EC - Opine dehydrogenase

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IntEnz Enzyme Nomenclature


Accepted name:
opine dehydrogenase
Other name:
(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)



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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0047129
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: 4466-4471 (1989). [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: 3169-3171 (1995). [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: 151-160 (1996).

[EC created 1999]