(S)-2-hydroxy-acid oxidase
| (S)-2-hydroxy-acid oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Glycolate oxidase tetramer, Human | |||||||||
| Identifiers | |||||||||
| EC no. | 1.1.3.15 | ||||||||
| CAS no. | 9037-63-2 | ||||||||
| 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, an (S)-2-hydroxy-acid oxidase (EC 1.1.3.15) is an enzyme that catalyzes the chemical reaction
- (S)-2-hydroxy acid + O2 2-oxo acid + H2O2
Thus, the two substrates of this enzyme are (S)-2-hydroxy acid and O2, whereas its two products are 2-oxo acid and H2O2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is (S)-2-hydroxy-acid:oxygen 2-oxidoreductase. Other names in common use include glycolate oxidase, hydroxy-acid oxidase A, hydroxy-acid oxidase B, oxidase, L-2-hydroxy acid, hydroxyacid oxidase A, L-alpha-hydroxy acid oxidase, and L-2-hydroxy acid oxidase. This enzyme participates in glyoxylate and dicarboxylate metabolism. It employs one cofactor, FMN.
Structural studies
[edit]As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1AL7, 1AL8, 1GYL, 1TB3, and 2NZL.
References
[edit]- Blanchard M, Green DE, Nocito-Carroll V, Ratner S (1946). "l-Hydroxy acid oxidase" (PDF). J. Biol. Chem. 163 (1): 137–144. doi:10.1016/S0021-9258(17)41353-6. PMID 21023634.
- FRIGERIO NA, HARBURY HA (1958). "Preparation and some properties of crystalline glycolic acid oxidase of spinach". J. Biol. Chem. 231 (1): 135–57. doi:10.1016/S0021-9258(19)77292-5. PMID 13538955.
- KUN E, DECHARY JM, PITOT HC (1954). "The oxidation of glycolic acid by a liver enzyme". J. Biol. Chem. 210 (1): 269–80. doi:10.1016/S0021-9258(18)65451-1. PMID 13201588.
- Nakano M, Danowski TS (1966). "Crystalline mammalian L-amino acid oxidase from rat kidney mitochondria". J. Biol. Chem. 241 (9): 2075–83. doi:10.1016/S0021-9258(18)96668-8. PMID 5946631.
- Nakano M, Ushijima Y, Saga M, Tsutsumi Y, Asami H (1968). "Aliphatic L-alpha-hydroxyacid oxidase from rat livers: purification and properties". Biochim. Biophys. Acta. 167 (1): 9–22. doi:10.1016/0005-2744(68)90273-8. PMID 5686300.
- Schuman M, Massey V (1971). "Purification and characterization of glycolic acid oxidase from pig liver" (PDF). Biochim. Biophys. Acta. 227 (3): 500–20. doi:10.1016/0005-2744(71)90003-9. hdl:2027.42/33685. PMID 5569122.
- Phillips DR, Duley JA, Fennell DJ, Holmes RS (1976). "The self-association of L-alpha hydroxyacid oxidase". Biochim. Biophys. Acta. 427 (2): 679–87. doi:10.1016/0005-2795(76)90211-7. PMID 1268224.
- Rembeza E, Engqvist MK (2021). "Experimental and computational investigation of enzyme functional annotations uncovers misannotation in the EC 1.1.3.15 enzyme class". PLOS Comput Biol. 17 (9): e1009446. Bibcode:2021PLSCB..17E9446R. doi:10.1371/journal.pcbi.1009446. PMC 8491902. PMID 34555022.
