Presence of an Inducible Semicarbazide-Sensitive Amine Oxidase in Mycobacterium sp. Strain JC1 DSM 3803 Grown on Benzylamine

  • Ro Young-Tae (Department of Biochemistry, Graduate School of Medicine, Konkuk University) ;
  • Lee Hyun-Il (Department of Biochemistry, Graduate School of Medicine, Konkuk University) ;
  • Kim Young-Min (Department of Biology, Yonsei University)
  • 발행 : 2006.04.01

초록

Mycobacterium sp. strain JC1 was capable of growth on benzylamine as a sole source of carbon and energy. The primary deamination of benzylamine was mediated by an inducible amine oxidase, which can also oxidize tyramine, histamine, and dopamine. Inhibitor study identified this enzyme as a copper-containing amine oxidase sensitive to semicarbazide.

키워드

참고문헌

  1. Chistoserdov, A.Y. 2001. Cloning, sequencing and mutagenesis of the genes for aromatic amine dehydrogenase from Alcaligenes faecalis and evolution of amine dehydrogenases. Microbiology 147, 2195-2202 https://doi.org/10.1099/00221287-147-8-2195
  2. Cho, J.W., H.S. Yim, and Y.M. Kim. 1985. Acinetobacter isolates growing with carbon monoxide. Kor. J. Microbiol. 23, 1-8
  3. Cooper, R.A., P.F. Knowles, D.E. Brown, M.A. McGuirl, and D.M. Dooley. 1992. Evidence for copper and 3,4,6- trihydroxyphenylalanine quinone cofactors in an amine oxidase from the gram-negative bacterium Escherichia coli K-12. Biochem. J. 288, 337-340 https://doi.org/10.1042/bj2880337
  4. Cuskey, S.M., V. Peccoraro, and R.H. Olsen. 1987. Initial catabolism of aromatic biogenic amines by Pseudomonas aeruginosa PAO: pathway description, mapping of mutations, and cloning of essential genes. J. Bacteriol. 169, 2398-2404 https://doi.org/10.1128/jb.169.6.2398-2404.1987
  5. Durham, D.R. and J.J. Perry. 1978. Purification and characterization of a heme-containing amine dehydrogenase from Pseudomonas putida. J. Bacteriol. 134, 837-843
  6. Eady, R.R. and P.J. Large. 1968. Purification and properties of an amine dehydrogenase from Pseudomonas AM1 and its role in growth on methylamine. Biochem. J. 106, 245-255 https://doi.org/10.1042/bj1060245
  7. Freeman, H.C., J.M. Guss, V. Kumar, W.S. McIntire, and V.M. Zubak. 1996. Purification, crystallization and preliminary X-ray crystal structure analysis of copper amine oxidase from Arthrobacter globoformis. Acta Crystallogr. D. Biol. Crystallogr. 52, 197-198 https://doi.org/10.1107/S0907444995007529
  8. Hacisalihoglu, A., J.A. Jongejan, and J.A. Duine. 1997. Distribution of amine oxidases and amine dehydrogenases in bacteria grown on primary amines and characterization of the amine oxidase from Klebsiella oxytoca. Microbiology 143, 505-512 https://doi.org/10.1099/00221287-143-2-505
  9. Hochman, A. and I. Goldberg. 1991. Purification and characterization of a catalase-peroxidase and a typical catalase from the bacterium Klebsiella pneumoniae. Biochim. Biophys. Acta. 1077, 299-307 https://doi.org/10.1016/0167-4838(91)90544-A
  10. Kim, Y.M. and G.D. Hegeman. 1981. Purification and some properties of carbon monoxide dehydrogenase from Pseudomonas carboxydohydrogena. J. Bacteriol. 148, 904- 911
  11. Kondo, T., E. Kondo, H. Maki, K. Yasumoto, K. Takagi, K. Kano, and T. Ikeda. 2004. Purification and characterization of aromatic amine dehydrogenase from Alcaligenes xylosoxidans. Biosci. Biotechnol. Biochem. 68, 1921-1928 https://doi.org/10.1271/bbb.68.1921
  12. Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685 https://doi.org/10.1038/227680a0
  13. Lee, M.H., M.T. Chuang, and W.C. Hou. 2002. Activity staining of plasma amine oxidase after polyacrylamide gel electrophoresis and its application to natural inhibitor screening. Electrophoresis 23, 2369-2372 https://doi.org/10.1002/1522-2683(200208)23:15<2369::AID-ELPS2369>3.0.CO;2-Z
  14. Levering, P.R., J.P. van Dijken, M. Veenhius, and W. Harder. 1981. Arthrobacter P1, a fast growing versatile methylotroph with amine oxidase as a key enzyme in the metabolism of methylated amines. Arch. Microbiol. 129, 72-80 https://doi.org/10.1007/BF00417184
  15. Murooka, Y., N. Doi, and T. Harada. 1979. Distribution of membrane-bound monoamine oxidase in bacteria. Appl. Environ. Microbiol. 38, 565-569
  16. Newton-Vinson, P., F. Hubalek, and D.E. Edmondson. 2000. High-level expression of human liver monoamine oxidase B in Pichia pastoris. Protein Expr. Purif. 20, 334-345 https://doi.org/10.1006/prep.2000.1309
  17. Okamura, H., Y. Murooka, and T. Harada. 1976. Regulation of tyramine oxidase synthesis in Klebsiella aerogenes. J. Bacteriol. 127, 24-31
  18. Park, S.W., E.H. Hwang, H. Park, J.A. Kim, J. Heo, K.H. Lee, T. Song, E. Kim, Y.T. Ro, S.W. Kim, and Y.M. Kim. 2003. Growth of mycobacteria on carbon monoxide and methanol. J. Bacteriol. 185, 142-147 https://doi.org/10.1128/JB.185.1.142-147.2003
  19. Parrott, S., S. Jones, and R.A. Cooper. 1987. 2-Phenylethylamine catabolism by Escherichia coli K12. J. Gen. Microbiol. 133, 347-351
  20. Ro, Y.T., E. Kim, and Y.M. Kim. 2000. Enzyme activities related to the methanol oxidation of Mycobacterium sp. strain JC1 DSM 3803. J. Microbiol. 38, 209-217
  21. Ro, Y.T., H.I. Lee, E.J. Kim, J.H. Koo, E. Kim, and Y.M. Kim. 2003. Purification, characterization, and physiological response of a catalase-peroxidase in Mycobacterium sp. strain JC1 DSM 3803 grown on methanol. FEMS Microbiol. Lett. 226, 397-403 https://doi.org/10.1016/S0378-1097(03)00644-X
  22. Ro, Y.T., J.G. Seo, J.H. Lee, D.M Kim, I.K. Chung, T.U. Kim, and Y.M. Kim. 1997. Growth on methanol of a carboxydobacterium, Acinetobacter sp. Strain JC1 DSM 3803. J. Microbiol. 35, 30-39
  23. Roh, J.H., J. Wouters, E. Depiereux, H. Yukawa, M. Inui, H. Minami, H. Suzuki, and H. Kumagai. 2000. Purification, cloning, and three-dimensional structure prediction of Micrococcus luteus FAD-containing tyramine oxidase. Biochem. Biophys. Res. Commun. 268, 293-297 https://doi.org/10.1006/bbrc.2000.2113
  24. Takagi, K., M. Torimura, K. Kawaguchi, K. Kano, and T. Ikeda. 1999. Biochemical and electrochemical characterization of quinohemoprotein amine dehydrogenase from Paracoccus denitrificans. Biochemistry 38, 6935-6942 https://doi.org/10.1021/bi9828268