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. 1972 Jun;128(2):253–263. doi: 10.1042/bj1280253

Inhibition of pig kidney diamine oxidase by substrate analogues

W G Bardsley 1,2, J S Ashford 1,2
PMCID: PMC1173761  PMID: 4628527

Abstract

1. The oxidation of p-dimethylaminomethylbenzylamine was followed spectrophotometrically by measuring the change in E250 caused by the p-dimethylaminomethylbenzaldehyde produced. 2. This reaction was inhibited by substrate analogues such as isothiouronium, guanidino, dimethylsulphonium and trimethylammonium compounds. 3. The inhibition by both mono- and bis-onium compounds has been studied and a comprehensive theory is developed to explain both the type and degree of inhibition produced.

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Selected References

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  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. BLASCHKO H., FASTIER F. N., WAJDA I. The inhibition of histaminase by amidines. Biochem J. 1951 Jul;49(2):250–253. doi: 10.1042/bj0490250. [DOI] [PMC free article] [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., 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]
  5. 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]
  6. CHAPMAN J. E., WALASZEK E. J. Inhibition of diamine oxidase by bulbocapnine. Biochem Pharmacol. 1962 Mar;11:205–210. doi: 10.1016/0006-2952(62)90075-8. [DOI] [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. Costa M. T., Rotilio G., Agró A. F., Vallogini M. P., Mondovì B. On the active site of diamine oxidase: kinetic studies. Arch Biochem Biophys. 1971 Nov;147(1):8–13. doi: 10.1016/0003-9861(71)90303-1. [DOI] [PubMed] [Google Scholar]
  11. 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]
  12. 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]
  13. Kumagai H., Yamada H., Suzuki H., Ogura Y. Action mechanism of tyramine oxidase from Sarcina lutea. J Biochem. 1971 Jan;69(1):137–144. doi: 10.1093/oxfordjournals.jbchem.a129442. [DOI] [PubMed] [Google Scholar]
  14. Macholan L., Rozprimova L., Sedlackova E. 1,4-diamino-2-butanon (2-ketoputrescine) as strong and short acting competitive inhibitor of diamine oxidase. Biochim Biophys Acta. 1967 Mar 15;132(2):505–507. doi: 10.1016/0005-2744(67)90169-6. [DOI] [PubMed] [Google Scholar]
  15. 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]
  16. 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]
  17. 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]
  18. 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]
  19. 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]
  20. 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]
  21. 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]

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