This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of the donor with oxygen as the acceptor. It employs one cofactor, FAD.
Alcohol oxidases catalyzes the oxidation of primary alcohols to their corresponding aldehydes. Unlike alcohol dehydrogenases, they are unable to catalyze the reverse reaction. This is reflected in their cofactor as well—unlike alcohol dehydrogenases, which use NAD+, alcohol oxidases use FAD.[1] SCAO is capable of oxidizing alcohols with up to 8 carbons, but their primary substrates are methanol and ethanol.
SCAO is an intracellular enzyme.[1] Its common source are fungi and yeasts, but it has also been shown to be present in mollusks.[1]
It appears as an octameric protein, except for SCAO from A. ochraceus, which has been shown to be a tetramer. Each of the subunites is 65-80 kDa. Nine SCAO isoforms have been found in Ogataea methanolica, which has been shown to be a result of different combinations of two different subunits in the octamers, each coded by a different gene.[1]
Several potential uses have been suggested for SCAO:
Biosensors with amperometric detection can be used within beverage testing, fermentation monitoring, methanol and ethanol detection, body fluid screening, and toxicological and phorensic laboratories[1]
Chemical synthesis of various aldehydes including aroma and flavor chemicals, where it could appear as a cheaper and more eco-friendly alternative to current methods[1]
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. PMID5636370.
Nishida A, Ishihara T, Hiroi T (1987). "Studies on enzymes related to lignan biodegradation". Baiomasu Henkan Keikaku Kenkyu. Hokoku: 38–59.
