| beta-alanopine dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.5.1.26 | ||||||||
| CAS no. | 113573-64-1 | ||||||||
| 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 | ||||||||
| |||||||||
Beta-alanopine dehydrogenase (EC 1.5.1.26) is an enzyme that catalyzes the chemical reaction
- beta-alanopine + NAD+ + H2O beta-alanine + pyruvate + NADH + H+
The 3 substrates of this enzyme are beta-alanopine, nicotinamide adenine dinucleotide ion, and water, whereas its 4 products are beta-alanine, pyruvate, nicotinamide adenine dinucleotide, and hydrogen ion.
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 N-(D-1-carboxyethyl)-beta-alanine:NAD+ oxidoreductase (beta-alanine-forming).
References
- Sato M, Takahara M, Kanno N, Sato Y, Ellington WR (1987). "Isolation of a new opine, beta-alanopine, from the extracts of the muscle of the marine bivalve mollusc Scapharca broughtonii". Comp. Biochem. Physiol. 88B: 803–806.
This page was last edited on 26 August 2023, at 13:18