| glyoxylate reductase (NADP) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.79 | ||||||||
| CAS no. | 37250-17-2 | ||||||||
| 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 glyoxylate reductase (NADP+) ( EC 1.1.1.79) is an enzyme that catalyzes the chemical reaction
- glycolate + NADP+ glyoxylate + NADPH + H+
Thus, the two substrates of this enzyme are glycolate and NADP+, whereas its 3 products are glyoxylate, NADPH, and H+.
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 glycolate:NADP+ oxidoreductase. Other names in common use include NADPH-glyoxylate reductase, and glyoxylate reductase (NADP+). This enzyme participates in pyruvate metabolism and glyoxylate and dicarboxylate metabolism.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2GCG, 2H1S, and 2Q50.
References
- Cartwright LN; Hullin RP (1966). "Purification and properties of two glyoxylate reductases from a species of Pseudomonas". Biochem. J. 101 (3): 781–791. doi: 10.1042/bj1010781. PMC 1270187. PMID 16742459.
- Kleczkowski LA, Randall DD, Blevins DG (1986). "Purification and characterization of a novel NADPH(NADH)-dependent glyoxylate reductase from spinach leaves. Comparison of immunological properties of leaf glyoxylate reductase and hydroxypyruvate reductase". Biochem. J. 239 (3): 653–9. doi: 10.1042/bj2390653. PMC 1147336. PMID 3548703.
