Serine 2-dehydrogenase

serine 2-dehydrogenase
Identifiers
EC no.1.4.1.7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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

+ NAD+
 
 
H2O
H+
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.