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2-oxoglutarate + NADH + H+
2-hydroxyglutarate + NAD+
2-oxoglutarate + NADH + H+
?
2-oxoglutarate + NADH + H+
D-2-hydroxyglutarate + NAD+
2-phospho-D-glycerate + NAD+
2-phosphohydroxypyruvate + NADH + H+
-
activity relative to 3-phospho-D-glycerate: 47%
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphohydroxypyruvate + NADH
3-phospho-D-glycerate + NAD+
3-phosphohydroxypyruvate + NADH + H+
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
3-phospho-D-glycerate + NADP+
3-phosphohydroxypyruvate + NADPH + H+
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
3-phosphohydroxypyruvate + NAD+
?
3-phosphohydroxypyruvate + NADH
3-phosphoglycerate + NAD+
-
specific for
-
-
?
3-phosphooxypyruvate + acetylpyridine
3-phospho-D-glycerate + ?
-
-
-
r
3-phosphooxypyruvate + NADH + H+
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + pyridinealdehyde adenine dinucleotide
3-phospho-D-glycerate + ?
-
-
-
r
3-phosphooxypyruvate + thionicotinamide
3-phospho-D-glycerate + ?
-
-
-
r
alpha-ketoglutarate + NADH
2-hydroxyglutaric acid + NAD+
DL-glyceraldehyde 3-phosphate + NAD+
?
-
activity relative to 3-phospho-D-glycerate: 9%
-
-
?
oxaloacetate + NADH + H+
?
-
-
-
?
oxaloacetate + NADH + H+
malate + NAD+
-
-
-
-
?
phosphonooxypyruvate + NADH + H+
?
additional information
?
-
2-oxoglutarate + NADH + H+
2-hydroxyglutarate + NAD+
-
-
-
?
2-oxoglutarate + NADH + H+
2-hydroxyglutarate + NAD+
-
-
-
-
?
2-oxoglutarate + NADH + H+
?
-
-
-
?
2-oxoglutarate + NADH + H+
?
-
-
-
?
2-oxoglutarate + NADH + H+
?
-
-
-
?
2-oxoglutarate + NADH + H+
D-2-hydroxyglutarate + NAD+
-
-
-
?
2-oxoglutarate + NADH + H+
D-2-hydroxyglutarate + NAD+
-
-
-
?
2-oxoglutarate + NADH + H+
D-2-hydroxyglutarate + NAD+
-
-
-
?
2-oxoglutarate + NADH + H+
D-2-hydroxyglutarate + NAD+
-
-
-
?
2-oxoglutarate + NADH + H+
D-2-hydroxyglutarate + NAD+
-
-
-
-
?
2-oxoglutarate + NADH + H+
D-2-hydroxyglutarate + NAD+
wild-type enzyme shows no activity. Mutant enzymes R72A and R72L utilize 2-oxoglutarate as substrate
-
-
?
2-oxoglutarate + NADH + H+
D-2-hydroxyglutarate + NAD+
wild-type enzyme shows no activity. Mutant enzymes R72A and R72L utilize 2-oxoglutarate as substrate
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
first step in biosynthesis of L-serine, pathway regulation, overview
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
r
3-phospho-D-glycerate + NAD+
3-phosphohydroxypyruvate + NADH
first step in biosynthesis of L-serine, the enzyme contains an ACT domain, which is involved in the allosteric regulation mechanism, residue W139 is involved
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
first step in biosynthesis of L-serine, the enzyme contains an ACT domain, which is involved in the allosteric regulation mechanism, residue W139 is involved
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphohydroxypyruvate + NADH
first step in biosynthesis of L-serine, Vmax regulation through domain and subunit changes, overview
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphohydroxypyruvate + NADH
D-isomer-specific
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
D-isomer-specific
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphohydroxypyruvate + NADH + H+
-
-
-
-
r
3-phospho-D-glycerate + NAD+
3-phosphohydroxypyruvate + NADH + H+
-
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphohydroxypyruvate + NADH + H+
-
highest activity
-
-
r
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
-
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
-
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
-
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
-
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
-
-
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
-
-
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
-
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
-
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
-
-
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
-
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
-
-
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
-
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
-
-
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
-
-
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
-
-
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
-
-
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
-
-
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
-
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
-
-
-
-
r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
-
-
-
r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
-
-
-
r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
first committed enzyme of the phosphorylated pathway of l-serine biosynthesis, regulated by negative feedback from L-serine in bacteria and plants
-
-
r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
-
-
-
r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
-
-
-
r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
-
-
-
r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
enzyme in the L-serine biosynthetic pathway
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
first step of L-serine biosynthesis
-
-
r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
-
-
-
r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
first step of L-serine biosynthesis
-
-
r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
-
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
-
-
-
r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
-
-
-
-
r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
-
-
-
r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
-
-
-
-
r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
-
-
-
r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
the enzyme has a 400fold higher affinity for NADH than NAD+
-
-
r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
-
-
-
r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
-
-
-
r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
-
-
-
-
r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
enzyme in the L-serine biosynthetic pathway
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
first step of L-serine biosynthesis
-
-
r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
-
-
-
r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
enzyme in the L-serine biosynthetic pathway
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
-
-
-
r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
first step of L-serine biosynthesis
-
-
r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
-
-
-
-
r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
-
-
-
r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
-
-
-
r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
-
-
-
r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
-
-
-
r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
enzyme in the L-serine biosynthetic pathway
-
-
?
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
-
-
-
-
r
3-phospho-D-glycerate + NADP+
3-phosphohydroxypyruvate + NADPH + H+
-
-
-
?
3-phospho-D-glycerate + NADP+
3-phosphohydroxypyruvate + NADPH + H+
-
-
-
-
?
3-phospho-D-glycerate + NADP+
3-phosphohydroxypyruvate + NADPH + H+
-
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
first enzyme in metabolic sequence of synthesis of serine from 3-phosphoglycerate
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
reduction of hydroxypyruvate-phosphate is faster than oxidation of phosphoglycerate
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
allosteric inhibition by L-serine, L-serine regulates the pathway of serine biosynthesis by end product inhibition interacting with His344, Asn346 and Asn364, 1 serine binds per subunit
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
allosteric inhibition by L-serine, L-serine regulates the pathway of serine biosynthesis by end product inhibition interacting with His344, Asn346 and Asn364, 1 serine binds per subunit
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
first enzyme in metabolic sequence of synthesis of serine from 3-phosphoglycerate
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
Frog
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
first enzyme in metabolic sequence of synthesis of serine from 3-phosphoglycerate
-
-
?
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
first enzyme in metabolic sequence of synthesis of serine from 3-phosphoglycerate
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
Pigeon
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
first enzyme in metabolic sequence of synthesis of serine from 3-phosphoglycerate
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
-
?
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
the enzyme catalyzes the first reaction of serine and glycine biosynthesis. SER3 and SER33 encode phosphoglycerate dehydrogenases. The requirement for the SER-dependent phosphoglycerate pathway is conditional since the glyoxylate route of serine/glycine biosynthesis is glucose repressed. Ser33p is likely to be the main isoenzyme of the phosphoglycerate pathway during growth on glucose
-
-
?
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
-
r
3-phosphohydroxypyruvate + NAD+
?
-
-
-
r
3-phosphohydroxypyruvate + NAD+
?
-
-
-
r
3-phosphooxypyruvate + NADH + H+
3-phospho-D-glycerate + NAD+
-
-
-
r
3-phosphooxypyruvate + NADH + H+
3-phospho-D-glycerate + NAD+
-
-
-
r
3-phosphooxypyruvate + NADH + H+
3-phospho-D-glycerate + NAD+
-
-
-
?
3-phosphooxypyruvate + NADH + H+
3-phospho-D-glycerate + NAD+
-
-
-
r
3-phosphooxypyruvate + NADH + H+
3-phospho-D-glycerate + NAD+
-
-
-
r
3-phosphooxypyruvate + NADH + H+
3-phospho-D-glycerate + NAD+
-
-
-
r
3-phosphooxypyruvate + NADH + H+
3-phospho-D-glycerate + NAD+
-
-
-
r
3-phosphooxypyruvate + NADH + H+
3-phospho-D-glycerate + NAD+
the enzyme has a 400fold higher affinity for NADH than NAD+
-
-
r
3-phosphooxypyruvate + NADH + H+
3-phospho-D-glycerate + NAD+
-
-
-
r
3-phosphooxypyruvate + NADH + H+
3-phospho-D-glycerate + NAD+
-
-
-
r
3-phosphooxypyruvate + NADH + H+
3-phospho-D-glycerate + NAD+
-
-
-
-
r
3-phosphooxypyruvate + NADH + H+
3-phospho-D-glycerate + NAD+
-
-
-
r
3-phosphooxypyruvate + NADH + H+
3-phospho-D-glycerate + NAD+
-
-
-
r
3-phosphooxypyruvate + NADH + H+
3-phospho-D-glycerate + NAD+
-
-
-
r
alpha-ketoglutarate + NADH
2-hydroxyglutaric acid + NAD+
-
-
-
-
?
alpha-ketoglutarate + NADH
2-hydroxyglutaric acid + NAD+
-
-
-
r
alpha-ketoglutarate + NADH
2-hydroxyglutaric acid + NAD+
-
-
-
?
alpha-ketoglutarate + NADH
2-hydroxyglutaric acid + NAD+
-
-
both D- and L-isomer serve as substrate for the reverse reaction, but L-isomer is a poor substrate and probably due to contamination
r
phosphonooxypyruvate + NADH + H+
?
-
-
-
?
phosphonooxypyruvate + NADH + H+
?
-
-
-
-
?
phosphonooxypyruvate + NADH + H+
?
-
-
-
?
phosphonooxypyruvate + NADH + H+
?
-
-
-
-
?
phosphonooxypyruvate + NADH + H+
?
catalytic His280, active site, regulatory, and substrate binding site structures, overview
-
-
?
phosphonooxypyruvate + NADH + H+
?
very slow NADH binding in absence of substrate, productive NADH binding, that would support catalytic turnover, is dependent on the presence of substrate, active site structure with the catalytic His280, modelling of ligand-free and substrate-bound active site, overview
-
-
?
phosphonooxypyruvate + NADH + H+
?
-
-
-
?
phosphonooxypyruvate + NADH + H+
?
very slow NADH binding in absence of substrate, productive NADH binding, that would support catalytic turnover, is dependent on the presence of substrate, active site structure with the catalytic His280, modelling of ligand-free and substrate-bound active site, overview
-
-
?
phosphonooxypyruvate + NADH + H+
?
-
-
-
?
phosphonooxypyruvate + NADH + H+
?
catalytic His280, active site, regulatory, and substrate binding site structures, overview
-
-
?
additional information
?
-
no activity with 2-oxoglutarate
-
-
?
additional information
?
-
-
no activity with 2-oxoglutarate
-
-
?
additional information
?
-
HOXA10 is required for enzyme regulation in the endometrium
-
-
?
additional information
?
-
-
HOXA10 is required for enzyme regulation in the endometrium
-
-
?
additional information
?
-
-
no activity with pyruvate
-
-
?
additional information
?
-
-
enzyme is involved in de novo L-serine biosynthesis, in the peripheral nervous system and non-neuronal tissues of mice
-
-
?
additional information
?
-
HOXA10 is required for enzyme regulation in the endometrium
-
-
?
additional information
?
-
-
HOXA10 is required for enzyme regulation in the endometrium
-
-
?
additional information
?
-
-
no activity with alpha-ketoglutarate
-
-
?