Opine dehydrogenase
| opine dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.5.1.28 | ||||||||
| CAS no. | 108281-02-3 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, an opine dehydrogenase (EC 1.5.1.28) is an enzyme that catalyzes the chemical reaction
- (2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate + NAD+ + H2O L-2-aminopentanoic acid + pyruvate + NADH + H+
The 3 substrates of this enzyme are [[(2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate]], NAD+, and H2O, whereas its 4 products are L-2-aminopentanoic acid, pyruvate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate:NAD+ oxidoreductase (L-aminopentanoate-forming). Other names in common use include (2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate dehydrogenase (NAD+,, and L-aminopentanoate-forming).
References
[edit]- Asano Y, Yamaguchi K, Kondo K (1989). "A new NAD+-dependent opine dehydrogenase from Arthrobacter sp strain 1C". J. Bacteriol. 171 (8): 4466–71. PMC 210226. PMID 2753861.
- Dairi T, Asano Y (1995). "Cloning, nucleotide sequencing, and expression of an opine dehydrogenase gene from Arthrobacter sp. strain 1C". Appl. Environ. Microbiol. 61 (8): 3169–71. PMC 167592. PMID 7487048.
- Kato Y, Yamada H, Asano Y (1996). "Stereoselective synthesis of opine-type secondary amine carboxylic acids by a new enzyme opine dehydrogenase. Use of recombinant enzymes". J. Mol. Catal., B Enzym. 1 (3–6): 151–160. doi:10.1016/1381-1177(95)00011-9.
