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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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-oxoglutarate + NADH + H+
D-2-hydroxyglutarate + NAD+
-
-
-
-
?
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-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
3-phosphooxypyruvate + NADH + H+
3-phospho-D-glycerate + NAD+
-
-
-
r
oxaloacetate + NADH + H+
malate + NAD+
-
-
-
-
?
phosphonooxypyruvate + NADH + H+
?
additional information
?
-
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
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-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+
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+
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+
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+
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+
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+
-
-
-
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-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
-
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
-
first enzyme in metabolic sequence of synthesis of serine from 3-phosphoglycerate
-
-
?
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
-
first enzyme in metabolic sequence of synthesis of serine from 3-phosphoglycerate
-
-
r
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
-
-
?
phosphonooxypyruvate + NADH + H+
?
-
-
-
?
phosphonooxypyruvate + NADH + H+
?
-
-
-
-
?
phosphonooxypyruvate + NADH + H+
?
-
-
-
?
phosphonooxypyruvate + NADH + H+
?
-
-
-
-
?
phosphonooxypyruvate + NADH + H+
?
-
-
-
?
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
-
-
?
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(2,3-dihydro-1H-benzotriazol-1-yl)(4-phenylpiperazin-1-yl)methanone
0.1 mM, 37% inhibition
-
(3,4-dichlorophenyl)(morpholin-4-yl)methanethione
0.1 mM, 96% inhibition
-
(3R)-N-(4,6-dimethylpyridin-2-yl)-3-methyl-4-[[4-(trifluoromethyl)phenyl]methyl]piperazine-1-carbothioamide
-
-
(3R,5S)-N-(4,6-dimethylpyridin-2-yl)-3,5-dimethyl-4-[[4-(trifluoromethyl)phenyl]methyl]piperazine-1-carbothioamide
-
-
(3S)-N-(4,6-dimethylpyridin-2-yl)-3-methyl-4-[[4-(trifluoromethyl)phenyl]methyl]piperazine-1-carbothioamide
-
-
(4-methylpyridin-2-yl)[4-[3-(trifluoromethyl)phenyl]piperazin-1-yl]methanethione
-
-
(NH4)2SO4
-
inhibitory effect on NADPH-dependent 3-phosphohydroxypyruvate reduction
(R)-2-amino-1-propanol
-
slightly
1-(2,4-dichlorophenyl)-2-morpholino-2-thioxoethan-1-one
-
-
1-(2-bromophenyl)-2-(morpholin-4-yl)-2-sulfanylideneethan-1-one
-
-
1-(2-chlorophenyl)-1H-pyrrole-2,5-dione
0.1 mM, 78% inhibition
-
1-(4-bromophenyl)-2-(morpholin-4-yl)-2-sulfanylideneethan-1-one
-
-
1-(4-chlorophenyl)-2-(morpholin-4-yl)-2-sulfanylideneethan-1-one
-
-
1-(4-chlorophenyl)-2-morpholino-2-thioxoethan-1-one
-
-
1-(4-fluorophenyl)-2-(morpholin-4-yl)-2-sulfanylideneethan-1-one
-
-
1-(4-iodophenyl)-2-(morpholin-4-yl)-2-sulfanylideneethan-1-one
-
-
1-(4-methoxybenzene-1-sulfonyl)piperazine
0.1 mM, 35% inhibition
-
2-(4-methylpiperidin-1-yl)-1-phenyl-2-thioxoethan-1-one
-
-
2-(4-methylpyridin-2-yl)-1-[4-[3-(trifluoromethyl)phenyl]piperazin-1-yl]ethane-1-thione
-
-
2-(morpholin-4-yl)-1-(3-nitrophenyl)-2-sulfanylideneethan-1-one
-
-
2-(morpholin-4-yl)-1-(4-nitrophenyl)-2-sulfanylideneethan-1-one
-
-
2-(morpholin-4-yl)-1-phenyl-2-sulfanylideneethan-1-one
-
-
2-chloro-4-(5-[(Z)-[2-(ethylcarbamothioyl)hydrazinylidene]methyl]furan-3-yl)benzoic acid
i.e. PKUMDL-WQ-2101, specifically binds to the enzyme (PHGDH) in PHGDH-amplified breast cancer cells with EC50 values less than 0.010 mM in serine-replete media. Mainly inhibits PHGDH activity by forming hydrogen-bond networks with R134, K57, and T59 of site I and T59, T56, and K57 of site II, respectively
-
2-methyl-N-(2-[[(2E)-2-[2-[(2-nitrobenzyl)oxy]benzylidene]hydrazinyl]carbonyl]phenyl)benzamide
-
2-morpholino-1-phenyl-2-thioxoethan-1-one
-
-
2-phenylmorpholine
0.1 mM, 61% inhibition
-
3-pentyl-5,5-diphenylimidazolidine-2,4-dione
0.1 mM, 25% inhibition
-
3-[(E)-(5-cyano-2-hydroxy-4-methyl-6-oxo-1,6-dihydropyridin-3-yl)diazenyl]benzoic acid
i.e. PKUMDL-WQ-2201, specifically binds to the enzyme (PHGDH) in PHGDH-amplified breast cancer cells with EC50 values less than 0.010 mM in serine-replete media. Mainly inhibits PHGDH activity by forming hydrogen-bond networks with R134, K57, and T59 of site I and T59, T56, and K57 of site II, respectively
-
4,5,6,7-tetrahydro-1,3-benzothiazol-2-amine
0.1 mM, 46% inhibition
-
4-(5-[(Z)-[1-(3,4-dimethylphenyl)-3,5-dioxopyrazolidin-4-ylidene]methyl]furan-2-yl)-N-(1,3-thiazol-2-yl)benzenesulfonamide
-
4-benzyl-N-(4,6-dimethylpyridin-2-yl)piperazine-1-carbothioamide
-
-
4-benzyl-N-[3,5-bis(trifluoromethyl)phenyl]piperazine-1-carbothioamide
0.1 mM, 80% inhibition
-
4-chloro-N-(2-nitrophenyl)benzamide
0.1 mM, 59% inhibition
-
4-[(1S)-1-[(5-chloro-6-[2-[(2-hydroxyethyl)amino]-2-oxoethoxy]-1H-indole-2-carbonyl)amino]-2-hydroxyethyl]benzoic acid
competitive, i.e. SPR Kd
-
4-[(2-chlorophenyl)methyl]-N-(4,6-dimethylpyridin-2-yl)piperazine-1-carbothioamide
-
-
4-[(3,5-dioxo-1,2,6-thiadiazinan-4-ylidene)methyl]phenyl 2,3-diphenylquinoxaline-6-carboxylate
-
4-[(3-chlorophenyl)methyl]-N-(4,6-dimethylpyridin-2-yl)piperazine-1-carbothioamide
-
-
4-[(4,6-dimethylpyridin-2-yl)carbamothioyl]-1-[[4-(trifluoromethyl)phenyl]methyl]piperazine-2-carboxylic acid
-
-
4-[(4-bromophenyl)methyl]-N-(4,6-dimethylpyridin-2-yl)piperazine-1-carbothioamide
-
-
4-[3-(trifluoromethyl)phenyl]-N-[4-(trifluoromethyl)pyridin-2-yl]piperazine-1-carbothioamide
-
-
5-[(2-furanylcarbonyl)amino]-3-methyl-4-thiocyanato-2-thiophenecarboxylic acid ethyl ester
i.e. CBR-5884, covalent inhibitor that binds to a Cys in the non-active site and disrupts its oligomeric state. CBR-5884 inhibits the growth of cells by 35% to 60% in serine-abundant media, and by 80% to 90% in serine-depleted media at 0.030 mM
-
adenosine 5'-diphosphoribose
0.12 mM, 50% inhibition. NAD+ competitive inhibitor
Ag+
-
inhibition can be overcome by addition of dithiothreitol
AMP
-
weak inhibitory effect on 3-phospho-D-glycerate oxidation, remaining activity: 75%
azacoccone E
non-competitive inhibitor in a time-dependent manner
-
cyclohexa-2,5-diene-1,4-dione
0.1 mM, 100% inhibition
ethyl 5-[(furan-2-carbonyl)amino]-3-methyl-4-(nitrilo-lambda4-sulfanyl)thiophene-2-carboxylate
noncompetitive, i.e. CBR-5884
-
hydroxyglutarate
-
product inhibition of the alpha-ketoglutarate reduction
ixocarpalactone A
non-competitive inhibitor relative to the substrate of NAD coenzyme
-
K2HPO4
-
inhibitory effect on NADPH-dependent 3-phosphohydroxypyruvate reduction. It appears that the phosphate ion PO43- exerts its inhibitory effect by binding to the free enzyme and NADPH-enzyme complex
Mercurials
-
inhibition can be overcome by addition of dithiothreitol
-
methyl 2-([4-[3-(trifluoromethyl)phenyl]piperazine-1-carbothioyl]amino)pyridine-4-carboxylate
-
-
morpholino(phenyl)methanethione
-
-
N'-(4,6-dimethylpyridin-2-yl)-N-methyl-N-[2-(methyl[[4-(trifluoromethyl)phenyl]methyl]amino)ethyl]thiourea
-
-
N-(3-methylphenyl)-4-[3-(trifluoromethyl)phenyl]piperazine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)(oxo)[4-(trifluoromethyl)phenyl]ethanethioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-3-(hydroxymethyl)-4-[[4-(trifluoromethyl)phenyl]methyl]piperazine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-3-([[4-(trifluoromethyl)phenyl]methyl]amino)piperidine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-3-methyl-4-[[4-(trifluoromethyl)phenyl]methyl]piperazine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-3-phenyl-4-[[4-(trifluoromethyl)phenyl]methyl]piperazine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-3-[3-(trifluoromethyl)anilino]piperidine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-3-[4-(trifluoromethyl)anilino]piperidine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-4-(2-methoxyphenyl)piperazine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-4-(3-methoxyphenyl)piperazine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-4-(4-(trifluoromethyl)benzyl)piperazine-1-carbothioamide
i.e. NCT-503, non-competitive inhibitor in regards to substrates and cofactors, closely binds to the active site
-
N-(4,6-dimethylpyridin-2-yl)-4-(4-methoxyphenyl)piperazine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-4-(pyridin-2-yl)piperazine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-4-(pyridin-3-yl)piperazine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-4-(pyridin-4-yl)piperazine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-4-[(2-fluorophenyl)methyl]piperazine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-4-[(2-methylphenyl)methyl]piperazine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-4-[(3-fluorophenyl)methyl]piperazine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-4-[(3-methylphenyl)methyl]piperazine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-4-[(4-fluorophenyl)methyl]piperazine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-4-[(4-methylphenyl)methyl]piperazine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-4-[(pyridin-2-yl)methyl]piperazine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-4-[(pyridin-3-yl)methyl]piperazine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-4-[(pyridin-4-yl)methyl]piperazine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-4-[2-(trifluoromethyl)phenyl]piperazine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-4-[2-[4-(trifluoromethyl)phenyl]ethyl]piperazine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-4-[3-(trifluoromethyl)anilino][1,4'-bipiperidine]-1'-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-4-[3-(trifluoromethyl)benzoyl]piperazine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-4-[3-(trifluoromethyl)phenyl]piperazine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-4-[4-(trifluoromethyl)anilino][1,4'-bipiperidine]-1'-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-4-[4-(trifluoromethyl)benzoyl]piperazine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-4-[4-(trifluoromethyl)phenyl]piperazine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-4-[5-(trifluoromethyl)pyridin-2-yl]piperazine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-4-[6-(trifluoromethyl)pyridin-2-yl]piperazine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-4-[[2-(trifluoromethyl)phenyl]methyl]piperazine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-4-[[3-(trifluoromethyl)phenyl]methyl]piperazine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-4-[[4-(trifluoromethoxy)phenyl]methyl]piperazine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-4-[[4-(trifluoromethyl)phenyl]methyl]-1,4-diazepane-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-4-[[4-(trifluoromethyl)phenyl]methyl]piperazine-1-carbothioamide
-
N-(4,6-dimethylpyridin-2-yl)-5-[[4-(trifluoromethyl)phenyl]methyl]hexahydropyrrolo[3,4-c]pyrrole-2(1H)-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-N'-[2-(methyl[[4-(trifluoromethyl)phenyl]methyl]amino)ethyl]thiourea
-
-
N-(4,6-dimethylpyridin-2-yl)-N'-[2-([[4-(trifluoromethyl)phenyl]methyl]amino)ethyl]thiourea
-
-
N-(4,6-dimethylpyridin-2-yl)[4-(trifluoromethyl)phenyl]ethanethioamide
-
-
N-(4,6-dimethylpyrimidin-2-yl)-4-nitrobenzamide
0.1 mM, 13% inhibition
-
N-(4-methylpyridin-2-yl)-4-[3-(trifluoromethyl)phenyl]piperazine-1-carbothioamide
-
-
N-(4-methylpyridin-2-yl)-4-[3-(trifluoromethyl)phenyl]piperazine-1-carboxamide
-
-
N-(4-methylpyridin-2-yl)-4-[3-(trifluoromethyl)phenyl]piperazine-1-carboximidamide
-
-
N-(4-methylquinolin-2-yl)-4-[3-(trifluoromethyl)phenyl]piperazine-1-carbothioamide
-
-
N-(diphenylmethyl)-4-nitrobenzamide
0.1 mM, 54% inhibition
-
N-(pyridin-2-yl)-4-[3-(trifluoromethyl)phenyl]piperazine-1-carbothioamide
-
-
N-(pyridin-3-yl)-4-[3-(trifluoromethyl)phenyl]piperazine-1-carbothioamide
-
-
N-(pyridin-4-yl)-4-[3-(trifluoromethyl)phenyl]piperazine-1-carbothioamide
-
-
N-(quinolin-2-yl)-4-[3-(trifluoromethyl)phenyl]piperazine-1-carbothioamide
-
-
N-cyclohexyl-N'-phenylthiourea
0.1 mM, 28% inhibition
-
N-methyl-N-(4-methylpyridin-2-yl)-4-[3-(trifluoromethyl)phenyl]piperazine-1-carbothioamide
-
-
N-morpholinobenzenesulfonamide
-
-
N-[(pyridin-2-yl)methyl]-4-[3-(trifluoromethyl)phenyl]piperazine-1-carbothioamide
-
-
N-[1'-[(4,6-dimethylpyridin-2-yl)carbamothioyl][1,4'-bipiperidin]-4-yl]-3-(trifluoromethyl)benzamide
-
-
N-[1-[(4,6-dimethylpyridin-2-yl)carbamothioyl]piperidin-3-yl]-4-(trifluoromethyl)benzamide
-
-
NAD+
-
product inhibition, competitive to NADH
naphthalene-1,4-dione
0.1 mM, 95% inhibition
p-chloromercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
phenyl cyclohexylcarbamodithioate
0.1 mM, 51% inhibition
-
pyridoxal 5'-phosphate
-
-
pyridoxamine 5'-phosphate
-
-
ZnCl2
-
inhibitory effect on 3-phosphohydroxypyruvate reduction, remaining activity: 29%
[4-[(4,6-dimethylpyridin-2-yl)carbamothioyl]piperazin-1-yl]methyl 2-methoxybenzoate
-
-
[4-[(4,6-dimethylpyridin-2-yl)carbamothioyl]piperazin-1-yl]methyl 3-methoxybenzoate
-
-
[4-[(4,6-dimethylpyridin-2-yl)carbamothioyl]piperazin-1-yl]methyl 4-methoxybenzoate
-
-
3-phosphoglycerate
-
-
3-phosphoglycerate
-
noncompetitive to phosphohydroxypyruvate
3-phosphohydroxypyruvate
substrate inhibition
3-phosphohydroxypyruvate
uncompetitive substrate inhibition at high substrate concentration
3-phosphohydroxypyruvate
-
product inhibition of 3-phospho-D-glycerate oxidation, variable substrate: 3-phospho-D-glycerate, inhibition pattern: competitive; product inhibition of 3-phospho-D-glycerate oxidation, variable substrate: NAD, inhibition pattern: non-competitive
3-phosphooxypyruvate
product inhibition
3-phosphooxypyruvate
significant substrate inhibition
3-phosphooxypyruvate
significant substrate inhibition. NADH bound at or near the ASB site and reduces the amount of substrate inhibition due to substrate interaction at the ASB site
ADP
-
free ADP is more effective than the magnesium complex
ADP
-
weak inhibitory effect on 3-phospho-D-glycerate oxidation, remaining activity: 86%
ATP
-
free ATP is more effective than the magnesium complex
ATP
-
weak inhibitory effect on 3-phospho-D-glycerate oxidation, remaining activity: 85%
glycine
-
-
glycine
-
mutants show less to no inhibition
L-alanine
-
-
L-alanine
-
native enzyme and mutant H344A
L-Ser
-
mutant enzyme SerADELTA197, a C-terminally truncated mutant enzyme, shows inhibition
L-Ser
-
binding of the inhibitor to the apoenzyme displays positive cooperativity in the binding of the first two serine molecules and negative cooperativity in the binding of the last two serine molecules. At least two NADH-induced conformational forms of the enzyme bind the inhibitor in the physiological range. Successive binding of NADH to the enzyme results in an increase in the affinity for the first inhibitor ligand bound and a lessening of both the positive and negative cooperativity of inhibitor binding
L-serine
-
L-serine
10 mM, inhibits AtPGDH3 at 55%; 10 mM, inhibits AtPGDH3 at 55%
L-serine
-
dithiothreitol inhibits enzyme inhibition by serine
L-serine
-
feedback regulation of the wild-type enzyme
L-serine
-
50% inhibition at 0.005 mM and pH 7.5
L-serine
-
inhibition of enzyme from E. coli, Salmonella typhimurium and Haemophilus influenzae, not of mammalian enzyme, inhibition in both reaction directions
L-serine
-
allosteric inhibition, regulates the pathway of serine biosynthesis by end product inhibition interacting with His344, Asn346 and Asn364
L-serine
-
50% inhibition at 0.008 mM L-serine; allosteric inhibition, regulates the pathway of serine biosynthesis by end product inhibition interacting with His344, Asn346 and Asn364
L-serine
-
sigmoidal binding curve with mutant G294V/G336V, mutants with decreased sensitivity to serine
L-serine
feedback regulation, positive and negative cooperativity in absence of NADH, positive in presence of NADH, overview
L-serine
the enzyme contains an ACT regulatory domain which binds L-serine for feedback regulation, binding site lies around residues H344-N364
L-serine
physiological inhibitor, exerts its effect on at least two steps in the kinetic mechanism. There is a small but significant effect on the dissociation constant of NADH, increasing the Kd to 5 and 23 microM from 0.6 and 9 microM, respectively, for the two sets of sites in the enzyme. After the second substrate is added, serine reduces the amplitude of the signal without a significant effect on the observed rate constants for binding. The serine concentration that reduces the amplitude by 50% is equal to the K0.5 for serine inhibition. Serine binding eliminates a conformational change subsequent to substrate binding by formation of a dead-end quaternary complex consisting of enzyme, coenzyme, substrate, and effector. The rate data conform to a model in which serine can bind to two forms of the enzyme with different affinities
L-serine
potent inhibitor
L-serine
40% inhibition in a cooperative manner
L-serine
-
I0.5: 0.03 mM. In presence of KCl, the binding and the inhibition of L-serine, are cooperative and in the absence of KCl they are not
L-serine
two serine molecules bound to the regulatory domain, anion- and serine-binding sites between two adjacent subunits
L-serine
-
non-linear and competitive
N-(4,6-dimethylpyridin-2-yl)-4-[[4-(trifluoromethyl)phenyl]methyl]piperazine-1-carbothioamide
-
-
N-(4,6-dimethylpyridin-2-yl)-4-[[4-(trifluoromethyl)phenyl]methyl]piperazine-1-carbothioamide
noncompetitive, i.e. NCT-503
-
N-ethylmaleimide
-
-
N-ethylmaleimide
-
D-3-phosphoglycerate and AMP protect against inhibition
NADH
-
inhibition of phosphoglycerate oxidation
NADH
-
product inhibition of 3-phospho-D-glycerate oxidation, variable substrate: 3-phospho-D-glycerate, inhibition pattern: non-competitive; product inhibition of 3-phospho-D-glycerate oxidation, variable substrate: NAD, inhibition pattern: competitive
additional information
-
Ser, Tyr, Val, Gly, Trp, O-acetyl-L-Ser, and Cys have no effect on enzyme activity in both directions
-
additional information
L-serine (10 mM) does not inhibit AtPGDH2
-
additional information
L-serine (10 mM) does not inhibit AtPGDH2
-
additional information
L-serine (10 mM) does not inhibit AtPGDH2
-
additional information
-
L-serine (10 mM) does not inhibit AtPGDH2
-
additional information
the enzyme contains an ACT domain, which is involved in the allosteric regulation mechanism
-
additional information
-
the enzyme contains an ACT domain, which is involved in the allosteric regulation mechanism
-
additional information
substrate inhibition at concentrations above 0.1 mM
-
additional information
-
substrate inhibition at concentrations above 0.1 mM
-
additional information
HOAX expression downregulates the enzyme by 40%
-
additional information
-
HOAX expression downregulates the enzyme by 40%
-
additional information
mechanism of substrate inhibition, linked to this pH-dependent depression in activity, overview
-
additional information
-
mechanism of substrate inhibition, linked to this pH-dependent depression in activity, overview
-
additional information
CBR5884, a potent inhibitor of the human enzyme (PGDH), does not inhibit the enzyme from Mycobacterium tuberculosis
-
additional information
-
CBR5884, a potent inhibitor of the human enzyme (PGDH), does not inhibit the enzyme from Mycobacterium tuberculosis
-
additional information
-
unlike the Escherichia coli PGDH no inhibition by L-serine
-
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0.088 - 53.1
2-oxoglutarate
0.00025 - 0.0054
3-acetylpyridine-NAD+
0.00016
3-acetylpyridine-NADH
-
25°C
0.003 - 320
3-phospho-D-glycerate
0.212
3-phosphoglycerate
pH 9.0
0.00013 - 40.2
3-phosphohydroxypyruvate
0.0032 - 0.17
3-phosphooxypyruvate
0.0393
acetylpyridine
pH 7.5, temperature not specified in the publication
-
0.038 - 0.088
alpha-ketoglutarate
0.4
D-2-hydroxyglutarate
pH and temperature not specified in the publication
0.15 - 1.1
D-3-phosphoglycerate
0.015
phosphohydroxypyruvate
pH 6.5
0.1477
pyridinealdehyde adenine dinucleotide
pH 7.5, temperature not specified in the publication
-
0.0118
Thionicotinamide
pH 7.5, temperature not specified in the publication
additional information
additional information
-
0.088
2-oxoglutarate
pH and temperature not specified in the publication
0.45
2-oxoglutarate
wild-type enzyme, pH 7.0, temperature not specified in the publication
3.7
2-oxoglutarate
pH 6.0, 25°C
5
2-oxoglutarate
mutant enzyme K141R, pH 7.0, temperature not specified in the publication
7.6
2-oxoglutarate
pH 6.0, 25°C
10.1
2-oxoglutarate
-
at pH 7.6 and 37°C
10.7
2-oxoglutarate
pH 6.0, 25°C
30.6
2-oxoglutarate
mutant enzyme R72L, pH 7.0, temperature not specified in the publication
53.1
2-oxoglutarate
mutant enzyme R72A, pH 7.0, temperature not specified in the publication
0.00025
3-acetylpyridine-NAD+
-
25°C
0.0054
3-acetylpyridine-NAD+
-
37°C
0.003
3-phospho-D-glycerate
-
in 50 mM MOPS buffer, pH 7.0, temperature not specified in the publication
0.004
3-phospho-D-glycerate
-
in 50 mM MOPS buffer, pH 7.0, temperature not specified in the publication
0.008
3-phospho-D-glycerate
-
in 50 mM MOPS buffer, pH 7.0, temperature not specified in the publication
0.014
3-phospho-D-glycerate
in 50 mM MOPS buffer, pH 7.0, temperature not specified in the publication
0.015
3-phospho-D-glycerate
-
in 50 mM MOPS buffer, pH 7.0, temperature not specified in the publication
0.025
3-phospho-D-glycerate
-
in 50 mM MOPS buffer, pH 7.0, temperature not specified in the publication
0.031
3-phospho-D-glycerate
-
in 200 mM KPO4 buffer, pH 7.0, temperature not specified in the publication
0.033
3-phospho-D-glycerate
-
value for 3-phospho-D-glycerate oxidation using NAD+ as a cofactor
0.041
3-phospho-D-glycerate
-
in 200 mM KPO4 buffer, pH 7.0, temperature not specified in the publication
0.049
3-phospho-D-glycerate
-
in 50 mM MOPS buffer, pH 7.0, temperature not specified in the publication
0.05
3-phospho-D-glycerate
-
-
0.05
3-phospho-D-glycerate
pH 8.0, 22°C
0.065
3-phospho-D-glycerate
-
in 200 mM KPO4 buffer, pH 7.0, temperature not specified in the publication
0.127
3-phospho-D-glycerate
-
in 200 mM KPO4 buffer, pH 7.0, temperature not specified in the publication
0.153
3-phospho-D-glycerate
-
in 200 mM KPO4 buffer, pH 7.0, temperature not specified in the publication
0.162
3-phospho-D-glycerate
in 200 mM KPO4 buffer, pH 7.0, temperature not specified in the publication
0.187
3-phospho-D-glycerate
pH 7.5, temperature not specified in the publication
0.19
3-phospho-D-glycerate
pH 7.5, mutant G336V
0.23
3-phospho-D-glycerate
pH 7.5, mutant H344A
0.26
3-phospho-D-glycerate
pH 7.5, mutant A144V
0.26
3-phospho-D-glycerate
-
at pH 7.6 and 37°C
0.28
3-phospho-D-glycerate
pH 7.5, mutant E387A
0.29
3-phospho-D-glycerate
pH 7.5, mutant N364A
0.292
3-phospho-D-glycerate
-
in 200 mM KPO4 buffer, pH 7.0, temperature not specified in the publication
0.294
3-phospho-D-glycerate
pH 8.5, temperature not specified in the publication
0.3
3-phospho-D-glycerate
pH 7.5, mutant E302A
0.33
3-phospho-D-glycerate
pH 7.5, mutant R338A
0.35
3-phospho-D-glycerate
pH 7.5, mutants A374V and D386A
0.39
3-phospho-D-glycerate
pH 7.5, mutant N346A
0.396
3-phospho-D-glycerate
wild type enzyme, at pH 9.0 and 25°C
0.45
3-phospho-D-glycerate
pH 7.5, mutant R347A
0.47
3-phospho-D-glycerate
pH 7.5, mutant Q361A
0.49
3-phospho-D-glycerate
pH 7.5, wild-type enzyme and mutant Q375A
0.49
3-phospho-D-glycerate
pH 9.0, temperature not specified in the publication
0.5
3-phospho-D-glycerate
pH 9.0, 25°C
0.54
3-phospho-D-glycerate
pH and temperature not specified in the publication
0.58
3-phospho-D-glycerate
pH 7.5, mutant P348A
0.6
3-phospho-D-glycerate
mutant enzyme K263A, at pH 9.0 and 25°C
0.63
3-phospho-D-glycerate
pH 7.5, mutant S316A
0.64
3-phospho-D-glycerate
pH 7.5, mutant G337V
0.66
3-phospho-D-glycerate
pH 7.5, mutant E360A
0.68
3-phospho-D-glycerate
pH 7.5, mutants S323A and G362V
0.69
3-phospho-D-glycerate
pH 7.5, mutant G349V
0.72
3-phospho-D-glycerate
pH 7.5, mutant S373A
0.76
3-phospho-D-glycerate
pH 7.5, mutant E345A
0.77
3-phospho-D-glycerate
pH 9.0, 25°C
0.79
3-phospho-D-glycerate
pH 7.5, mutant H335A
0.899
3-phospho-D-glycerate
isoform PGDH2, at pH 8.1 and 37°C
0.9
3-phospho-D-glycerate
-
-
0.97
3-phospho-D-glycerate
pH 7.5, mutant S107A
1.006
3-phospho-D-glycerate
isoform PGDH3, at pH 8.1 and 37°C
1.03
3-phospho-D-glycerate
pH 9.0, 25°C
1.19
3-phospho-D-glycerate
-
pH 9.0
1.19
3-phospho-D-glycerate
pH 7.5, mutant A143V
1.2
3-phospho-D-glycerate
pH and temperature not specified in the publication
1.308
3-phospho-D-glycerate
isoform PGDH1, at pH 8.1 and 37°C
1.35
3-phospho-D-glycerate
-
-
1.37
3-phospho-D-glycerate
pH 7.5, mutant S296A
1.38
3-phospho-D-glycerate
30°C, pH 9.0
1.41
3-phospho-D-glycerate
pH 7.5, mutants Q298A and N303A
1.6
3-phospho-D-glycerate
pH 7.5, mutant D317A
1.77
3-phospho-D-glycerate
pH 7.5, mutant E307A
1.926
3-phospho-D-glycerate
isoform PGDH2, at pH 7.2 and 37°C
1.99
3-phospho-D-glycerate
pH 7.5, mutant E299A
2.11
3-phospho-D-glycerate
isoform PGDH1, at pH 7.2 and 37°C
2.559
3-phospho-D-glycerate
isoform PGDH3, at pH 7.2 and 37°C
2.92
3-phospho-D-glycerate
30°C, pH 9.0
4.33
3-phospho-D-glycerate
pH 7.5, mutant S111A
4.78
3-phospho-D-glycerate
pH 7.5, mutant Q301A
6.6
3-phospho-D-glycerate
pH 7.5, mutant S107A/S111A
7.2
3-phospho-D-glycerate
pH 7.5, mutant G145V
12
3-phospho-D-glycerate
pH 7.5, mutant K311A
13.1
3-phospho-D-glycerate
pH 7.5, mutant N303A/K311A
16.9
3-phospho-D-glycerate
pH 7.5, mutant T297A
29.1
3-phospho-D-glycerate
pH 7.5, mutant K141A
320
3-phospho-D-glycerate
pH 7.5, mutant S111A/K311A
0.00013
3-phosphohydroxypyruvate
-
25°C
0.0013
3-phosphohydroxypyruvate
-
Km at pH 7.5 is lower than at pH 8.8
0.0032
3-phosphohydroxypyruvate
-
apparent
0.0096
3-phosphohydroxypyruvate
-
value for 3-phosphohydroxypyruvate reduction using NADH as a cofactor
0.015 - 0.02
3-phosphohydroxypyruvate
pH 7.1, 25°C, wild-type enzyme from fibroblasts
0.0216
3-phosphohydroxypyruvate
pH 7.1, 25°C, recombinant FLAG-tagged wild-type enzyme from HEK-293 cells
0.045
3-phosphohydroxypyruvate
-
25°C
0.07
3-phosphohydroxypyruvate
-
37°C
0.075
3-phosphohydroxypyruvate
mutant K439A
0.085
3-phosphohydroxypyruvate
-
pH 7.5, 37°C
0.12
3-phosphohydroxypyruvate
-
value for 3-phosphohydroxypyruvate reduction using NADPH as a cofactor
0.123
3-phosphohydroxypyruvate
mutant R446A
0.15
3-phosphohydroxypyruvate
-
-
0.16
3-phosphohydroxypyruvate
mutant H447A
0.17
3-phosphohydroxypyruvate
-
0.18
3-phosphohydroxypyruvate
mutant R501A
0.19
3-phosphohydroxypyruvate
mutant R451A
0.243
3-phosphohydroxypyruvate
mutant R501A/R451A/K439A
0.35
3-phosphohydroxypyruvate
-
pH 7.1
40.2
3-phosphohydroxypyruvate
-
-
0.0032
3-phosphooxypyruvate
pH and temperature not specified in the publication
0.015
3-phosphooxypyruvate
pH 7.0, temperature not specified in the publication
0.015
3-phosphooxypyruvate
mutant enzyme R132K, pH 7.0, temperature not specified in the publication
0.027
3-phosphooxypyruvate
pH and temperature not specified in the publication
0.068
3-phosphooxypyruvate
wild-type enzyme, pH 7.0, temperature not specified in the publication
0.081
3-phosphooxypyruvate
mutant enzyme K141R, pH 7.0, temperature not specified in the publication
0.09355
3-phosphooxypyruvate
30°C, pH 7.5
0.1164
3-phosphooxypyruvate
30°C, pH 7.5
0.153
3-phosphooxypyruvate
wild-type enzyme, pH 7.0, temperature not specified in the publication
0.169
3-phosphooxypyruvate
mutant enzyme R72A/R132K, pH 7.0, temperature not specified in the publication
0.17
3-phosphooxypyruvate
pH and temperature not specified in the publication
0.038
alpha-ketoglutarate
-
apparent, double mutant H344A/N364A
0.042
alpha-ketoglutarate
-
apparent
0.044
alpha-ketoglutarate
-
apparent, mutant N346A
0.088
alpha-ketoglutarate
-
apparent
0.15
D-3-phosphoglycerate
-
pH 7.5
0.29
D-3-phosphoglycerate
-
pH 9.4
1.1
D-3-phosphoglycerate
-
-
1.1
D-3-phosphoglycerate
-
Km at pH 7.5 is lower than at pH 8.8
0.0053
NAD+
pH 7.5, temperature not specified in the publication
0.0078
NAD+
-
Km at pH 7.5 is lower than at pH 8.8
0.022
NAD+
-
with 3-phospho-D-glycerate as cosubstrate, at pH 7.6 and 37°C
0.027
NAD+
pH 7.0, temperature not specified in the publication
0.0304
NAD+
pH 8.5, temperature not specified in the publication
0.04
NAD+
-
value for 3-phospho-D-glycerate oxidation
0.096
NAD+
pH 9.0, temperature not specified in the publication
0.189
NAD+
isoform PGDH2, at pH 8.1 and 37°C
0.239
NAD+
isoform PGDH3, at pH 8.1 and 37°C
0.271
NAD+
isoform PGDH2, at pH 7.2 and 37°C
0.377
NAD+
isoform PGDH1, at pH 7.2 and 37°C
0.39
NAD+
isoform PGDH1, at pH 8.1 and 37°C
0.551
NAD+
isoform PGDH3, at pH 7.2 and 37°C
0.0005
NADH
-
25°C
0.0013
NADH
-
value for 3-phosphohydroxypyruvate reduction using NADH as a cofactor
0.004
NADH
-
with 2-oxoglutarate as cosubstrate, at pH 7.6 and 37°C
0.004
NADH
-
with oxaloacetate as cosubstrate, at pH 7.6 and 37°C
0.025
NADH
pH 7.0, temperature not specified in the publication
0.114
NADH
pH 7.5, 25°C, recombinant mutant G316V
0.12
NADH
pH 7.5, 25°C, recombinant mutant N481A
0.14
NADH
pH 7.5, 25°C, recombinant mutant D463A
0.165
NADH
pH 7.5, 25°C, recombinant mutant G317V
0.17
NADH
pH 7.5, 25°C, wild-type enzyme
0.203
NADH
pH 7.5, 25°C, recombinant mutant G318V
0.22
NADH
pH 7.5, 25°C, recombinant mutant G317V/G318V
0.27
NADH
pH 7.5, 25°C, recombinant mutant Y461A
0.47
NADH
pH 7.5, 25°C, recombinant mutant G316V/G318V
0.61
NADH
pH 7.5, 25°C, recombinant mutant G316V/G317V
0.02
NADPH
-
value for 3-phosphohydroxypyruvate reduction using NADPH as a cofactor
3.9
oxaloacetate
pH 6.0, 25°C
6.5
oxaloacetate
-
at pH 7.6 and 37°C
11.2
oxaloacetate
pH 6.0, 25°C
14.1
oxaloacetate
pH 6.0, 25°C
additional information
additional information
-
-
-
additional information
additional information
kinetics, overview
-
additional information
additional information
-
kinetics, overview
-
additional information
additional information
kinetic analysis of wild-type and mutant enzymes
-
additional information
additional information
-
kinetic analysis of wild-type and mutant enzymes
-
additional information
additional information
stopped flow and steady-state kinetic analysis
-
additional information
additional information
-
stopped flow and steady-state kinetic analysis
-
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0.016
(3,4-dichlorophenyl)(morpholin-4-yl)methanethione
Homo sapiens
pH 8.8, 25°C
-
0.012
(3R)-N-(4,6-dimethylpyridin-2-yl)-3-methyl-4-[[4-(trifluoromethyl)phenyl]methyl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.0099
(3S)-N-(4,6-dimethylpyridin-2-yl)-3-methyl-4-[[4-(trifluoromethyl)phenyl]methyl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.077
1-(2,4-dichlorophenyl)-2-morpholino-2-thioxoethan-1-one
Homo sapiens
pH 8.5, temperature not specified in the publication
-
0.1607
1-(2-bromophenyl)-2-(morpholin-4-yl)-2-sulfanylideneethan-1-one
Homo sapiens
pH 8.8, 25°C
-
0.1307
1-(4-bromophenyl)-2-(morpholin-4-yl)-2-sulfanylideneethan-1-one
Homo sapiens
pH 8.8, 25°C
-
0.00987
1-(4-chlorophenyl)-2-(morpholin-4-yl)-2-sulfanylideneethan-1-one
Homo sapiens
pH 8.8, 25°C
-
0.0203
1-(4-chlorophenyl)-2-morpholino-2-thioxoethan-1-one
Homo sapiens
pH 8.5, temperature not specified in the publication
-
0.0689
1-(4-fluorophenyl)-2-(morpholin-4-yl)-2-sulfanylideneethan-1-one
Homo sapiens
pH 8.8, 25°C
-
0.1777
1-(4-iodophenyl)-2-(morpholin-4-yl)-2-sulfanylideneethan-1-one
Homo sapiens
pH 8.8, 25°C
-
0.0851
2-(4-methylpiperidin-1-yl)-1-phenyl-2-thioxoethan-1-one
Homo sapiens
pH 8.5, temperature not specified in the publication
-
0.0881
2-(morpholin-4-yl)-1-(3-nitrophenyl)-2-sulfanylideneethan-1-one
Homo sapiens
pH 8.8, 25°C
-
0.0351
2-(morpholin-4-yl)-1-(4-nitrophenyl)-2-sulfanylideneethan-1-one
Homo sapiens
pH 8.8, 25°C
-
0.0309
2-(morpholin-4-yl)-1-phenyl-2-sulfanylideneethan-1-one
Homo sapiens
pH 8.8, 25°C
-
0.131
2-methyl-N-(2-[[(2E)-2-[2-[(2-nitrobenzyl)oxy]benzylidene]hydrazinyl]carbonyl]phenyl)benzamide
Escherichia coli
at pH 7.5 and 25°C
0.111
2-morpholino-1-phenyl-2-thioxoethan-1-one
Homo sapiens
pH 8.5, temperature not specified in the publication
-
0.058
4-(5-[(Z)-[1-(3,4-dimethylphenyl)-3,5-dioxopyrazolidin-4-ylidene]methyl]furan-2-yl)-N-(1,3-thiazol-2-yl)benzenesulfonamide
Escherichia coli
at pH 7.5 and 25°C
0.04
4-benzyl-N-(4,6-dimethylpyridin-2-yl)piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.0752
4-chloro-N-(2-nitrophenyl)benzamide
Homo sapiens
pH 8.8, 25°C
-
0.02
4-[(2-chlorophenyl)methyl]-N-(4,6-dimethylpyridin-2-yl)piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.0348
4-[(3,5-dioxo-1,2,6-thiadiazinan-4-ylidene)methyl]phenyl 2,3-diphenylquinoxaline-6-carboxylate
Escherichia coli
at pH 7.5 and 25°C
0.011
4-[(3-chlorophenyl)methyl]-N-(4,6-dimethylpyridin-2-yl)piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.033
4-[(4,6-dimethylpyridin-2-yl)carbamothioyl]-1-[[4-(trifluoromethyl)phenyl]methyl]piperazine-2-carboxylic acid
Homo sapiens
pH 8.0, 22°C
-
0.017
4-[(4-bromophenyl)methyl]-N-(4,6-dimethylpyridin-2-yl)piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.0064 - 0.037
4-[3-(trifluoromethyl)phenyl]-N-[4-(trifluoromethyl)pyridin-2-yl]piperazine-1-carbothioamide
-
0.033
5-[(2-furanylcarbonyl)amino]-3-methyl-4-thiocyanato-2-thiophenecarboxylic acid ethyl ester
Homo sapiens
pH and temperature not specified in the publication
-
0.0098
azacoccone E
Homo sapiens
pH and temperature not specified in the publication
-
0.00166
ixocarpalactone A
Homo sapiens
pH and temperature not specified in the publication
-
0.013
methyl 2-([4-[3-(trifluoromethyl)phenyl]piperazine-1-carbothioyl]amino)pyridine-4-carboxylate
Homo sapiens
pH 8.0, 22°C
-
0.106
morpholino(phenyl)methanethione
Homo sapiens
pH 8.5, temperature not specified in the publication
-
0.0073
N'-(4,6-dimethylpyridin-2-yl)-N-methyl-N-[2-(methyl[[4-(trifluoromethyl)phenyl]methyl]amino)ethyl]thiourea
Homo sapiens
pH 8.0, 22°C
-
0.01
N-(4,6-dimethylpyridin-2-yl)(oxo)[4-(trifluoromethyl)phenyl]ethanethioamide
Homo sapiens
pH 8.0, 22°C
-
0.0058
N-(4,6-dimethylpyridin-2-yl)-3-(hydroxymethyl)-4-[[4-(trifluoromethyl)phenyl]methyl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.012
N-(4,6-dimethylpyridin-2-yl)-3-([[4-(trifluoromethyl)phenyl]methyl]amino)piperidine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.0083
N-(4,6-dimethylpyridin-2-yl)-3-methyl-4-[[4-(trifluoromethyl)phenyl]methyl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.031
N-(4,6-dimethylpyridin-2-yl)-3-phenyl-4-[[4-(trifluoromethyl)phenyl]methyl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.0072
N-(4,6-dimethylpyridin-2-yl)-3-[3-(trifluoromethyl)anilino]piperidine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.0057 - 0.01
N-(4,6-dimethylpyridin-2-yl)-3-[4-(trifluoromethyl)anilino]piperidine-1-carbothioamide
-
0.024
N-(4,6-dimethylpyridin-2-yl)-4-(2-methoxyphenyl)piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.014
N-(4,6-dimethylpyridin-2-yl)-4-(3-methoxyphenyl)piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.0025
N-(4,6-dimethylpyridin-2-yl)-4-(4-(trifluoromethyl)benzyl)piperazine-1-carbothioamide
Homo sapiens
pH and temperature not specified in the publication
-
0.016
N-(4,6-dimethylpyridin-2-yl)-4-(4-methoxyphenyl)piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.037
N-(4,6-dimethylpyridin-2-yl)-4-(pyridin-2-yl)piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.05
N-(4,6-dimethylpyridin-2-yl)-4-(pyridin-3-yl)piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.041
N-(4,6-dimethylpyridin-2-yl)-4-[(2-fluorophenyl)methyl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.0092
N-(4,6-dimethylpyridin-2-yl)-4-[(2-methylphenyl)methyl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.039
N-(4,6-dimethylpyridin-2-yl)-4-[(3-fluorophenyl)methyl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.02
N-(4,6-dimethylpyridin-2-yl)-4-[(3-methylphenyl)methyl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.038
N-(4,6-dimethylpyridin-2-yl)-4-[(4-fluorophenyl)methyl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.015 - 0.017
N-(4,6-dimethylpyridin-2-yl)-4-[(4-methylphenyl)methyl]piperazine-1-carbothioamide
-
0.05
N-(4,6-dimethylpyridin-2-yl)-4-[(pyridin-2-yl)methyl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.059
N-(4,6-dimethylpyridin-2-yl)-4-[(pyridin-4-yl)methyl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.0087
N-(4,6-dimethylpyridin-2-yl)-4-[2-(trifluoromethyl)phenyl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.023
N-(4,6-dimethylpyridin-2-yl)-4-[2-[4-(trifluoromethyl)phenyl]ethyl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.0065
N-(4,6-dimethylpyridin-2-yl)-4-[3-(trifluoromethyl)anilino][1,4'-bipiperidine]-1'-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.022
N-(4,6-dimethylpyridin-2-yl)-4-[3-(trifluoromethyl)benzoyl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.0063
N-(4,6-dimethylpyridin-2-yl)-4-[3-(trifluoromethyl)phenyl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.0077
N-(4,6-dimethylpyridin-2-yl)-4-[4-(trifluoromethyl)anilino][1,4'-bipiperidine]-1'-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.019
N-(4,6-dimethylpyridin-2-yl)-4-[4-(trifluoromethyl)benzoyl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.0043
N-(4,6-dimethylpyridin-2-yl)-4-[4-(trifluoromethyl)phenyl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.0037
N-(4,6-dimethylpyridin-2-yl)-4-[5-(trifluoromethyl)pyridin-2-yl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.011
N-(4,6-dimethylpyridin-2-yl)-4-[6-(trifluoromethyl)pyridin-2-yl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.0063
N-(4,6-dimethylpyridin-2-yl)-4-[[2-(trifluoromethyl)phenyl]methyl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.0053
N-(4,6-dimethylpyridin-2-yl)-4-[[3-(trifluoromethyl)phenyl]methyl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.011
N-(4,6-dimethylpyridin-2-yl)-4-[[4-(trifluoromethoxy)phenyl]methyl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.0073 - 0.008
N-(4,6-dimethylpyridin-2-yl)-4-[[4-(trifluoromethyl)phenyl]methyl]-1,4-diazepane-1-carbothioamide
-
0.0025
N-(4,6-dimethylpyridin-2-yl)-4-[[4-(trifluoromethyl)phenyl]methyl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.016
N-(4,6-dimethylpyridin-2-yl)-5-[[4-(trifluoromethyl)phenyl]methyl]hexahydropyrrolo[3,4-c]pyrrole-2(1H)-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.021
N-(4,6-dimethylpyridin-2-yl)-N'-[2-(methyl[[4-(trifluoromethyl)phenyl]methyl]amino)ethyl]thiourea
Homo sapiens
pH 8.0, 22°C
-
0.0097
N-(4,6-dimethylpyridin-2-yl)-N'-[2-([[4-(trifluoromethyl)phenyl]methyl]amino)ethyl]thiourea
Homo sapiens
pH 8.0, 22°C
-
0.015
N-(4,6-dimethylpyridin-2-yl)[4-(trifluoromethyl)phenyl]ethanethioamide
Homo sapiens
pH 8.0, 22°C
-
0.0153
N-(4-methylpyridin-2-yl)-4-[3-(trifluoromethyl)phenyl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.021
N-(4-methylquinolin-2-yl)-4-[3-(trifluoromethyl)phenyl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.0069
N-(pyridin-2-yl)-4-[3-(trifluoromethyl)phenyl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.0089
N-(pyridin-3-yl)-4-[3-(trifluoromethyl)phenyl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.014
N-(pyridin-4-yl)-4-[3-(trifluoromethyl)phenyl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.01
N-(quinolin-2-yl)-4-[3-(trifluoromethyl)phenyl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.0921
N-morpholinobenzenesulfonamide
Homo sapiens
pH 8.5, temperature not specified in the publication
-
0.021
N-[(pyridin-2-yl)methyl]-4-[3-(trifluoromethyl)phenyl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.011
N-[1'-[(4,6-dimethylpyridin-2-yl)carbamothioyl][1,4'-bipiperidin]-4-yl]-3-(trifluoromethyl)benzamide
Homo sapiens
pH 8.0, 22°C
-
0.0087
N-[1-[(4,6-dimethylpyridin-2-yl)carbamothioyl]piperidin-3-yl]-4-(trifluoromethyl)benzamide
Homo sapiens
pH 8.0, 22°C
-
0.03
[4-[(4,6-dimethylpyridin-2-yl)carbamothioyl]piperazin-1-yl]methyl 3-methoxybenzoate
Homo sapiens
pH 8.0, 22°C
-
0.026
[4-[(4,6-dimethylpyridin-2-yl)carbamothioyl]piperazin-1-yl]methyl 4-methoxybenzoate
Homo sapiens
pH 8.0, 22°C
-
0.0064
4-[3-(trifluoromethyl)phenyl]-N-[4-(trifluoromethyl)pyridin-2-yl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.037
4-[3-(trifluoromethyl)phenyl]-N-[4-(trifluoromethyl)pyridin-2-yl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.0057
N-(4,6-dimethylpyridin-2-yl)-3-[4-(trifluoromethyl)anilino]piperidine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.01
N-(4,6-dimethylpyridin-2-yl)-3-[4-(trifluoromethyl)anilino]piperidine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.015
N-(4,6-dimethylpyridin-2-yl)-4-[(4-methylphenyl)methyl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.017
N-(4,6-dimethylpyridin-2-yl)-4-[(4-methylphenyl)methyl]piperazine-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.0073
N-(4,6-dimethylpyridin-2-yl)-4-[[4-(trifluoromethyl)phenyl]methyl]-1,4-diazepane-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
0.008
N-(4,6-dimethylpyridin-2-yl)-4-[[4-(trifluoromethyl)phenyl]methyl]-1,4-diazepane-1-carbothioamide
Homo sapiens
pH 8.0, 22°C
-
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E108A
-
in contrast to wild-type mutant existed as monomer even at pH 7
K263A
the mutant shows strongly reduced activity compared to the wild type enzyme
A143A
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
A144V
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
A374V
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
D317A
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
D386A
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
E299A
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
E302A
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
E307A
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
E345A
site-directed mutagenesis, mutation of a residue in the serine binding site, the mutant shows only slightly altered kinetics and activity compared to the wild-type enzyme
E360A
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
E387A
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
G145V
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
G336V/G337V
changing glycine residues 336 and 337 to valine affect the sensitivity of the enzyme to inhibition by L-serine but not the extent of inhibition. The decrease in sensitivity is caused primarily by a decrease in the affinity of the enzyme for L-serine. The mutations also affect the domain rotation of the subunits in response to L-serine binding
G337V
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
G349V
site-directed mutagenesis, mutation of a residue in the serine binding site, the mutant shows only slightly altered kinetics and activity compared to the wild-type enzyme
G362V
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
H335A
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
H344A/N364A
-
no inhibition by L-serine
K141A
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
K141R
kcat/KM for 2-oxoglutarate is 4.8fold lower than the value for the wild-type enzyme, kcat/KM for 3-phosphooxypyruvate is 2.6fold higher than the value for the wild-type enzyme
K311A
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
N190A
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, no protein expression
N303A
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
N303A/K311A
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
N346A/H344A
-
no inhibition by L-serine
N346A/N364A
-
no inhibition by L-serine
P348A
site-directed mutagenesis, mutation of a residue in the serine binding site, the mutant shows only slightly altered kinetics and activity compared to the wild-type enzyme
Q298A
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
Q301A
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
Q361A
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
Q375A
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
R338A
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
R347A
site-directed mutagenesis, mutation of a residue in the serine binding site, the mutant shows only slightly altered kinetics and activity compared to the wild-type enzyme
S107A
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
S107A/S111A
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
S111A
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
S111A/K311A
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
S296A
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
S316A
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
S323A
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
S373A
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
T297A
site-directed mutagenesis, mutation of a residue in the polypeptide connecting the substrate binding domain and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
W139F/E360W
exhibits catalytic activity comparable to that of the native enzyme and is effectively inhibited by L-serine. The only fluorescence signal of the mutant is due to the single tryptophan at position 360. Pre-steady state analysis of binding of inhibitor serine shows that each serine binding interface produces an integrated fluorescent signal
W139F/E360W/G294V
-
placement of a tryptophanyl residue near the serine binding site (W139F/E360W) allows serine binding to be monitored by fluorescence quenching analysis. Pre-steady state analysis demonstrate that serine binds to two forms of the free enzyme, E and E*. Conversion of Gly-336 to valine has its main effect on the Kd of serine binding to one form of the free enzyme (E) while maintaining the cooperativity of binding observed in the native enzyme
W139F/E360W/G336V
-
placement of a tryptophanyl residue near the serine binding site (W139F/E360W) allows serine binding to be monitored by fluorescence quenching analysis. Pre-steady state analysis demonstrate that serine binds to two forms of the free enzyme, E and E*. Conversion of Gly-294 to valine eliminates a rate limiting conformational change that follows serine binding to E. The conformational change between the two forms of free enzyme is maintained, but the Hill coefficient for cooperativity is significantly lowered
K141R
-
kcat/KM for 2-oxoglutarate is 4.8fold lower than the value for the wild-type enzyme, kcat/KM for 3-phosphooxypyruvate is 2.6fold higher than the value for the wild-type enzyme
-
A373T
naturally occuring mutation located in the nucleotide binding and regulatory domains of 3-PGDH, the mutation does not affect steady-state expression, protein stability, and protein degradation rates, the mutant is almost catalytically inactive
G377S
naturally occuring mutation located in the nucleotide binding and regulatory domains of 3-PGDH, the mutation does not affect steady-state expression, protein stability, and protein degradation rates, the mutant is almost catalytically inactive
R135W
naturally occuring mutation located in the nucleotide binding and regulatory domains of 3-PGDH, the mutation does not affect steady-state expression, protein stability, and protein degradation rates, the mutant is almost catalytically inactive
V261M
naturally occuring mutation located in the nucleotide binding and regulatory domains of 3-PGDH, the mutation does not affect steady-state expression, protein stability, and protein degradation rates, the mutant is almost catalytically inactive
V425M
naturally occuring mutation in the carboxy-terminal regulatory domain, leads to 3-PGDH deficiency, the mutant is almost catalytically inactive
V490M
naturally occuring mutation in the carboxy-terminal regulatory domain, leads to 3-PGDH deficiency, the mutant is almost catalytically inactive
up
-
Phgdh is transiently upregulated in the brain by kainic acid-treatment, causing selective lesions in the hippocampal region, kainic acid is injected into the bregma, overview
D463A
site-directed mutagenesis, a very large reduction in the sensitivity of the mutant enzyme to L-serine
G316V
site-directed mutagenesis, the mutant shows slightly reduced activity and decreased sensitivity to L-serine compared to the wild-type
G316V/G317V
site-directed mutagenesis, the mutant shows reduced activity and decreased sensitivity to L-serine compared to the wild-type
G316V/G317V/G318V
site-directed mutagenesis, the mutant is not producable
G316V/G318V
site-directed mutagenesis, the mutant shows reduced activity and decreased sensitivity to L-serine compared to the wild-type
G317V
site-directed mutagenesis, the mutant shows slightly reduced activity and decreased sensitivity to L-serine compared to the wild-type
G317V/G318V
site-directed mutagenesis, the mutant shows reduced activity and decreased sensitivity to L-serine compared to the wild-type
G318V
site-directed mutagenesis, the mutant shows slightly reduced activity and decreased sensitivity to L-serine compared to the wild-type
K439A/R451A/R501A
site-directed mutagenesis, the mutation eliminates substrate inhibition and pH-dependent depression in activity
N481A
site-directed mutagenesis, a very large reduction in the sensitivity of the mutant enzyme to L-serine. Mutant N481A co-elutes with native PGDH in gel filtration, it shows loss of cooperativity, which cannot be explained by a change in the quaternary structure of the enzyme from tetramer to dimer or monomer
R132K
mutation decreases the Km-value for 3-phosphooxypyruvate by approximately 10fold
R451A/R501A/K439A
site-directed mutagenesis, the mutation eliminates substrate inhibition and pH-dependent depression in activity
R501A/R451A/K439A
anion binding site mutant: Km (mM) (3-phosphohydroxypyruvate): 0.243, kcat: 1558, Ki (mM) (3-phosphohydroxypyruvate): 7.218, mutant displays only little uncompetitive substrate inhibition, no dual pH optima compared to wild-type
R72A
mutant enzyme utilize 2-oxoglutarate as substrate
R72L
mutant enzyme utilize 2-oxoglutarate as substrate
W130F
site-directed mutagenesis, catalytically inactive mutant
W29F
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
W327F
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
Y461A
site-directed mutagenesis, a very large reduction in the sensitivity of the mutant enzyme to L-serine
D463A
-
site-directed mutagenesis, a very large reduction in the sensitivity of the mutant enzyme to L-serine
-
G316V
-
site-directed mutagenesis, the mutant shows slightly reduced activity and decreased sensitivity to L-serine compared to the wild-type
-
G316V/G317V/G318V
-
site-directed mutagenesis, the mutant is not producable
-
N481A
-
site-directed mutagenesis, a very large reduction in the sensitivity of the mutant enzyme to L-serine. Mutant N481A co-elutes with native PGDH in gel filtration, it shows loss of cooperativity, which cannot be explained by a change in the quaternary structure of the enzyme from tetramer to dimer or monomer
-
R132K
-
mutation decreases the Km-value for 3-phosphooxypyruvate by approximately 10fold
-
R72A
-
mutant enzyme utilize 2-oxoglutarate as substrate
-
R72L
-
mutant enzyme utilize 2-oxoglutarate as substrate
-
Y461A
-
site-directed mutagenesis, a very large reduction in the sensitivity of the mutant enzyme to L-serine
-
G336V
site-directed mutagenesis, mutation of a residue in the Trp-139-loop and the regulatory domain, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
G336V
changing glycine residues 336 and/or 337 to valine affect the sensitivity of the enzyme to inhibition by L-serine but not the extent of inhibition. The decrease in sensitivity is caused primarily by a decrease in the affinity of the enzyme for L-serine. The mutations also affect the domain rotation of the subunits in response to L-serine binding. Crystal structure of G336V demonstrates that the minimal effect of L-serine binding leading to inhibition of enzyme activity requires a domain rotation of approximately only 6° in just two of the four subunits of the enzyme that are oriented diagonally across from each other in the tetramer
H344A
-
50% inhibition at 0.8 mM L-serine
H344A
site-directed mutagenesis, mutation of a residue in the serine binding site, the mutant shows only slightly altered kinetics and activity compared to the wild-type enzyme
N346A
-
50% inhibition at 6 mM L-serine
N346A
site-directed mutagenesis, mutation of a residue in the serine binding site, the mutant shows only slightly altered kinetics and activity compared to the wild-type enzyme
N364A
-
50% inhibition at 48 mM L-serine
N364A
site-directed mutagenesis, mutation of a residue in the serine binding site, the mutant shows only slightly altered kinetics and activity compared to the wild-type enzyme
H447A
anion binding site mutant: Km (mM) (3-phosphohydroxypyruvate): 0.16, kcat: 1446, Ki (mM) (3-phosphohydroxypyruvate): 0.87, mutant displays complete uncompetitive substrate inhibition, no dual pH optima compared to wild-type
H447A
site-directed mutagenesis, the mutant shows altered L-serine binding, kinetics for NADH, and activity compared to the wild-type enzyme
K439A
anion binding site mutant: Km (mM) (3-phosphohydroxypyruvate): 0.075, kcat: 368, Ki (mM) (3-phosphohydroxypyruvate): 0.054, mutant displays partial uncompetitive substrate inhibition, mutant retains dual pH optima
K439A
site-directed mutagenesis, the mutant shows altered L-serine binding, kinetics for NADH, and activity compared to the wild-type enzyme
R446A
anion binding site mutant: Km (mM) (3-phosphohydroxypyruvate): 0.123 kcat: 467, Ki (mM) (3-phosphohydroxypyruvate): 0.289, mutant displays partial uncompetitive substrate inhibition, no dual pH optima compared to wild-type
R446A
site-directed mutagenesis, the mutant shows altered L-serine binding, kinetics for NADH, and activity compared to the wild-type enzyme
R451A
anion binding site mutant: Km (mM) (3-phosphohydroxypyruvate): 0.19, kcat: 1881, Ki (mM) (3-phosphohydroxypyruvate): 0.95, mutant displays complete uncompetitive substrate inhibition, no dual pH optima compared to wild-type
R451A
site-directed mutagenesis, the mutant shows altered L-serine binding, kinetics for NADH, and activity compared to the wild-type enzyme
R501A
anion binding site mutant: Km (mM) (3-phosphohydroxypyruvate): 0.18, kcat: 1989, Ki (mM) (3-phosphohydroxypyruvate): 1.02, mutant displays complete uncompetitive substrate inhibition, no dual pH optima compared to wild-type
R501A
site-directed mutagenesis, the mutant shows altered L-serine binding, kinetics for NADH, and activity compared to the wild-type enzyme
H447A
-
anion binding site mutant: Km (mM) (3-phosphohydroxypyruvate): 0.16, kcat: 1446, Ki (mM) (3-phosphohydroxypyruvate): 0.87, mutant displays complete uncompetitive substrate inhibition, no dual pH optima compared to wild-type
-
H447A
-
site-directed mutagenesis, the mutant shows altered L-serine binding, kinetics for NADH, and activity compared to the wild-type enzyme
-
K439A
-
anion binding site mutant: Km (mM) (3-phosphohydroxypyruvate): 0.075, kcat: 368, Ki (mM) (3-phosphohydroxypyruvate): 0.054, mutant displays partial uncompetitive substrate inhibition, mutant retains dual pH optima
-
K439A
-
site-directed mutagenesis, the mutant shows altered L-serine binding, kinetics for NADH, and activity compared to the wild-type enzyme
-
R446A
-
anion binding site mutant: Km (mM) (3-phosphohydroxypyruvate): 0.123 kcat: 467, Ki (mM) (3-phosphohydroxypyruvate): 0.289, mutant displays partial uncompetitive substrate inhibition, no dual pH optima compared to wild-type
-
R446A
-
site-directed mutagenesis, the mutant shows altered L-serine binding, kinetics for NADH, and activity compared to the wild-type enzyme
-
R451A
-
anion binding site mutant: Km (mM) (3-phosphohydroxypyruvate): 0.19, kcat: 1881, Ki (mM) (3-phosphohydroxypyruvate): 0.95, mutant displays complete uncompetitive substrate inhibition, no dual pH optima compared to wild-type
-
R451A
-
site-directed mutagenesis, the mutant shows altered L-serine binding, kinetics for NADH, and activity compared to the wild-type enzyme
-
R501A
-
anion binding site mutant: Km (mM) (3-phosphohydroxypyruvate): 0.18, kcat: 1989, Ki (mM) (3-phosphohydroxypyruvate): 1.02, mutant displays complete uncompetitive substrate inhibition, no dual pH optima compared to wild-type
-
R501A
-
site-directed mutagenesis, the mutant shows altered L-serine binding, kinetics for NADH, and activity compared to the wild-type enzyme
-
additional information
-
expression of the Aphanothece PGDH gene in Escherichia coli causes an increase in levels of betaine as well as glycine and serine. Expression of the Aphanothece PGDH gene in Arabidopsis thaliana, in which the betaine synthetic pathway is introduced via glycine methylation, further increases betaine levels and improves the stress tolerance
additional information
-
expression of GFP-mutant enzyme in Arabidopsis to investigate the tissue distribution, complementation of Escherichia coli serA- mutant
additional information
-
C-terminally truncated SerA-mutant 197 shows phosphoglycerate dehydrogenase activity of 1.3 U/mg protein, the activity is no longer sensitive to L-Ser. The mutant enzyme exists as a dimer
additional information
-
construction of an L-serine-insensitive mutant serADELAT197
additional information
-
diverse mutants with different interaction between the 3 binding domains of each of 4 subunits and modified kinetics
additional information
-
diverse mutants with modified active siteand increased Km values
additional information
-
sequence analysis of the PHGDH promoter region exhibits several putative transcription factor binding sites for NF-Y, Sp1, GATA-1, p53, AP2, and AP1, with no TATA-box motif at an appropriate position. Transfection of a series of deletion constructs of the promoter region into HeLa cells reveals that the core positive promoter activity resides in the -276 to +1, which contains two GC-motifs for binding Sp1 and one CCAAT-motif for NF-Y. Mutational analysis and electrophoretic mobility shift assay indicates that both the proximal GC-motif and CCAAT-motif are crucial for full induction of the promoter activity
additional information
p.G238fsX is a naturally occuring frameshift mutation, the mutant is almost catalytically inactive with a 4fold increased Km for 3-phosphohydroxypyruvate
additional information
-
p.G238fsX is a naturally occuring frameshift mutation, the mutant is almost catalytically inactive with a 4fold increased Km for 3-phosphohydroxypyruvate
additional information
-
generation of Phgdh heterozygous mice, Phgdh+/-, using E14 embryonic stem cells 129P2/OlaHsd background
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Mus musculus
-
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Entamoeba histolytica (Q76KF5), Entamoeba histolytica
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Escherichia coli (P0A9T0), Escherichia coli
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Entamoeba histolytica
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Mycobacterium tuberculosis
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Entamoeba histolytica
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2015
Acanthamoeba castellanii (U3RH61), Acanthamoeba castellanii, Acanthamoeba castellanii ATCC 30011 (U3RH61)
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Benstein, R.M.; Ludewig, K.; Wulfert, S.; Wittek, S.; Gigolashvili, T.; Frerigmann, H.; Gierth, M.; Fluegge, U.I.; Krueger, S.
Arabidopsis phosphoglycerate dehydrogenase1 of the phosphoserine pathway is essential for development and required for ammonium assimilation and tryptophan biosynthesis
Plant Cell
25
5011-5029
2013
Arabidopsis thaliana (O04130), Arabidopsis thaliana (O49485), Arabidopsis thaliana (Q9LT69), Arabidopsis thaliana
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Toujani, W.; Munoz-Bertomeu, J.; Flores-Tornero, M.; Rosa-Tellez, S.; Anoman, A.D.; Alseekh, S.; Fernie, A.R.; Ros, R.
Functional characterization of the plastidial 3-phosphoglycerate dehydrogenase family in Arabidopsis
Plant Physiol.
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2013
Arabidopsis thaliana (Q9LT69), Arabidopsis thaliana
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Toujani, W.; Munoz-Bertomeu, J.; Flores-Tornero, M.; Rosa-Tellez, S.; Anoman, A.; Ros, R.
Identification of the phosphoglycerate dehydrogenase isoform EDA9 as the essential gene for embryo and male gametophyte development in Arabidopsis
Plant Signal. Behav.
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Arabidopsis thaliana (O49485)
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Wang, Q.; Qi, Y.; Yin, N.; Lai, L.
Discovery of novel allosteric effectors based on the predicted allosteric sites for Escherichia coli D-3-phosphoglycerate dehydrogenase
PLoS ONE
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2014
Escherichia coli (P0A9T0), Escherichia coli
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Xu, X.L.; Grant, G.A.
Determinants of substrate specificity in D-3-phosphoglycerate dehydrogenase. Conversion of the M. tuberculosis enzyme from one that does not use alpha-ketoglutarate as a substrate to one that does
Arch. Biochem. Biophys.
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218-224
2019
Escherichia coli (P0A9T0), Escherichia coli, Mycobacterium tuberculosis (P9WNX3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WNX3), Escherichia coli K12 (P0A9T0)
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Yamamoto, K.; Mohri, S.; Furuya, S.
D-3-phosphoglycerate dehydrogenase from the silkworm Bombyx mori Identification, functional characterization, and expression
Arch. Insect Biochem. Physiol.
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2021
Bombyx mori (H9JRZ9), Bombyx mori
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Rohde, J.M.; Brimacombe, K.R.; Liu, L.; Pacold, M.E.; Yasgar, A.; Cheff, D.M.; Lee, T.D.; Rai, G.; Baljinnyam, B.; Li, Z.; Simeonov, A.; Hall, M.D.; Shen, M.; Sabatini, D.M.; Boxer, M.B.
Discovery and optimization of piperazine-1-thiourea-based human phosphoglycerate dehydrogenase inhibitors
Bioorg. Med. Chem.
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1727-1739
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Homo sapiens (O43175), Homo sapiens
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Grant, G.A.
D-3-Phosphoglycerate dehydrogenase
Front. Mol. Biosci.
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110
2018
Escherichia coli (C3SVM7), Escherichia coli, Rattus norvegicus (O08651), Homo sapiens (O43175), Homo sapiens, Mycobacterium tuberculosis (P9WNX3), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 (P9WNX3)
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Akashi, H.; Okamura, E.; Nishihama, R.; Kohchi, T.; Hirai, M.Y.
Identification and biochemical characterization of the serine biosynthetic enzyme 3-phosphoglycerate dehydrogenase in Marchantia polymorpha
Front. Plant Sci.
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956
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Marchantia polymorpha (A0A2R6X868), Marchantia polymorpha
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Zhao, X.; Fu, J.; Du, J.; Xu, W.
The role of D-3-phosphoglycerate dehydrogenase in Cancer
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1495-1506
2020
Homo sapiens (O43175), Homo sapiens
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Yoshida, K.; Ohtaka, K.; Hirai, M.Y.; Hisabori, T.
Biochemical insight into redox regulation of plastidial 3-phosphoglycerate dehydrogenase from Arabidopsis thaliana
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Arabidopsis thaliana (O04130), Arabidopsis thaliana (O49485), Arabidopsis thaliana (Q9LT69), Arabidopsis thaliana
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Ravez, S.; Corbet, C.; Spillier, Q.; Dutu, A.; Robin, A.D.; Mullarky, E.; Cantley, L.C.; Feron, O.; Frederick, R.
alpha-Ketothioamide derivatives a promising tool to interrogate phosphoglycerate dehydrogenase (PHGDH)
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Homo sapiens (O43175)
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Unterlass, J.E.; Wood, R.J.; Basle, A.; Tucker, J.; Cano, C.; Noble, M.M.E.; Curtin, N.J.
Structural insights into the enzymatic activity and potential substrate promiscuity of human 3-phosphoglycerate dehydrogenase (PHGDH)
Oncotarget
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104478-104491
2017
Homo sapiens (O43175), Homo sapiens
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Spillier, Q.; Ravez, S.; Unterlass, J.; Corbet, C.; Degavre, C.; Feron, O.; Frederick, R.
Structure-activity relationships (SARs) of alpha-ketothioamides as inhibitors of phosphoglycerate dehydrogenase (PHGDH)
Pharmaceuticals
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20
2020
Homo sapiens (O43175)
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Zhang, W.; Zhang, M.; Gao, C.; Zhang, Y.; Ge, Y.; Guo, S.; Guo, X.; Zhou, Z.; Liu, Q.; Zhang, Y.; Ma, C.; Tao, F.; Xu, P.
Coupling between D-3-phosphoglycerate dehydrogenase and D-2-hydroxyglutarate dehydrogenase drives bacterial L-serine synthesis
Proc. Natl. Acad. Sci. USA
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E7574-E7582
2017
Pseudomonas stutzeri (A4VGK3), Pseudomonas aeruginosa (Q9I6H5), Pseudomonas stutzeri A1501 (A4VGK3), Pseudomonas stutzeri A1501
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Kito, K.; Tsutsumi, K.; Rai, V.; Theerawitaya, C.; Cha-Um, S.; Yamada-Kato, N.; Sakakibara, S.; Tanaka, Y.; Takabe, T.
Isolation and functional characterization of 3-phosphoglycerate dehydrogenase involved in salt responses in sugar beet
Protoplasma
254
2305-2313
2017
Beta vulgaris (A0A1Z4EAX3), Beta vulgaris (A0A1Z4EAX4)
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Okamura, E.; Hirai, M.Y.
Novel regulatory mechanism of serine biosynthesis associated with 3-phosphoglycerate dehydrogenase in Arabidopsis thaliana
Sci. Rep.
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3533
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Arabidopsis thaliana (O04130), Arabidopsis thaliana (O49485), Arabidopsis thaliana (Q9LT69), Arabidopsis thaliana
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