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 | ||||||||
| |||||||||
Opine dehydrogenase (EC 1.5.1.28) is an enzyme that catalyzes several chemical reactions involving a class of molecules called opines.[1][2] An example is:
The three substrates of this enzyme are an opine such as (2S)-2-[(R)-1-carboxyethylamino]pentanoic acid (1), oxidised nicotinamide adenine dinucleotide (NAD+), and water. When acting in the forward direction, the products in this example are L-norvaline, reduced NADH, pyruvic acid and a proton.[3][4]
The enzyme can also catalyse reactions that make opines by adding a molecule of pyruvic acid or other keto acids to L-amino acids. This includes making derivatives of L-methionine, L-isoleucine, L-valine, and L-phenylalanine.[2]
References
- ^ Asano Y, Yamaguchi K, Kondo K (1989). "A new NAD+-dependent opine dehydrogenase from Arthrobacter sp strain 1C". J. Bacteriol. 171 (8): 4466–71. doi:10.1128/jb.171.8.4466-4471.1989. PMC 210226. PMID 2753861.
- ^ a b 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.
- ^ Enzyme 1.5.1.28 at KEGG Pathway Database.
- ^ 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. Bibcode:1995ApEnM..61.3169D. doi:10.1128/aem.61.8.3169-3171.1995. PMC 167592. PMID 7487048.
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