Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1973 Mar;131(3):459–469. doi: 10.1042/bj1310459

Kinetics of the diamine oxidase reaction

William G Bardsley 1, M James C Crabbe 2, Julian S Shindler 2
PMCID: PMC1177494  PMID: 4198360

Abstract

1. The oxidation of p-dimethylaminomethylbenzylamine was followed spectrophotometrically by measuring the change in E250 caused by the p-dimethylaminomethylbenzaldehyde produced under a wide variety of experimental conditions. 2. The effect of variations in concentrations of both substrates (amine and oxygen) and all products (aminoaldehyde, hydrogen peroxide and ammonia) on this reaction was studied and the results used to develop a formal mechanism. 3. The nature of the rate-limiting step was elucidated by studying the effects of alterations in ionic strength, dielectric constant and deuterium substitution on the velocity of the forward reaction. 4. Thermodynamic activation energy parameters were obtained at several pH values from the effects of temperature on the reaction.

Full text

PDF
459

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Agro A. F., Rotilio G., Costa M. T., Mondovi B. Evidence for a ping-pong mechanism in the diamine oxidase reaction. FEBS Lett. 1969 Jul;4(1):31–32. doi: 10.1016/0014-5793(69)80188-2. [DOI] [PubMed] [Google Scholar]
  2. BELLEAU B., MORAN J. Deuterium isotope effects in relation to the chemical mechanism of monoamine oxidase. Ann N Y Acad Sci. 1963 Jul 8;107:822–839. doi: 10.1111/j.1749-6632.1963.tb13326.x. [DOI] [PubMed] [Google Scholar]
  3. Bardsley W. G., Ashford J. S., Hill C. M. Synthesis and oxidation of aminoalkyl-onium compounds by pig kidney diamine oxidase. Biochem J. 1971 May;122(4):557–567. doi: 10.1042/bj1220557. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bardsley W. G., Ashford J. S. Inhibition of pig kidney diamine oxidase by substrate analogues. Biochem J. 1972 Jun;128(2):253–263. doi: 10.1042/bj1280253. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Bardsley W. G., Crabbe M. J., Shindler J. S., Ashford J. S. Oxidation of p-dimethylaminomethylbenzylamine by pig kidney diamine oxidase. A new method for spectrophotometric assay. Biochem J. 1972 May;127(5):875–879. doi: 10.1042/bj1270875. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Bardsley W. G., Hill C. M., Lobley R. W. A reinvestigation of the substrate specificity of pig kidney diamine oxidase. Biochem J. 1970 Mar;117(1):169–176. doi: 10.1042/bj1170169. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. CLELAND W. W. The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations. Biochim Biophys Acta. 1963 Jan 8;67:104–137. doi: 10.1016/0006-3002(63)91800-6. [DOI] [PubMed] [Google Scholar]
  8. CLELAND W. W. The kinetics of enzyme-catalyzed reactions with two or more substrates or products. II. Inhibition: nomenclature and theory. Biochim Biophys Acta. 1963 Feb 12;67:173–187. doi: 10.1016/0006-3002(63)91815-8. [DOI] [PubMed] [Google Scholar]
  9. CLELAND W. W. The kinetics of enzyme-catalyzed reactions with two or more substrates or products. III. Prediction of initial velocity and inhibition patterns by inspection. Biochim Biophys Acta. 1963 Feb 12;67:188–196. doi: 10.1016/0006-3002(63)91816-x. [DOI] [PubMed] [Google Scholar]
  10. Hopper D. J., Chapman P. J., Dagley S. The enzymic degradation of alkyl-substituted gentisates, maleates and malates. Biochem J. 1971 Mar;122(1):29–40. doi: 10.1042/bj1220029. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Kumagai H., Nagate T., Yamada H., Fukami H. Characterization of sodium borohydride-reduced histaminase-histamine intermediate. Biochim Biophys Acta. 1969 Jul 8;185(1):242–244. doi: 10.1016/0005-2744(69)90299-x. [DOI] [PubMed] [Google Scholar]
  12. Mondovi B., Rotilio G., Agro A. F., Vallogini M. P., Malmström B. G., Antonini E. Copper reduction by substrate in diamine oxidase. FEBS Lett. 1969 Jan;2(3):182–184. doi: 10.1016/0014-5793(69)80013-x. [DOI] [PubMed] [Google Scholar]
  13. Mondovì B., Costa M. T., Agrò A. F., Rotilio G. Pyridoxal phosphate as a prosthetic group of pig kidney diamine oxidase. Arch Biochem Biophys. 1967 Mar;119(1):373–381. doi: 10.1016/0003-9861(67)90468-7. [DOI] [PubMed] [Google Scholar]
  14. Mondovì B., Rotilio G., Costa M. T., Finazzi-Agrò A., Chiancone E., Hansen R. E., Beinert H. Diamine oxidase from pig kidney. Improved purification and properties. J Biol Chem. 1967 Mar 25;242(6):1160–1167. [PubMed] [Google Scholar]
  15. Mondovì B., Rotilio G., Finazzi-Agrò A., Costa M. T. Diamine oxidase inactivation by hydrogen peroxide. Biochim Biophys Acta. 1967 Mar 15;132(2):521–523. doi: 10.1016/0005-2744(67)90175-1. [DOI] [PubMed] [Google Scholar]
  16. Oi S., Inamasu M., Yasunobu K. T. Mechanistic studies of beef plasma amine oxidase. Biochemistry. 1970 Aug 18;9(17):3378–3383. doi: 10.1021/bi00819a013. [DOI] [PubMed] [Google Scholar]
  17. Oi S., Yasunobu K. T., Westley J. The effect of pH on the kinetic parameters and mechanism of beef liver monoamine oxidase. Arch Biochem Biophys. 1971 Aug;145(2):557–564. doi: 10.1016/s0003-9861(71)80015-2. [DOI] [PubMed] [Google Scholar]
  18. Rotilio G., Calabrese L., Finazzi Agrò A., Mondovì B. Indirect evidence for the production of superoxide anion radicals by pig kidney diamine oxidase. Biochim Biophys Acta. 1970 Mar 18;198(3):618–620. doi: 10.1016/0005-2744(70)90143-9. [DOI] [PubMed] [Google Scholar]
  19. Tipton K. F. The reaction pathway of pig brain mitochondrial monoamine oxidase. Eur J Biochem. 1968 Aug;5(3):316–320. doi: 10.1111/j.1432-1033.1968.tb00372.x. [DOI] [PubMed] [Google Scholar]
  20. Yamasaki E. F., Swindell R., Reed D. J. Some aspects of catalysis by the amine oxidase of pea seedlings. Biochemistry. 1970 Mar 3;9(5):1206–1210. doi: 10.1021/bi00807a022. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES