Biology:Serine 2-dehydrogenase
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Short description: Enzyme
| serine 2-dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 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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In enzymology, a serine 2-dehydrogenase (EC 1.4.1.7) is an enzyme that catalyzes the chemical reaction
- L-serine + H2O + NAD+ [math]\displaystyle{ \rightleftharpoons }[/math] 3-hydroxypyruvate + NH3 + NADH + H+
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
- "[The enzyme catalyzing the reductive amination of oxypyruvate]". Izv. Akad. Nauk. SSSR. Biol. 2: 295–300. 1966. PMID 5972761.
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