Alcohol Oxidase from Pichea pastoris, 5ku

Alcohol oxidase has been detected in several strains of yeast, such as Candida, Pichia, and Hansenula, that utilize methanol as a sole carbon and energy source. Some of these enzymes have been isolated and partially characterized. Alcohol oxidase plays a major role in the metabolism of methanol resulting in the formation of formaldehyde. Primarily localized in the peroxisome, alcohol oxidase has also been found in the cytoplasm. Monomers are synthesized in the cytosol and assembled into octomers in the peroxisome. Octomerization is thought to be chaperone mediated. Alcohol oxidase is of interest for the study of protein translocation into peroxisomes. It catalyzes the oxidation of an alcohol to an aldehyde and hydrogen peroxide. Alcohol oxidase is used for qualitative and quantitative determination of methanol or ethanol (blood alcohol) by colorimetric procedures. Unlike present ADH based assays for ethanol in biological specimens, no labile cofactors or trapping agents are required and considerably less enzyme is used per assay. Quantitative determination of alcohol using an oxygen electrode (enzyme electrode) is also possible. With or without catalase, alcohol oxidase can be used to remove alcohol or scavenge oxygen. Using dilute methanol, sensitive samples can be sterilized through release of the products formaldehyde and hydrogen peroxide. The enzyme can also be used to generate H2O2 in radio-iodine labelling procedures. Alcohol oxidase catalyzes the oxidation of short-chain, primary, aliphatic alcohols to their respective aldehydes. It has the highest affinity for methanol. Alcohol oxidase is involved in the metabolism of methanol, which is important for yeasts that utilize methanol as their sole energy source. Alcohol oxidase is primarily found in the peroxisome but may be present in the cytoplasm as well.

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