Glucuronolactone reductase
| glucuronolactone reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.20 | ||||||||
| CAS no. | 9028-30-2 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a glucuronolactone reductase (EC 1.1.1.20) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are L-gulono-1,4-lactone and oxidised nicotinamide adenine dinucleotide phosphate (NADP+). Its products are [-glucurono-3,6-lactone, reduced NADPH, 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 L-gulono-1,4-lactone:NADP+ 1-oxidoreductase. Other names in common use include GRase, and gulonolactone dehydrogenase. This enzyme participates in ascorbate and aldarate metabolism.
References
- ^ Enzyme 1.1.1.20 at KEGG Pathway Database.
- ^ Suzuki K, Mano Y, Shimazono N (1960). "Conversion of L-gulonolactone to L-ascorbic acid; properties of the microsomal enzyme in rat liver". J. Biochem. 48 (2): 313–315. doi:10.1093/oxfordjournals.jbchem.a127175. ISSN 0021-924X.