| L-amino-acid dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.4.1.5 | ||||||||
| CAS no. | 9029-13-4 | ||||||||
| 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 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
a 2-oxo acid + NH3 + NADH + HThe 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).
References
- Nisman B, Mager J (February 1952). "Diphosphopyridine nucleotide and phosphate requirement for oxidation of amino-acids by cell-free extracts of obligate anaerobes". Nature. 169 (4293): 243–4. doi:10.1038/169243a0. PMID 14910739.
| CH-NH2 oxidoreductases (EC 1.4) - primarily amino acid oxidoreductases | |
|---|---|
| 1.4.1: NAD/NADP acceptor | |
| 1.4.3: oxygen acceptor | |
| 1.4.4: disulfide acceptor | |
| 1.4.99: other acceptors | |
| Enzymes | |
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| Activity | |
| Regulation | |
| Classification | |
| Kinetics | |
| Types |
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