Alcohol oxidase
alcohol oxidase | |||||||||
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Identifiers | |||||||||
EC number | 1.1.3.13 | ||||||||
CAS number | 9073-63-6 | ||||||||
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 / EGO | ||||||||
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In enzymology, an alcohol oxidase (EC 1.1.3.13) is an enzyme that catalyzes the chemical reaction
- a primary alcohol + O2 an aldehyde + H2O2
Thus, the two substrates of this enzyme are primary alcohol and O2, whereas its two products are aldehyde 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 alcohol:oxygen oxidoreductase. This enzyme is also called ethanol oxidase. It employs one cofactor, FAD.
Structural studies
As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes 1AHU, 1AHV, 1AHZ, 1VAO, 1W1J, 1W1K, 1W1L, 1W1M, and 2VAO.
References
- Janssen FW, Ruelius HW (1968). "Alcohol oxidase, a flavoprotein from several Basidiomycetes species Crystallization by fractional precipitation with polyethylene glycol". Biochim. Biophys. Acta 151 (2): 330–42. doi:10.1016/0005-2744(68)90100-9. PMID 5636370.
- Nishida A, Ishihara T and Hiroi T (1987). "Studies on enzymes related to lignan biodegradation". Baiomasu Henkan Keikaku Kenkyu. Hokoku: 38–59.
- Suye S (1997). "Purification and properties of alcohol oxidase from Candida methanosorbosa M-2003". Curr. Microbiol. 34 (6): 374–7. doi:10.1007/s002849900198. PMID 9142745.
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