Biology:(S)-2-hydroxy-acid oxidase
| (S)-2-hydroxy-acid oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Glycolate oxidase tetramer, Human | |||||||||
| Identifiers | |||||||||
| EC number | 1.1.3.15 | ||||||||
| CAS number | 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 [math]\displaystyle{ \rightleftharpoons }[/math] 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
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
- "l-Hydroxy acid oxidase". J. Biol. Chem. 163 (1): 137–144. 1946. doi:10.1016/S0021-9258(17)41353-6. PMID 21023634. http://www.jbc.org/content/163/1/137.full.pdf.
- "Preparation and some properties of crystalline glycolic acid oxidase of spinach". J. Biol. Chem. 231 (1): 135–57. 1958. doi:10.1016/S0021-9258(19)77292-5. PMID 13538955.
- "The oxidation of glycolic acid by a liver enzyme". J. Biol. Chem. 210 (1): 269–80. 1954. doi:10.1016/S0021-9258(18)65451-1. PMID 13201588.
- "Crystalline mammalian L-amino acid oxidase from rat kidney mitochondria". J. Biol. Chem. 241 (9): 2075–83. 1966. doi:10.1016/S0021-9258(18)96668-8. PMID 5946631.
- "Aliphatic L-alpha-hydroxyacid oxidase from rat livers: purification and properties". Biochim. Biophys. Acta 167 (1): 9–22. 1968. doi:10.1016/0005-2744(68)90273-8. PMID 5686300.
- "Purification and characterization of glycolic acid oxidase from pig liver". Biochim. Biophys. Acta 227 (3): 500–20. 1971. doi:10.1016/0005-2744(71)90003-9. PMID 5569122. https://deepblue.lib.umich.edu/bitstream/2027.42/33685/1/0000197.pdf.
- "The self-association of L-alpha hydroxyacid oxidase". Biochim. Biophys. Acta 427 (2): 679–87. 1976. doi:10.1016/0005-2795(76)90211-7. PMID 1268224.
- "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. 2021. doi:10.1371/journal.pcbi.1009446. PMID 34555022.
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