(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
Search PMC articles PubMed articles NCBI proteins

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 ${\displaystyle \rightleftharpoons }$ 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.

As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1AL7, 1AL8, 1GYL, 1TB3, and 2NZL.

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• 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.