The Enzyme Database

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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
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.
[EC created 1999]

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