✦ LIBER ✦

Oxidation of kynuramine by lentil seedling copper amine oxidase: demonstration of a single turnover mechanism in the apoenzyme

✍ Scribed by Alessandra Padiglia; Rosaria Medda; Anita Lorrai; Donatella Congiu; Jens Z. Pedersen; Giovanni Floris

Publisher: John Wiley and Sons
Year: 1998
Tongue: English
Weight: 85 KB
Volume: 9
Category: Article
ISSN: 0958-0344
DOI: 10.1002/(sici)1099-1565(199809/10)9:5<223::aid-pca414>3.0.co;2-y

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✦ Synopsis

Copper amine oxidase was shown to be able to oxidize kynuramine to the corresponding aldehyde, which spontaneously rearranged to 4-hydroxyquinoline. Under anaerobic conditions, the native enzyme oxidized one equivalent of kynuramine and released one equivalent of aldehyde per enzyme subunit. The apoenzyme gave exactly the same 1:1:1 stoichiometry under anaerobic as well as aerobic conditions. These findings demonstrate unequivocally that copper-free amine oxidase can oxidize substrates with a single incomplete turnover.