L-amino-acid dehydrogenase
From Wikipedia, the free encyclopedia
In enzymology, a L-amino-acid dehydrogenase (EC 1.4.1.5) is an enzyme that catalyzes the chemical reaction
- an L-amino acid + H2O + NAD+ a 2-oxo acid + NH3 + NADH + H+
The 3 substrates of this enzyme are L-amino acid, H2O, and NAD+, whereas its 4 products are 2-oxo acid, NH3, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-amino-acid:NAD+ oxidoreductase (deaminating).
[edit] References
- IUBMB entry for 1.4.1.5
- BRENDA references for 1.4.1.5 (Recommended.)
- PubMed references for 1.4.1.5
- PubMed Central references for 1.4.1.5
- Google Scholar references for 1.4.1.5
- Nisman B and Mager J (Lond.). "Diphosphopyridine nucleotide and phosphate requirement for oxidation of amino-acids by cell-free extracts of obligate anaerobes". N Nature: 243–244.
[edit] External links
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- The CAS registry number for this enzyme class is 9029-13-4.