Serine 2-dehydrogenase

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serine 2-dehydrogenase
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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PMC articles
PubMed articles
NCBI proteins

In enzymology, serine 2-dehydrogenase (EC 1.4.1.7) is an enzyme that catalyzes the chemical reaction

+ NAD+
 
 
H2O
H+
Serine 2-dehydrogenase
H2O
H+
 
+ NADH + NH3
 

The three substrates of this enzyme are serine, water, and oxidised nicotinamide adenine dinucleotide (NAD+). Its products are hydroxypyruvic acid, reduced NADH, ammonia, and a proton. [1] [2]

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

  1. Enzyme 1.4.1.7 at KEGG Pathway Database.
  2. Kretovich VL, Stepanovich KM (1966). "[The enzyme catalyzing the reductive amination of oxypyruvate]". Izv. Akad. Nauk. SSSR. Biol. 2: 295–300. PMID   5972761.