| EC |
1.5.1.28 |
| Accepted name: |
opine dehydrogenase |
| Reaction: |
(2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate + NAD+ + H2O = L-2-aminopentanoic acid + pyruvate + NADH + H+ |
| Other name(s): |
(2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate dehydrogenase (NAD+, L-aminopentanoate-forming) |
| Systematic name: |
(2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate:NAD+ oxidoreductase (L-aminopentanoate-forming) |
| Comments: |
In the forward direction, the enzyme from Arthrobacter sp. acts also on secondary amine dicarboxylates such as N-(1-carboxyethyl)methionine and N-(1-carboxyethyl)phenylalanine. Dehydrogenation forms an imine, which dissociates to the amino acid and pyruvate. In the reverse direction, the enzyme acts also on neutral amino acids as an amino donor. They include L-amino acids such as 2-aminopentanoic acid, 2-aminobutyric acid, 2-aminohexanoic acid, 3-chloroalanine, O-acetylserine, methionine, isoleucine, valine, phenylalanine, leucine and alanine. The amino acceptors include 2-oxoacids such as pyruvate, oxaloacetate, glyoxylate and 2-oxobutyrate. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 108281-02-3 |
| References: |
| 1. |
Asano, Y., Yamaguchi, K. and Kondo, K. A new NAD+-dependent opine dehydrogenase from Arthrobacter sp. strain 1C. J. Bacteriol. 171 (1989) 4466–4471. [DOI] [PMID: 2753861] |
| 2. |
Dairi, T. and Asano, Y. Cloning, nucleotide sequencing, and expression of an opine dehydrogenase gene from Arthrobacter sp. strain 1C. Appl. Environ. Microbiol. 61 (1995) 3169–3171. [PMID: 7487048] |
| 3. |
Kato, Y., Yamada, H. and Asano, Y. 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 (1996) 151–160. |
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| [EC 1.5.1.28 created 1999] |
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