Serine 2-dehydrogenase
In enzymology, a serine 2-dehydrogenase (EC 1.4.1.7) is an enzyme that catalyzes the chemical reaction
- L-serine + H2O + NAD+ 3-hydroxypyruvate + NH3 + NADH + H+
serine 2-dehydrogenase | |||||||||
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Identifiers | |||||||||
EC no. | 1.4.1.7 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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The 3 substrates of this enzyme are L-serine, H2O, and NAD+, whereas its 4 products are 3-hydroxypyruvate, NH3, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-serine:NAD+ 2-oxidoreductase (deaminating). Other names in common use include L-serine:NAD+ oxidoreductase (deaminating), and serine dehydrogenase.
References
- Kretovich VL, Stepanovich KM (1966). "[The enzyme catalyzing the reductive amination of oxypyruvate]". Izv. Akad. Nauk. SSSR. Biol. 2: 295–300. PMID 5972761.
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