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. 1973 Dec;135(4):735–750. doi: 10.1042/bj1350735

The reaction pathway of membrane-bound rat liver mitochondrial monoamine oxidase

Miles D Houslay 1, Keith F Tipton 1
PMCID: PMC1165890  PMID: 4778271

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 O2 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, NaN3, 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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Selected References

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  1. ALIVISATOS S. G., MOURKIDES G. A., JIBRIL A. Non-enzymic reactions of indoles with coenzyme I. Nature. 1960 May 28;186:718–719. doi: 10.1038/186718a0. [DOI] [PubMed] [Google Scholar]
  2. 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]
  3. Coleman R. Membrane-bound enzymes and membrane ultrastructure. Biochim Biophys Acta. 1973 Apr 3;300(1):1–30. doi: 10.1016/0304-4157(73)90010-5. [DOI] [PubMed] [Google Scholar]
  4. DALZIEL K. Some observations on the preparation and properties of dihydronicotinamide-adenine dinucleotide. Biochem J. 1962 Aug;84:240–244. doi: 10.1042/bj0840240. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. DIXON M. The determination of enzyme inhibitor constants. Biochem J. 1953 Aug;55(1):170–171. doi: 10.1042/bj0550170. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Duncan R. J., Tipton K. F. The purification and properties of the NAD-linked aldehyde dehydrogenase from pig brain. Eur J Biochem. 1971 Sep 24;22(2):257–262. doi: 10.1111/j.1432-1033.1971.tb01539.x. [DOI] [PubMed] [Google Scholar]
  7. Feldman R. I., Weiner H. Horse liver aldehyde dehydrogenase. I. Purification and characterization. J Biol Chem. 1972 Jan 10;247(1):260–266. [PubMed] [Google Scholar]
  8. Feldman R. I., Weiner H. Horse liver aldehyde dehydrogenase. I. Purification and characterization. J Biol Chem. 1972 Jan 10;247(1):260–266. [PubMed] [Google Scholar]
  9. Fischer A. G., Schulz A. R., Oliner L. Thyroidal biosynthesis of iodothyronines. II. General charactero acteristics and purification of mitochondrial monoamine oxidase. Biochim Biophys Acta. 1968 Jul 9;159(3):460–471. doi: 10.1016/0005-2744(68)90130-7. [DOI] [PubMed] [Google Scholar]
  10. Gabay S., Valcourt A. J. Studies of monoamine oxidases. I. Purification and properties of the rabbit liver mitochondrial enzyme. Biochim Biophys Acta. 1968 Jul 9;159(3):440–450. doi: 10.1016/0005-2744(68)90128-9. [DOI] [PubMed] [Google Scholar]
  11. Gomes B., Igaue I., Kloepper H. G., Yasunobu K. T. Amine oxidase. XIV. Isolation and characterization of the multiple beef liver amine oxidase components. Arch Biochem Biophys. 1969 Jun;132(1):16–27. doi: 10.1016/0003-9861(69)90334-8. [DOI] [PubMed] [Google Scholar]
  12. Greenawalt J. W. Localization of monoamine oxidase in rat liver mitochondria. Adv Biochem Psychopharmacol. 1972;5:207–226. [PubMed] [Google Scholar]
  13. Harada M., Mizutani K., Nagatsu T. Purification and properties of mitochondrial monoamine oxidase in beef brain. J Neurochem. 1971 Apr;18(4):559–569. doi: 10.1111/j.1471-4159.1971.tb11986.x. [DOI] [PubMed] [Google Scholar]
  14. Hare M. L. Tyramine oxidase: A new enzyme system in liver. Biochem J. 1928;22(4):968–979. doi: 10.1042/bj0220968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Houslay M. D., Tipton K. F. The nature of the electrophoretically separable multiple forms of rat liver monoamine oxidase. Biochem J. 1973 Sep;135(1):173–186. doi: 10.1042/bj1350173. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Huszti Z., Borsy J. Differences between amine oxidases deaminating mescaline and the structurally related 3,4-dimethoxyphenylethyl amine. Biochem Pharmacol. 1966 Apr;15(4):475–480. doi: 10.1016/0006-2952(66)90257-7. [DOI] [PubMed] [Google Scholar]
  17. Jarrott B. Occurrence and properties of monoamine oxidase in adrenergic neurons. J Neurochem. 1971 Jan;18(1):7–16. doi: 10.1111/j.1471-4159.1971.tb00162.x. [DOI] [PubMed] [Google Scholar]
  18. Johnston J. P. Some observations upon a new inhibitor of monoamine oxidase in brain tissue. Biochem Pharmacol. 1968 Jul;17(7):1285–1297. doi: 10.1016/0006-2952(68)90066-x. [DOI] [PubMed] [Google Scholar]
  19. Kohn H. I. Tyramine oxidase. Biochem J. 1937 Oct;31(10):1693–1704. doi: 10.1042/bj0311693. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  21. McEwen C. M., Jr, Sasaki G., Jones D. C. Human liver mitochondrial monoamine oxidase. II. Determinants of substrate and inhibitor specificities. Biochemistry. 1969 Oct;8(10):3952–3962. doi: 10.1021/bi00838a011. [DOI] [PubMed] [Google Scholar]
  22. Middleton B. The kinetic mechanism of 3-hydroxy-3-methylglutaryl-coenzyme A synthase from baker's yeast. Biochem J. 1972 Jan;126(1):35–47. doi: 10.1042/bj1260035. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. OSWALD E. O., STRITTMATTER C. F. COMPARATIVE STUDIES IN THE CHARACTERIZATION OF MONOAMINE OXIDASES. Proc Soc Exp Biol Med. 1963 Dec;114:668–673. doi: 10.3181/00379727-114-28765. [DOI] [PubMed] [Google Scholar]
  24. Oi S., Shimada K., Inamasu M., Yasunobu K. T. Mechanistic studies of beef liver mitochondrial amine oxidase. 18. Amine oxidase. Arch Biochem Biophys. 1970 Jul;139(1):28–37. doi: 10.1016/0003-9861(70)90041-x. [DOI] [PubMed] [Google Scholar]
  25. 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]
  26. Philpot F. J. Some observations on the oxidation of tyramine in the liver. Biochem J. 1937 Jun;31(6):856–861. doi: 10.1042/bj0310856. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Robinson D. S., Lovenberg W., Keiser H., Sjoerdsma A. Effects of drugs on human blood platelet and plasma amine oxidase activity in vitro and in vivo. Biochem Pharmacol. 1968 Jan;17(1):109–119. doi: 10.1016/0006-2952(68)90163-9. [DOI] [PubMed] [Google Scholar]
  28. Schnaitman C., Erwin V. G., Greenawalt J. W. The submitochondrial localization of monoamine oxidase. An enzymatic marker for the outer membrane of rat liver mitochondria. J Cell Biol. 1967 Mar;32(3):719–735. doi: 10.1083/jcb.32.3.719. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Sottocasa G. L., Kuylenstierna B., Ernster L., Bergstrand A. An electron-transport system associated with the outer membrane of liver mitochondria. A biochemical and morphological study. J Cell Biol. 1967 Feb;32(2):415–438. doi: 10.1083/jcb.32.2.415. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Sourkes T. L. Properties of the monoamine oxidase of rat liver mitochondria. Adv Pharmacol. 1968;6(Pt A):61–69. doi: 10.1016/s1054-3589(08)61156-4. [DOI] [PubMed] [Google Scholar]
  31. Squires R. F., Lassen J. B. Some pharmacological and biochemical properties of gamma-morpholino-butyrophenone (NSD 2023), a new monoamine oxidase inhibitor. Biochem Pharmacol. 1968 Mar;17(3):369–384. doi: 10.1016/0006-2952(68)90247-5. [DOI] [PubMed] [Google Scholar]
  32. TABOR C. W., TABOR H., ROSENTHAL S. M. Purification of amine oxidase from beef plasma. J Biol Chem. 1954 Jun;208(2):645–661. [PubMed] [Google Scholar]
  33. TUBBS P. K. Effects of inhibitors on mitochondrial D-alpha-hydroxy acid dehydrogenase. Biochem J. 1962 Jan;82:36–42. doi: 10.1042/bj0820036. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Tipton K. F., Spires I. P. Oxidation of 2-phenylethylhydrazine by monoamine oxidase. Biochem Pharmacol. 1972 Jan 15;21(2):268–270. doi: 10.1016/0006-2952(72)90278-x. [DOI] [PubMed] [Google Scholar]
  35. Tipton K. F., Spires I. P. The kinetics of phenethylhydrazine oxidation by monoamine oxidase. Biochem J. 1971 Nov;125(2):521–524. doi: 10.1042/bj1250521. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Tipton K. F. The prosthetic groups of pig brain mitochondrial monoamine oxidase. Biochim Biophys Acta. 1968 Jul 9;159(3):451–459. doi: 10.1016/0005-2744(68)90129-0. [DOI] [PubMed] [Google Scholar]
  37. Tipton K. F. The purification of pig brain mitochondrial monoamine oxidase. Eur J Biochem. 1968 Mar;4(1):103–107. doi: 10.1111/j.1432-1033.1968.tb00178.x. [DOI] [PubMed] [Google Scholar]
  38. 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]
  39. Tipton K. F. The sub-mitochondrial localization of monoamine oxidase in rat liver and brain. Biochim Biophys Acta. 1967;135(5):910–920. doi: 10.1016/0005-2736(67)90060-0. [DOI] [PubMed] [Google Scholar]
  40. Van Woert M. H., Cotzias G. C. Anion inhibition of monoamine oxidase. Biochem Pharmacol. 1966 Mar;15(3):275–285. doi: 10.1016/0006-2952(66)90299-1. [DOI] [PubMed] [Google Scholar]
  41. Veryovkina I. V., Samed M. M., Gorkin V. Z. Mitochondrial monoamine oxidase of rat liver: reversible qualitative alterations in catalytic properties. Biochim Biophys Acta. 1972 Jan 20;258(1):56–70. doi: 10.1016/0005-2744(72)90966-7. [DOI] [PubMed] [Google Scholar]
  42. Yang H. Y., Goridis C., Neff N. H. Properties of monoamine oxidases in sympathetic nerve and pineal gland. J Neurochem. 1972 May;19(5):1241–1250. doi: 10.1111/j.1471-4159.1972.tb01450.x. [DOI] [PubMed] [Google Scholar]

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