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Information on EC 1.1.1.95 - phosphoglycerate dehydrogenase
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EC Tree
1.1.1.95 phosphoglycerate dehydrogenaseIUBMB Comments
This enzyme catalyses the first committed and rate-limiting step in the phosphoserine pathway of serine biosynthesis. The reaction occurs predominantly in the direction of reduction. The enzyme from the bacterium Escherichia coli also catalyses the activity of EC 1.1.1.399, 2-oxoglutarate reductase .
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Word Map
- 1.1.1.95
- l-serine
- aminotransferase
- microcephaly
-
psychomotor
- hydroxymethyltransferase
-
one-carbon
- hydroxypyruvate
- l-ser
-
2-hydroxyacid
- biotechnology
- molecular biology
- synthesis
The enzyme appears in viruses and cellular organisms
Synonyms
phgdh, phosphoglycerate dehydrogenase, 3-phosphoglycerate dehydrogenase, d-3-phosphoglycerate dehydrogenase, 3-pgdh, 3pgdh, pgdh3, pgdh1, ehpgdh, d-phosphoglycerate dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-PGDH
3-phosphoglycerate dehydrogenase
3-phosphoglyceric acid dehydrogenase
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3PGDH
A10
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alpha-phosphoglycerate dehydrogenase
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D-3-PG dehydrogenase
D-3-phosphoglycerate dehydrogenase
D-3-phosphoglycerate:NAD oxidoreductase
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D-phosphoglycerate dehydrogenase
dehydrogenase, phosphoglycerate
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EDA9
EhPGDH
glycerate 3-phosphate dehydrogenase
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glycerate-1,3-phosphate dehydrogenase
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NAD-dependent D-3-phosphoglycerate dehydrogenase
PGDH
PGDH1
PGDH2
PGDH3
PGK
Phgdh
phosphoglycerate kinase
phosphoglycerate oxidoreductase
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phosphoglyceric acid dehydrogenase
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Rv2996c
serA
type 1 D-3-phosphoglycerate dehydrogenase
additional information
the enzyme belongs to the D-isomer-specific 2-hydroxyacid dehydrogenase family
3-PGDH
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3-phosphoglycerate dehydrogenase
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D-3-phosphoglycerate dehydrogenase
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PGDH
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-phospho-D-glycerate + NAD+ = 3-phosphooxypyruvate + NADH + H+
member of the 2-hydroxyacid dehydrogenases family, whereof only the enzymes from E. coli and Pisum sativum utilize phosphorylated substrates and transfer the hydride ion to the A-site of NAD+, uses also alpha-ketoglutarate as substrate
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3-phospho-D-glycerate + NAD+ = 3-phosphooxypyruvate + NADH + H+
regulation model with effector L-serine, member of the D-2-hydroxyacid dehydrogenases, D-isomer substrate specific, overview of related enzymes from other species
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3-phospho-D-glycerate + NAD+ = 3-phosphooxypyruvate + NADH + H+
model for catalytic mechanism
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3-phospho-D-glycerate + NAD+ = 3-phosphooxypyruvate + NADH + H+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
3-phospho-D-glycerate:NAD+ 2-oxidoreductase
This enzyme catalyses the first committed and rate-limiting step in the phosphoserine pathway of serine biosynthesis. The reaction occurs predominantly in the direction of reduction. The enzyme from the bacterium Escherichia coli also catalyses the activity of EC 1.1.1.399, 2-oxoglutarate reductase [6].
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CAS REGISTRY NUMBER
COMMENTARY
9075-29-0
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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+
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activity relative to 3-phospho-D-glycerate: 47%
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?
3-phosphohydroxypyruvate + NADH
3-phosphoglycerate + NAD+
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specific for
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?
3-phosphooxypyruvate + pyridinealdehyde adenine dinucleotide
3-phospho-D-glycerate + ?
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r
3-phosphooxypyruvate + thionicotinamide
3-phospho-D-glycerate + ?
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r
DL-glyceraldehyde 3-phosphate + NAD+
?
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activity relative to 3-phospho-D-glycerate: 9%
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?
2-oxoglutarate + NADH + H+
D-2-hydroxyglutarate + NAD+
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?
2-oxoglutarate + NADH + H+
D-2-hydroxyglutarate + NAD+
wild-type enzyme shows no activity. Mutant enzymes R72A and R72L utilize 2-oxoglutarate as substrate
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?
2-oxoglutarate + NADH + H+
D-2-hydroxyglutarate + NAD+
wild-type enzyme shows no activity. Mutant enzymes R72A and R72L utilize 2-oxoglutarate as substrate
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?
3-phospho-D-glycerate + NAD+
3-phosphohydroxypyruvate + NADH
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-
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?
3-phospho-D-glycerate + NAD+
3-phosphohydroxypyruvate + NADH
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first step in biosynthesis of L-serine, pathway regulation, overview
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?
3-phospho-D-glycerate + NAD+
3-phosphohydroxypyruvate + NADH
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?
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
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?
3-phospho-D-glycerate + NAD+
3-phosphohydroxypyruvate + NADH
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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
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?
3-phospho-D-glycerate + NAD+
3-phosphohydroxypyruvate + NADH
first step in biosynthesis of L-serine, Vmax regulation through domain and subunit changes, overview
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?
3-phospho-D-glycerate + NAD+
3-phosphohydroxypyruvate + NADH
D-isomer-specific
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?
3-phospho-D-glycerate + NAD+
3-phosphohydroxypyruvate + NADH
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D-isomer-specific
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?
3-phospho-D-glycerate + NAD+
3-phosphohydroxypyruvate + NADH + H+
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r
3-phospho-D-glycerate + NAD+
3-phosphohydroxypyruvate + NADH + H+
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?
3-phospho-D-glycerate + NAD+
3-phosphohydroxypyruvate + NADH + H+
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highest activity
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r
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
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?
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
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?
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
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?
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
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?
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
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?
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
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?
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
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?
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
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?
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
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?
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
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?
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
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?
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
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?
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
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?
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
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?
3-phospho-D-glycerate + NAD+
3-phosphonooxypyruvate + NADH + H+
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?
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
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r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
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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
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r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
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r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
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r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
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r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
enzyme in the L-serine biosynthetic pathway
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?
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
first step of L-serine biosynthesis
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r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
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r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
first step of L-serine biosynthesis
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r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
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r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
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r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
the enzyme has a 400fold higher affinity for NADH than NAD+
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r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
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r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
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-
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r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
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r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
enzyme in the L-serine biosynthetic pathway
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?
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
first step of L-serine biosynthesis
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r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
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r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
enzyme in the L-serine biosynthetic pathway
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?
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
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r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
first step of L-serine biosynthesis
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r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
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-
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r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
-
-
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r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
-
-
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r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
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-
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r
3-phospho-D-glycerate + NAD+
3-phosphooxypyruvate + NADH + H+
enzyme in the L-serine biosynthetic pathway
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?
3-phospho-D-glycerate + NADP+
3-phosphohydroxypyruvate + NADPH + H+
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?
3-phospho-D-glycerate + NADP+
3-phosphohydroxypyruvate + NADPH + H+
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r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
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r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
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first enzyme in metabolic sequence of synthesis of serine from 3-phosphoglycerate
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r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
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r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
-
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r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
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reduction of hydroxypyruvate-phosphate is faster than oxidation of phosphoglycerate
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r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
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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
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r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
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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
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r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
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first enzyme in metabolic sequence of synthesis of serine from 3-phosphoglycerate
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r
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
first enzyme in metabolic sequence of synthesis of serine from 3-phosphoglycerate
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?
3-phosphoglycerate + NAD+
3-phosphohydroxypyruvate + NADH
-
first enzyme in metabolic sequence of synthesis of serine from 3-phosphoglycerate
287540
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