For bovine serum amine oxidase, two different mechanisms of substrate-induced inactivation have been proposed. One consists of a slow oxidation by H2O2of a conserved residue in the reduced enzyme after the fast turnover phase [Pietr-angeli, P., Nocera, S., Fattibene, P., Wang, ., Mondovı`, B. &Morpurgo, L. (2000)Biochem. Biophys. Res. Commun. 267, 174–178] and the other of the oxidation byH2O2of the dihydrobenzoxazole in equilibrium with the product Schiff base, during the catalytic cycle [Lee, Y., Shepard, E., Smith, J., Dooley, . & Sayre, . (2001)Biochemistry40, 822–829]. .
