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Description
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. Monomers are synthesized in the cytosol and assembled into octomers in the peroxisome. Octomerization is thought to be chaparone 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.
- Catalyzes the oxidation of short-chain, primary, aliphatic alcohols to their respective aldehydes (it has the highest affinity for methanol)
- Involved in the metabolism of methanol, which is important for yeasts that utilize methanol as their sole energy source
- Primarily found in the peroxisome, but may be present in the cytoplasm as well
- One unit will oxidize 1.0 μmole of methanol to formaldehyde per minute at pH 7.5 at 25°C
Specifications
Specifications
| Quantity | 250 U |
| Formula Weight | about 630,000g/mol |
| Physical Form | Frozen Liquid |
Safety and Handling
| Recommended Storage | Freeze at –20°C |
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