Biology:Glyoxylate reductase (NADP+)
| glyoxylate reductase (NADP) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.1.1.79 | ||||||||
| CAS number | 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 | ||||||||
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In enzymology, a glyoxylate reductase (NADP+) (EC 1.1.1.79) is an enzyme that catalyzes the chemical reaction
- glycolate + NADP+ [math]\displaystyle{ \rightleftharpoons }[/math] 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. PMID 16742459.
- "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. 1986. doi:10.1042/bj2390653. PMID 3548703.
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