase in maize
J. Exp. Bot.
62
2023-2038
2011
Zea mays (Q58HB2), Zea mays (Q58I01), Zea mays
brenda
Battilana, J.; Emanuelli, F.; Gambino, G.; Gribaudo, I.; Gasperi, F.; Boss, P.K.; Grando, M.S.
Functional effect of grapevine 1-deoxy-D-xylulose 5-phosphate synthase substitution K284N on Muscat flavour formation
J. Exp. Bot.
62
5497-5508
2011
Vitis vinifera
brenda
Yang, J.; Adhikari, M.; Liu, H.; Xu, H.; He, G.; Zhan, R.; Wei, J.; Chen, W.
Characterization and functional analysis of the genes encoding 1-deoxy-D-xylulose-5-phosphate reductoisomerase and 1-deoxy-D-xylulose-5-phosphate synthase, the two enzymes in the MEP pathway, from Amomum villosum Lour
Mol. Biol. Rep.
39
8287-8296
2012
Wurfbainia villosa (C6G1Y5), Wurfbainia villosa
brenda
Ghirardo, A.; Zimmer, I.; Brueggemann, N.; Schnitzler, J.P.
Analysis of 1-deoxy-D-xylulose 5-phosphate synthase activity in Grey poplar leaves using isotope ratio mass spectrometry
Phytochemistry
71
918-922
2010
Populus tremula x Populus alba
brenda
Matsushima, D.; Jenke-Kodama, H.; Sato, Y.; Fukunaga, Y.; Sumimoto, K.; Kuzuyama, T.; Matsunaga, S.; Okada, S.
The single cellular green microalga Botryococcus braunii, race B possesses three distinct 1-deoxy-D-xylulose 5-phosphate synthases
Plant Sci.
185-186
309-320
2012
Botryococcus braunii (H5ZXI0), Botryococcus braunii (H5ZXI1), Botryococcus braunii
brenda
Gupta, P.; Agarwal, A.; Akhtar, N.; Sangwan, R.; Singh, S.; Trivedi, P.
Cloning and characterization of 2-C-methyl-D-erythritol-4-phosphate pathway genes for isoprenoid biosynthesis from Indian ginseng, Withania somnifera
Protoplasma
250
285-295
2013
Withania somnifera (I1YA59), Withania somnifera
brenda
Kirby, J.; Nishimoto, M.; Chow, R.W.; Baidoo, E.E.; Wang, G.; Martin, J.; Schackwitz, W.; Chan, R.; Fortman, J.L.; Keasling, J.D.
Enhancing terpene yield from sugars via novel routes to 1-deoxy-D-xylulose 5-phosphate
Appl. Environ. Microbiol.
81
130-138
2015
Escherichia coli (P77735), Escherichia coli, Escherichia coli MG1655 (P77735)
brenda
Morris, F.; Vierling, R.; Boucher, L.; Bosch, J.; Freel Meyers, C.L.
DXP synthase-catalyzed C-N bond formation: nitroso substrate specificity studies guide selective inhibitor design
ChemBioChem
14
1309-1315
2013
Escherichia coli (P77488), Escherichia coli
brenda
Bartee, D.; Morris, F.; Al-Khouja, A.; Freel Meyers, C.L.
Hydroxybenzaldoximes are D-GAP-competitive inhibitors of E. coli 1-deoxy-D-xylulose-5-phosphate synthase
ChemBioChem
16
1771-1781
2015
Escherichia coli
brenda
Brammer Basta, L.A.; Patel, H.; Kakalis, L.; Jordan, F.; Freel Meyers, C.L.
Defining critical residues for substrate binding to 1-deoxy-D-xylulose 5-phosphate synthase: active site substitutions stabilize the predecarboxylation intermediate C2alpha-lactylthiamin diphosphate
FEBS J.
281
2820-2837
2014
Deinococcus radiodurans
brenda
Banerjee, A.; Wu, Y.; Banerjee, R.; Li, Y.; Yan, H.; Sharkey, T.D.
Feedback inhibition of deoxy-D-xylulose-5-phosphate synthase regulates the methylerythritol 4-phosphate pathway
J. Biol. Chem.
288
16926-16936
2013
Populus trichocarpa
brenda
Kudoh, K.; Kawano, Y.; Hotta, S.; Sekine, M.; Watanabe, T.; Ihara, M.
Prerequisite for highly efficient isoprenoid production by cyanobacteria discovered through the over-expression of 1-deoxy-D-xylulose 5-phosphate synthase and carbon allocation analysis
J. Biosci. Bioeng.
118
20-28
2014
Synechocystis sp. (P73067), Synechocystis sp.
brenda
Mendoza-Poudereux, I.; Munoz-Bertomeu, J.; Arrillaga, I.; Segura, J.
Deoxyxylulose 5-phosphate reductoisomerase is not a rate-determining enzyme for essential oil production in spike lavender
J. Plant Physiol.
171
1564-1570
2014
Lavandula latifolia
brenda
Li, H.; Ma, D.; Jin, Y.; Tu, Y.; Liu, L.; Leng, C.; Dong, J.; Wang, T.
Helper component-proteinase enhances the activity of 1-deoxy-D-xylulose-5-phosphate synthase and promotes the biosynthesis of plastidic isoprenoids in Potato virus Y-infected tobacco
Plant Cell Environ.
38
2023-2034
2015
Nicotiana tabacum (D2CS41)
brenda
Xu, Y.; Liu, J.; Liang, L.; Yang, X.; Zhang, Z.; Gao, Z.; Sui, C.; Wei, J.
Molecular cloning and characterization of three cDNAs encoding 1-deoxy-D-xylulose-5-phosphate synthase in Aquilaria sinensis (Lour.) Gilg.
Plant Physiol. Biochem.
82
133-141
2014
Aquilaria sinensis
brenda
Henriquez, M.A.; Soliman, A.; Li, G.; Hannoufa, A.; Ayele, B.T.; Daayf, F.
Molecular cloning, functional characterization and expression of potato (Solanum tuberosum) 1-deoxy-D-xylulose 5-phosphate synthase 1 (StDXS1) in response to Phytophthora infestans
Plant Sci.
243
71-83
2016
Solanum tuberosum (E7CCH1), Solanum tuberosum
brenda
Battistini, M.R.; Shoji, C.; Handa, S.; Breydo, L.; Merkler, D.J.
Mechanistic binding insights for 1-deoxy-D-xylulose-5-phosphate synthase, the enzyme catalyzing the first reaction of isoprenoid biosynthesis in the malaria-causing protists, Plasmodium falciparum and Plasmodium vivax
Protein Expr. Purif.
120
16-27
2016
Plasmodium falciparum, Plasmodium vivax
brenda
Sanders, S.; Vierling, R.J.; Bartee, D.; DeColli, A.A.; Harrison, M.J.; Aklinski, J.L.; Koppisch, A.T.; Freel Meyers, C.L.
Challenges and hallmarks of establishing alkylacetylphosphonates as probes of bacterial 1-deoxy-D-xylulose 5-phosphate synthase
ACS Infect. Dis.
3
467-478
2017
Escherichia coli, Escherichia coli MG1655
brenda
Handa, S.; Dempsey, D.R.; Ramamoorthy, D.; Cook, N.; Guida, W.C.; Spradling, T.J.; White, J.K.; Woodcock, H.L.; Merkler, D.J.
Mechanistic studies of 1-deoxy-D-xylulose-5-phosphate synthase from Deinococcus radiodurans
Biochem. Mol. Biol. J.
4
2
2018
Deinococcus radiodurans (Q9RUB5), Deinococcus radiodurans DSM 20539 (Q9RUB5)
brenda
Bartee, D.; Freel Meyers, C.L.
Targeting the unique mechanism of bacterial 1-deoxy-D-xylulose-5-phosphate synthase
Biochemistry
57
4349-4356
2018
Escherichia coli
brenda
DeColli, A.A.; Zhang, X.; Heflin, K.L.; Jordan, F.; Freel Meyers, C.L.
Active site histidines link conformational dynamics with catalysis on anti-infective target 1-deoxy-D-xylulose 5-phosphate synthase
Biochemistry
58
4970-4982
2019
Escherichia coli
brenda
Wang, Y.; Yuan, X.; Li, S.; Chen, W.; Li, J.
Gene cloning and functional characterization of three 1-deoxy-D-xylulose 5-phosphate synthases in Simao pine
BioResources
13
6370-6382
2019
Pinus kesiya var. langbianensis
-
brenda
Wang, H.; Feng, G.; Li, Z.; Qiu, F.; Lan, X.; Liao, Z.; Yang, C.
Molecular cloning and characterization of 1-deoxy-D-xylulose 5-phosphate synthase gene from Taxus chinensis
Chin. Tradit. Herbal Drugs
49
4636-4643
2018
Taxus chinensis
-
brenda
Goswami, A.M.
Computational analysis, structural modeling and ligand binding site prediction of Plasmodium falciparum 1-deoxy-D-xylulose-5-phosphate synthase
Comput. Biol. Chem.
66
1-10
2017
Plasmodium falciparum (Q8IDW0), Plasmodium falciparum
brenda
Chen, P.Y.; DeColli, A.A.; Freel Meyers, C.L.; Drennan, C.L.
X-ray crystallography-based structural elucidation of enzyme-bound intermediates along the 1-deoxy-D-xylulose 5-phosphate synthase reaction coordinate
J. Biol. Chem.
294
12405-12414
2019
Deinococcus radiodurans
brenda
Kudoh, K.; Hotta, S.; Sekine, M.; Fujii, R.; Uchida, A.; Kubota, G.; Kawano, Y.; Ihara, M.
Overexpression of endogenous 1-deoxy-D-xylulose 5-phosphate synthase (DXS) in cyanobacterium Synechocystis sp. PCC6803 accelerates protein aggregation
J. Biosci. Bioeng.
123
590-596
2017
Synechocystis sp. PCC 6803
brenda
White, J.K.; Handa, S.; Vankayala, S.L.; Merkler, D.J.; Woodcock, H.L.
Thiamin diphosphate activation in 1-deoxy-D-xylulose 5-phosphate synthase insights into the mechanism and underlying intermolecular interactions
J. Phys. Chem. B
120
9922-9934
2016
Deinococcus radiodurans (Q9RUB5), Deinococcus radiodurans DSM 20539 (Q9RUB5)
brenda
Zhou, W.; Huang, F.; Li, S.; Wang, Y.; Zhou, C.; Shi, M.; Wang, J.; Chen, Y.; Wang, Y.; Wang, H.; Kai, G.
Molecular cloning and characterization of two 1-deoxy-D-xylulose-5-phosphate synthase genes involved in tanshinone biosynthesis in Salvia miltiorrhiza
Mol. Breed.
36
124
2016
Salvia miltiorrhiza (B4YSH1), Salvia miltiorrhiza (C4NXC0)
-
brenda
Fan, H.; Wu, Q.; Wang, X.; Wu, L.; Cai, Y.; Lin, Y.
Molecular cloning and expression of 1-deoxy-D-xylulose-5-phosphate synthase and 1-deoxy-D-xylulose-5-phosphate reductoisomerase in Dendrobium officinale
Plant Cell Tissue Organ Cult.
125
381-385
2016
Dendrobium officinale (W0FI66)
-
brenda
Zhou, J.; Yang, L.; DeColli, A.; Freel Meyers, C.; Nemeria, N.S.; Jordan, F.
Conformational dynamics of 1-deoxy-D-xylulose 5-phosphate synthase on ligand binding revealed by H/D exchange MS
Proc. Natl. Acad. Sci. USA
114
9355-9360
2017
Escherichia coli (P77488), Escherichia coli
brenda
Liang, Y.F.; Liu, H.; Li, H.; Gao, W.Y.
Determination of the activity of 1-deoxy-D-xylulose 5-phosphate synthase by pre-column derivatization-HPLC using 1,2-diamino-4,5-methylenedioxybenzene as a derivatizing reagent
Protein J.
38
160-166
2019
Escherichia coli (P77488)
brenda
Garcia-Alcazar, M.; Gimenez, E.; Pineda, B.; Capel, C.; Garcia-Sogo, B.; Sanchez, S.; Yuste-Lisbona, F.J.; Angosto, T.; Capel, J.; Moreno, V.; Lozano, R.
Albino T-DNA tomato mutant reveals a key function of 1-deoxy-D-xylulose-5-phosphate synthase (DXS1) in plant development and survival
Sci. Rep.
7
45333
2017
Solanum lycopersicum (C7U110), Solanum lycopersicum
brenda