Rat liver mitochondrial monoamine oxidase. A change in the reaction mechanism on solubilization.
1. The kinetics of benzylamine oxidation by a soluble preparation of rat liver mitochondrial monoamine oxidase were investigated and were shown to conform to adouble-displacement (or Ping Pong) mechanism. 2. The pathway differs in detail from that followed by other amine oxidases, including the membrane-bound enzyme in rat liver mitochondrial outer membranes. 3. It is suggested taht the conformation of the protein in the soluble state differs from that in the membrane-bound state. 4. The full rate equations for this mechanism have been deposited as Supplementary Publication SUP 50039 (5pages) at the British Library (lending Division) (formely the National Lending Library for Science and Technology), Boston Spa, Yorks, LS237BQ, U.K.. from whom copies can be obtained on the terms indicated in Biochem. J (1975) 145,5.
D000641:Ammonia; D000818:Animals; D001547:Benzaldehydes; D001593:Benzyl Compounds; D006861:Hydrogen Peroxide; D007700:Kinetics; D008566:Membranes / Q000201:enzymology; D008930:Mitochondria, Liver / Q000201:enzymology*; D008995:Monoamine Oxidase; D010084:Oxidation-Reduction; D011487:Protein Conformation; D051381:Rats; D012995:Solubility
D001547:Benzaldehydes; D001593:Benzyl Compounds; D000641:Ammonia; D006861:Hydrogen Peroxide; D008995:Monoamine Oxidase