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
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1.1.1.95
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l-serine
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aminotransferase
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microcephaly
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psychomotor
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hydroxymethyltransferase
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one-carbon
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hydroxypyruvate
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l-ser
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2-hydroxyacid
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synthesis
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molecular biology
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biotechnology
- 1.1.1.95
- l-serine
- aminotransferase
- microcephaly
-
psychomotor
- hydroxymethyltransferase
-
one-carbon
- hydroxypyruvate
- l-ser
-
2-hydroxyacid
- synthesis
- molecular biology
- biotechnology
Reaction
Synonyms
3-PGDH, 3-phosphoglycerate dehydrogenase, 3-phosphoglyceric acid dehydrogenase, 3PGDH, A10, alpha-phosphoglycerate dehydrogenase, ApPGDH, 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, More, NAD-dependent D-3-phosphoglycerate dehydrogenase, PGDH, PGDH1, PGDH2, PGDH3, PGK, Phgdh, phosphoglycerate dehydrogenase, phosphoglycerate kinase, phosphoglycerate oxidoreductase, phosphoglyceric acid dehydrogenase, serA, type 1 D-3-phosphoglycerate dehydrogenase, type III 3-phosphoglycerate dehydrogenase, type IIIK PGDH
ECTree
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General Information
General Information on EC 1.1.1.95 - phosphoglycerate dehydrogenase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
malfunction
metabolism
physiological function
malfunction
3-PGDH deficiency is a rare recessive inborn error in the biosynthesis of the amino acid L-serine characterized clinically by congenital microcephaly, psychomotor retardation, and intractable seizures. The biochemical abnormalities associated with this disorder are low concentrations of L-serine, D-serine, and glycine in cerebrospinal fluid
malfunction
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mutations in the human PHGDH cause serine deficiency disorders characterized by severe neurological symptoms including congenital microcephaly and psychomotor retardation, growth retardation phenotypes seen in human patients suffering from SDD caused by PHGDH mutations, overview
malfunction
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Phgdh null mice have markedly decreased free serine content in their tissues, which is associated with overall growth retardation, striking brain malformation, and embryonic lethality
malfunction
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targeted disruption of Phgdh in mice causes overall growth retardation with severe brain microcephaly and leads to embryonic lethality
malfunction
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enzyme-depleted astrocytes accumulate 20fold less L-serine compared with controls
malfunction
lacking of isoform EDA9 expression causes drastic developmental defects
malfunction
PGDH1-silenced lines are inhibited in growth
metabolism
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3-phosphoglycerate dehydrogenase catalyzes the first step of the phosphorylated pathway in the de novo synthesis of L-serine. Availability of L-serine within neural stem/progenitor cells may be a critical factor for neurogenesis in developing and adult brain
metabolism
the enzyme is required for the de novo biosynthesis of L-serine
metabolism
the enzyme is required for the de novo biosynthesis of L-serine
metabolism
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the enzyme catalyzes the first committed step of L-serine biosynthesis
physiological function
3-PGDH deficiency is a rare recessive inborn error in the biosynthesis of the amino acid L-serine characterized clinically by congenital microcephaly, psychomotor retardation, and intractable seizures. The biochemical abnormalities associated with this disorder are low concentrations of L-serine, D-serine, and glycine in cerebrospinal fluid
physiological function
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mutations in the human PHGDH cause serine deficiency disorders characterized by severe neurological symptoms including congenital microcephaly and psychomotor retardation
physiological function
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Phgdh knockout mouse embryos demonstrate that free serine and glycine concentrations are decreased markedly in head samples
physiological function
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Phgdh null mice have markedly decreased free serine content in their tissues, which is associated with overall growth retardation, striking brain malformation, and embryonic lethality
physiological function
phosphoglycerate dehydrogenase isoform EDA9 is the essential gene for embryo and male gametophyte development in Arabidopsis thaliana
physiological function
the gene EDA9 plays a crucial role in embryo and pollen development
