A catalytic mechanism for the enzyme benzylamine oxidase from pig plasma
- 1 December 1972
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 130 (3), 713-728
- https://doi.org/10.1042/bj1300713
Abstract
Initial-velocity and product-inhibition studies on the enzyme benzylamine oxidase from pig plasma indicate that the order of substrate addition and product release is benzylamine on, ammonia off, oxygen on, hydrogen peroxide off, benzaldehyde off. Ammonia, but not benzaldehyde, is released under strictly anaerobic conditions which provides independent evidence for this order. Benzyl alcohol is a substrate for the enzyme. A chemical mechanism consistent with all the data is proposed.This publication has 23 references indexed in Scilit:
- Multiple Phases in the Reduction of Xanthine Oxidase by SubstratesEuropean Journal of Biochemistry, 1972
- The Resolution of Active and Inactive Xanthine Oxidase by Affinity ChromatographyJournal of Biological Chemistry, 1972
- Mechanistic studies of beef plasma amine oxidaseBiochemistry, 1970
- Determination of submicro quantities of ammoniaAnalytical Biochemistry, 1970
- Electron paramagnetic resonance spectra of amine oxidase from Aspergillus nigerBiochimica et Biophysica Acta (BBA) - Enzymology, 1969
- The nature of copper in pig plasma benzylamine oxidaseBiochemical Journal, 1968
- The inactivation of pea-seedling diamine oxidase by peroxidase and 1,5-diaminopentaneBiochemical Journal, 1967
- DIAMINE OXIDASE FROM PIG KIDNEY - IMPROVED PURIFICATION AND PROPERTIES1967
- The inhibition of caeruloplasmin by azideBiochemical Journal, 1966
- Purification of pig-kidney diamine oxidase and its identity with histaminaseBiochemical Journal, 1964