Alanopine dehydrogenase
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Alanopine dehydrogenase (EC 1.5.1.17) is an enzyme that catalyzes the chemical reaction
| alanopine dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.5.1.17 | ||||||||
| CAS no. | 71343-07-2 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
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.
