Asparagusate reductase
| asparagusate reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.8.1.11 | ||||||||
| CAS no. | 56126-52-4 | ||||||||
| 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 | ||||||||
| |||||||||
Asparagusate reductase (EC 1.8.1.11) is an enzyme that catalyzes the chemical reaction
- 3-mercapto-2-mercaptomethylpropanoate + NAD+ asparagusate + NADH + H+
Thus, the two substrates of this enzyme are 3-mercapto-2-mercaptomethylpropanoate and nicotinamide adenine dinucleotide ion, whereas its 3 products are asparagusate, nicotinamide adenine dinucleotide, and hydrogen ion.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 3-mercapto-2-mercaptomethylpropanoate:NAD+ oxidoreductase. Other names in common use include asparagusate dehydrogenase, asparagusic dehydrogenase, asparagusate reductase (NADH2), and NADH2:asparagusate oxidoreductase.
References
[edit]- Yanagawa H, Egami F (1975). "Asparagusate dehydrogenases and lipoyl dehydrogenase from asparagus mitochondria". Biochim. Biophys. Acta. 384 (2): 342–52. doi:10.1016/0005-2744(75)90035-2. PMID 1125255.
- Yanagawa H, Egami F (1976). "Asparagusate dehydrogenases and lipoyl dehydrogenase from asparagus mitochondria. Physical, chemical, and enzymatic properties". J. Biol. Chem. 251 (12): 3637–44. PMID 180003.
