1.1.1.95: phosphoglycerate dehydrogenase
This is an abbreviated version!
For detailed information about phosphoglycerate dehydrogenase, go to the full flat file.
Word Map on EC 1.1.1.95
-
1.1.1.95
-
l-serine
-
aminotransferase
-
microcephaly
-
psychomotor
-
hydroxymethyltransferase
-
one-carbon
-
hydroxypyruvate
-
l-ser
-
2-hydroxyacid
-
biotechnology
-
molecular biology
-
synthesis
- 1.1.1.95
- l-serine
- aminotransferase
- microcephaly
-
psychomotor
- hydroxymethyltransferase
-
one-carbon
- hydroxypyruvate
- l-ser
-
2-hydroxyacid
- biotechnology
- molecular biology
- synthesis
Reaction
Synonyms
3-PGDH, 3-phosphoglycerate dehydrogenase, 3-phosphoglyceric acid dehydrogenase, 3PGDH, A10, alpha-phosphoglycerate dehydrogenase, ApPGDH, At1g17745, At3g19480, At4g34200, BvSHMTa, BvSHMTb, D-3-PG dehydrogenase, D-3-phosphoglycerate dehydrogenase, D-3-phosphoglycerate:NAD oxidoreductase, D-phosphoglycerate dehydrogenase, dehydrogenase, phosphoglycerate, EDA9, EhPGDH, glycerate 3-phosphate dehydrogenase, glycerate-1,3-phosphate dehydrogenase, MARPO_0030s0029, More, NAD-dependent D-3-phosphoglycerate dehydrogenase, PGDH, PGDH1, PGDH2, PGDH3, PGK, Phgdh, phosphoglycerate dehydrogenase, phosphoglycerate kinase, phosphoglycerate oxidoreductase, phosphoglyceric acid dehydrogenase, Rv2996c, serA, serA1, type 1 D-3-phosphoglycerate dehydrogenase, type III 3-phosphoglycerate dehydrogenase, type IIIK PGDH
ECTree
1.1.1.95 phosphoglycerate dehydrogenaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 1.1.1.95 - phosphoglycerate dehydrogenase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-phospho-D-glycerate + NAD+
2-phosphohydroxypyruvate + NADH + H+
-
activity relative to 3-phospho-D-glycerate: 47%
-
-
?
3-phosphohydroxypyruvate + NADH
3-phosphoglycerate + NAD+
-
specific for
-
-
?
3-phosphooxypyruvate + pyridinealdehyde adenine dinucleotide
3-phospho-D-glycerate + ?
-
-
-
r
3-phosphooxypyruvate + thionicotinamide
3-phospho-D-glycerate + ?
-
-
-
r
DL-glyceraldehyde 3-phosphate + NAD+
?
-
activity relative to 3-phospho-D-glycerate: 9%
-
-
?
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
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-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+
-
-
-
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+
enzyme in the L-serine biosynthetic pathway
-
-
?
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
-
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
-
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
-
-
-
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
-
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-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
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+
-
-
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+
?
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+
?
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+
?
catalytic His280, active site, regulatory, and substrate binding site structures, overview
-
-
?
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
?
-
-
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
-
-
?
