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+

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.


Allikas: http://en.wikipedia.org/wiki/Serine_2-dehydrogenase
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