Two isoenzymes of aldehyde oxidase (E.C. 1.2.3.1) can be separated from potato tubers (Solanum tuberosum) by polyacrylamide gel electrophoresis. The pH optima of these two isoenzymes were pH 7.5. Both enzymes can oxidize different aldehydes, e.g. crotonaldehyde, Propionaldehyde, acetaldehyde, formaldehyde, glyoxal and benzyl-aldehyde. The isoenzymes could not use xanthine as a substrate. Formaldehyde was oxidized only in the presence of phosphate ions. A substrate dependent inhibition of the enzyme activity is possible through chloral hydrate. PMS, FMN, riboflavine, cytochrome c and O2 serve as electron acceptors.
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Gunter M. Rothe (1974) studied this question.