Enzyme Structure
The enzyme is a octamer of ~46kD subunits (except in C. tropicalis, in which it is a dimer of subunits ~70kD). It is a Cytochrome c oxidase containing a covalently-bound heme group using the Cys-X-X-Cys-His motif. It also contains flavin to assist in oxidation-reduction. The enzyme is bound to the endoplasmic reticulum membrane.
Long-chain fatty alcohol oxidases vary between species in their specificity; some species have multiple different alcohol oxidases. They generally have a broad range of substrates, ranging from short chain alcohols starting at 4 carbons to the longest long-chain alcohols at 22 carbons. Some can also oxidize select diols, secondary alcohols, hydroxy fatty acids, and even long-chain aldehydes. However, each enzyme is optimized to function for specific alcohol, often between 10 and 16 carbons. In at least one species, the enzyme was stereoselective for the R(-) entantiomer.
Read more about this topic: Long-chain-alcohol Oxidase
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