Biology:Alanopine dehydrogenase
| alanopine dehydrogenase | |||||||||
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| Identifiers | |||||||||
| EC number | 1.5.1.17 | ||||||||
| CAS number | 71343-07-2 | ||||||||
| 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 | ||||||||
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Alanopine dehydrogenase (EC 1.5.1.17) is an enzyme that catalyzes the chemical reaction
- REDIRECT Template:Chemical reaction
The three substrates of this enzyme are alanopine, oxidised nicotinamide adenine dinucleotide (NAD+) and water. Its products are L-alanine, reduced NADH, pyruvic acid, and a proton.[1][2][3][4]
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 2,2'-iminodipropanoate:NAD+ oxidoreductase (L-alanine-forming). Other names in common use include ALPDH, alanopine[meso-N-(1-carboxyethyl)-alanine]dehydrogenase, meso-N-(1-carboxyethyl)-alanine:NAD+ oxidoreductase, alanopine: NAD+ oxidoreductase, ADH, and alanopine:NAD+ oxidoreductase.
References
- ↑ Enzyme 1.5.1.17 at KEGG Pathway Database.
- ↑ Dando PR (1981). "Strombine [N-(carboxymethyl)-D-alanine] dehydrogenase and alanopine [meso-N-(1-carboxyethyl)-alanine]dehydrogenase from the mussel Mytilus edulis L". Biochem. Soc. Trans. 9 (4): 297–298. doi:10.1042/bst0090297.
- ↑ "Alanopine and strombine are novel imino acids produced by a dehydrogenase found in the adductor muscle of the oyster, Crassostrea gigas". Arch. Biochem. Biophys. 201 (1): 110–4. 1980. doi:10.1016/0003-9861(80)90493-2. PMID 6156653.
- ↑ "Purification and properties of alanopine dehydrogenase from the adductor muscle of the oyster, Crassostrea gigas (Mollusca, Bivalvia)". Eur. J. Biochem. 114 (3): 615–21. 1981. doi:10.1111/j.1432-1033.1981.tb05188.x. PMID 7238503.
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