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Oxidation of kynuramine by lentil seedling copper amine oxidase: demonstration of a single turnover mechanism in the apoenzyme
Author(s) -
Padiglia Alessandra,
Medda Rosaria,
Lorrai Anita,
Congiu Donatella,
Pedersen Jens Z.,
Floris Giovanni
Publication year - 1998
Publication title -
phytochemical analysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.574
H-Index - 72
eISSN - 1099-1565
pISSN - 0958-0344
DOI - 10.1002/(sici)1099-1565(199809/10)9:5<223::aid-pca414>3.0.co;2-y
Subject(s) - chemistry , amine oxidase , copper , aldehyde , amine gas treating , enzyme , stoichiometry , oxidase test , turnover number , anaerobic exercise , organic chemistry , stereochemistry , catalysis , physiology , biology
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. © 1998 John Wiley & Sons, Ltd.