Tagaturonate reductase
| tagaturonate reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.58 | ||||||||
| CAS no. | 9028-45-9 | ||||||||
| 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 | ||||||||
| |||||||||
Tagaturonate reductase (EC 1.1.1.58) is an enzyme that catalyzes the chemical reaction
Thhe two substrates of this enzyme are D-altronic acid and oxidised nicotinamide adenine dinucleotide (NAD+). Its products are D-tagaturonic acid, reduced NADH, and a proton.[1][2]
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is D-altronate:NAD+ 3-oxidoreductase. Other names in common use include altronic oxidoreductase, altronate oxidoreductase, TagUAR, altronate dehydrogenase, and D-tagaturonate reductase. This enzyme participates in pentose and glucuronate interconversions.
References
- ^ Enzyme 1.1.1.58 at KEGG Pathway Database.
- ^ Hickman J, Ashwell G (1960). "Uronic acid metabolism in bacteria. II. Purification and properties of D-altronic acid and D-mannonic acid dehyrogenases in Escherichia coli". J. Biol. Chem. 235 (6): 1566–1570. doi:10.1016/S0021-9258(19)76841-0. PMID 14401695.