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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
-
-
?
alpha-ketoglutarate + NADH
2-hydroxyglutaric acid + NAD+
DL-glyceraldehyde 3-phosphate + NAD+
?
-
activity relative to 3-phospho-D-glycerate: 9%
-
-
?
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+
?
-
-
-
?
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 + 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
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-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
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-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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(NH4)2SO4
-
inhibitory effect on NADPH-dependent 3-phosphohydroxypyruvate reduction
(R)-2-amino-1-propanol
-
slightly
2-methyl-N-(2-[[(2E)-2-[2-[(2-nitrobenzyl)oxy]benzylidene]hydrazinyl]carbonyl]phenyl)benzamide
-
4-(5-[(Z)-[1-(3,4-dimethylphenyl)-3,5-dioxopyrazolidin-4-ylidene]methyl]furan-2-yl)-N-(1,3-thiazol-2-yl)benzenesulfonamide
-
4-[(3,5-dioxo-1,2,6-thiadiazinan-4-ylidene)methyl]phenyl 2,3-diphenylquinoxaline-6-carboxylate
-
Ag+
-
inhibition can be overcome by addition of dithiothreitol
AMP
-
weak inhibitory effect on 3-phospho-D-glycerate oxidation, remaining activity: 75%
hydroxyglutarate
-
product inhibition of the alpha-ketoglutarate reduction
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
-
NAD+
-
product inhibition, competitive to NADH
p-chloromercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxamine 5'-phosphate
-
-
ZnCl2
-
inhibitory effect on 3-phosphohydroxypyruvate reduction, remaining activity: 29%
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
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
-
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
-
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-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
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
-
unlike the Escherichia coli PGDH no inhibition by L-serine
-
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10.1
2-oxoglutarate
-
at pH 7.6 and 37ưC
0.00025 - 0.0054
3-acetylpyridine-NAD+
0.00016
3-acetylpyridine-NADH
-
25ưC
0.003 - 320
3-phospho-D-glycerate
0.212
3-phosphoglycerate
pH 9.0
0.00013 - 40.2
3-phosphohydroxypyruvate
0.038 - 0.088
alpha-ketoglutarate
0.15 - 1.1
D-3-phosphoglycerate
6.5
oxaloacetate
-
at pH 7.6 and 37ưC
0.015
phosphohydroxypyruvate
pH 6.5
additional information
additional information
-
0.00025
3-acetylpyridine-NAD+

-
25ưC
0.0054
3-acetylpyridine-NAD+
-
37ưC
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
-
-
0.065
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
0.19
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 37ưC
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
0.3
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 25ưC
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
0.58
3-phospho-D-glycerate
pH 7.5, mutant P348A
0.6
3-phospho-D-glycerate
mutant enzyme K263A, at pH 9.0 and 25ưC
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
0.79
3-phospho-D-glycerate
pH 7.5, mutant H335A
0.899
3-phospho-D-glycerate
isoform PGDH2, at pH 8.1 and 37ưC
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 37ưC
1.19
3-phospho-D-glycerate
-
pH 9.0
1.19
3-phospho-D-glycerate
pH 7.5, mutant A143V
1.308
3-phospho-D-glycerate
isoform PGDH1, at pH 8.1 and 37ưC
1.35
3-phospho-D-glycerate
-
-
1.37
3-phospho-D-glycerate
pH 7.5, mutant S296A
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 37ưC
1.99
3-phospho-D-glycerate
pH 7.5, mutant E299A
2.11
3-phospho-D-glycerate
isoform PGDH1, at pH 7.2 and 37ưC
2.559
3-phospho-D-glycerate
isoform PGDH3, at pH 7.2 and 37ưC
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

-
25ưC
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, 25ưC, wild-type enzyme from fibroblasts
0.0216
3-phosphohydroxypyruvate
pH 7.1, 25ưC, recombinant FLAG-tagged wild-type enzyme from HEK-293 cells
0.045
3-phosphohydroxypyruvate
-
25ưC
0.07
3-phosphohydroxypyruvate
-
37ưC
0.075
3-phosphohydroxypyruvate
mutant K439A
0.085
3-phosphohydroxypyruvate
-
pH 7.5, 37ưC
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
-
-
0.038
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
0.0078
NAD+

-
-
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 37ưC
0.04
NAD+
-
value for 3-phospho-D-glycerate oxidation
0.189
NAD+
isoform PGDH2, at pH 8.1 and 37ưC
0.239
NAD+
isoform PGDH3, at pH 8.1 and 37ưC
0.271
NAD+
isoform PGDH2, at pH 7.2 and 37ưC
0.377
NAD+
isoform PGDH1, at pH 7.2 and 37ưC
0.39
NAD+
isoform PGDH1, at pH 8.1 and 37ưC
0.551
NAD+
isoform PGDH3, at pH 7.2 and 37ưC
0.0005
NADH

-
25ưC
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 37ưC
0.004
NADH
-
with oxaloacetate as cosubstrate, at pH 7.6 and 37ưC
0.114
NADH
pH 7.5, 25ưC, recombinant mutant G316V
0.12
NADH
pH 7.5, 25ưC, recombinant mutant N481A
0.14
NADH
pH 7.5, 25ưC, recombinant mutant D463A
0.165
NADH
pH 7.5, 25ưC, recombinant mutant G317V
0.17
NADH
pH 7.5, 25ưC, wild-type enzyme
0.203
NADH
pH 7.5, 25ưC, recombinant mutant G318V
0.22
NADH
pH 7.5, 25ưC, recombinant mutant G317V/G318V
0.27
NADH
pH 7.5, 25ưC, recombinant mutant Y461A
0.47
NADH
pH 7.5, 25ưC, recombinant mutant G316V/G318V
0.61
NADH
pH 7.5, 25ưC, recombinant mutant G316V/G317V
0.02
NADPH

-
value for 3-phosphohydroxypyruvate reduction using NADPH as a cofactor
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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0.078
2-oxoglutarate
-
at pH 7.6 and 37ưC
0.075 - 3850
3-phospho-D-glycerate
0.463 - 2461
3-phosphohydroxypyruvate
0.128 - 0.555
alpha-ketoglutarate
0.177
oxaloacetate
-
at pH 7.6 and 37ưC
additional information
additional information
-
-
-
0.075
3-phospho-D-glycerate

-
at pH 7.6 and 37ưC
0.13
3-phospho-D-glycerate
mutant enzyme K263A, at pH 9.0 and 25ưC
1.741
3-phospho-D-glycerate
isoform PGDH1, at pH 8.1 and 37ưC
3.2
3-phospho-D-glycerate
pH 7.5, mutant K141A
4.2
3-phospho-D-glycerate
pH 7.5, mutant S111A/K311A
4.6
3-phospho-D-glycerate
pH 7.5, mutant D317A
4.9
3-phospho-D-glycerate
pH 7.5, mutants E299A and G337V
5.2
3-phospho-D-glycerate
pH 7.5, mutant K311A
5.8
3-phospho-D-glycerate
pH 7.5, mutant R338A
6
3-phospho-D-glycerate
pH 7.5, mutant G349V
6.4
3-phospho-D-glycerate
pH 7.5, mutant G362V
7
3-phospho-D-glycerate
pH 7.5, mutant T297A
7.4
3-phospho-D-glycerate
pH 7.5, mutant S296A
7.5
3-phospho-D-glycerate
pH 7.5, mutant S111A
7.8
3-phospho-D-glycerate
pH 7.5, mutant H335A
8.6
3-phospho-D-glycerate
pH 7.5, mutant A143V
8.7
3-phospho-D-glycerate
pH 7.5, mutant G145V
9
3-phospho-D-glycerate
pH 7.5, mutants S107A and Q361A
9.3
3-phospho-D-glycerate
pH 7.5, mutant P348A
9.6
3-phospho-D-glycerate
pH 7.5, mutant N303A/K311A
9.8
3-phospho-D-glycerate
pH 7.5, mutant H344A
9.9
3-phospho-D-glycerate
pH 7.5, mutant G336V
10.6
3-phospho-D-glycerate
pH 7.5, mutant Q301A
10.8
3-phospho-D-glycerate
pH 7.5, mutant E360A
11
3-phospho-D-glycerate
pH 7.5, mutant S323A
11.2
3-phospho-D-glycerate
pH 7.5, mutant E302A
11.4
3-phospho-D-glycerate
pH 7.5, mutant S107A/S111A
11.5
3-phospho-D-glycerate
pH 7.5, mutants Q298A and S316A
11.7
3-phospho-D-glycerate
pH 7.5, mutant A374V
11.8
3-phospho-D-glycerate
pH 7.5, mutant N364A
11.9
3-phospho-D-glycerate
pH 7.5, mutant E345A
11.9
3-phospho-D-glycerate
pH 7.5, mutant S373A
12.1
3-phospho-D-glycerate
pH 7.5, mutant R347A
12.3
3-phospho-D-glycerate
pH 7.5, mutant E307A
12.4
3-phospho-D-glycerate
pH 7.5, mutant N303A
12.8
3-phospho-D-glycerate
pH 7.5, mutant E387A
13.1
3-phospho-D-glycerate
pH 7.5, mutant D386A
13.5
3-phospho-D-glycerate
pH 7.5, wild-type enzyme
13.8
3-phospho-D-glycerate
pH 7.5, mutant A144V
14.9
3-phospho-D-glycerate
pH 7.5, mutant N346A
16.28
3-phospho-D-glycerate
wild type enzyme, at pH 9.0 and 25ưC
18.7
3-phospho-D-glycerate
pH 7.5, mutant Q375A
41
3-phospho-D-glycerate
-
in 50 mM MOPS buffer, pH 7.0, temperature not specified in the publication
97
3-phospho-D-glycerate
isoform PGDH3, at pH 7.2 and 37ưC
115.1
3-phospho-D-glycerate
isoform PGDH1, at pH 7.2 and 37ưC
119.7
3-phospho-D-glycerate
isoform PGDH2, at pH 7.2 and 37ưC
142.4
3-phospho-D-glycerate
isoform PGDH3, at pH 8.1 and 37ưC
147.4
3-phospho-D-glycerate
isoform PGDH2, at pH 8.1 and 37ưC
194
3-phospho-D-glycerate
in 50 mM MOPS buffer, pH 7.0, temperature not specified in the publication
198
3-phospho-D-glycerate
-
in 50 mM MOPS buffer, pH 7.0, temperature not specified in the publication
311
3-phospho-D-glycerate
-
in 200 mM KPO4 buffer, pH 7.0, temperature not specified in the publication
341
3-phospho-D-glycerate
-
in 200 mM KPO4 buffer, pH 7.0, temperature not specified in the publication
350
3-phospho-D-glycerate
-
in 200 mM KPO4 buffer, pH 7.0, temperature not specified in the publication
464
3-phospho-D-glycerate
-
in 50 mM MOPS buffer, pH 7.0, temperature not specified in the publication
567
3-phospho-D-glycerate
-
in 200 mM KPO4 buffer, pH 7.0, temperature not specified in the publication
576
3-phospho-D-glycerate
in 200 mM KPO4 buffer, pH 7.0, temperature not specified in the publication
608
3-phospho-D-glycerate
-
in 50 mM MOPS buffer, pH 7.0, temperature not specified in the publication
1515
3-phospho-D-glycerate
-
in 50 mM MOPS buffer, pH 7.0, temperature not specified in the publication
1575
3-phospho-D-glycerate
-
in 50 mM MOPS buffer, pH 7.0, temperature not specified in the publication
2425
3-phospho-D-glycerate
-
in 200 mM KPO4 buffer, pH 7.0, temperature not specified in the publication
3850
3-phospho-D-glycerate
-
in 200 mM KPO4 buffer, pH 7.0, temperature not specified in the publication
0.463
3-phosphohydroxypyruvate

-
apparent
368
3-phosphohydroxypyruvate
mutant K439A
467
3-phosphohydroxypyruvate
mutant R446A
1446
3-phosphohydroxypyruvate
mutant H447A
1558
3-phosphohydroxypyruvate
mutant R501A/R451A/K439A
1881
3-phosphohydroxypyruvate
mutant R451A
1989
3-phosphohydroxypyruvate
mutant R501A
2461
3-phosphohydroxypyruvate
-
0.128
alpha-ketoglutarate

-
-
0.137
alpha-ketoglutarate
-
double mutant H344A/N364A
0.32
alpha-ketoglutarate
-
mutant N346A
0.555
alpha-ketoglutarate
-
apparent
1.741
NAD+

isoform PGDH1, at pH 8.1 and 37ưC
97
NAD+
isoform PGDH3, at pH 7.2 and 37ưC
115.1
NAD+
isoform PGDH1, at pH 7.2 and 37ưC
119.7
NAD+
isoform PGDH2, at pH 7.2 and 37ưC
142.4
NAD+
isoform PGDH3, at pH 8.1 and 37ưC
147.4
NAD+
isoform PGDH2, at pH 8.1 and 37ưC
603
NADH

pH 7.5, 25ưC, recombinant mutant N481A
605
NADH
pH 7.5, 25ưC, recombinant mutant G317V/G318V
720
NADH
pH 7.5, 25ưC, recombinant mutant D463A
1111
NADH
pH 7.5, 25ưC, recombinant mutant G316V
2111
NADH
pH 7.5, 25ưC, recombinant mutant G317V
2349
NADH
pH 7.5, 25ưC, recombinant mutant G318V
2461
NADH
pH 7.5, 25ưC, wild-type enzyme
2754
NADH
pH 7.5, 25ưC, recombinant mutant Y461A
2805
NADH
pH 7.5, 25ưC, recombinant mutant G316V/G317V
2827
NADH
pH 7.5, 25ưC, recombinant mutant G316V/G318V
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.