The reaction pathway of membrane-bound rat liver mitochondrial monoamine oxidase |
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Authors: | Miles D. Houslay and Keith F. Tipton |
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Affiliation: | Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1QW, U.K. |
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Abstract: | 1. A preparation of a partly purified mitochondrial outer-membrane fraction suitable for kinetic investigations of monoamine oxidase is described. 2. An apparatus suitable for varying the O(2) concentration in a spectrophotometer cuvette is described. 3. The reaction catalysed by the membrane-bound enzyme is shown to proceed by a double-displacement (Ping Pong) mechanism, and a formal mechanism is proposed. 4. KCN, NaN(3), benzyl cyanide and 4-cyanophenol are shown to be reversible inhibitors of the enzyme. 5. The non-linear reciprocal plot obtained with impure preparations of benzylamine, which is typical of high substrate inhibition, is shown to be due to aldehyde contamination of the substrate. |
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