Biology:Fructuronate reductase
| fructuronate reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.1.1.57 | ||||||||
| CAS number | 9028-44-8 | ||||||||
| 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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In enzymology, fructuronate reductase (EC 1.1.1.57) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are D-mannonic acid and oxidised nicotinamide adenine dinucleotide (NAD+). Its products are D-fructuronic acid (shown in its keto form), reduced NADH, and a proton.[1][2][3]
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-mannonate:NAD+ 5-oxidoreductase. Other names in common use include mannonate oxidoreductase, mannonic dehydrogenase, D-mannonate dehydrogenase, and D-mannonate:NAD+ oxidoreductase. This enzyme participates in pentose and glucuronate interconversions.
References
- ↑ Enzyme 1.1.1.57 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.
- ↑ "Catabolism of galacturonic and glucuronic acids by Erwinia carotovora". J. Biol. Chem. 234 (9): 2227–35. 1959. doi:10.1016/S0021-9258(18)69789-3. PMID 14409051.
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