Cloning of the maoA gene that encodes aromatic amine oxidase of Escherichia coli W3350 and characterization of the overexpressed enzyme

European Journal of Biochemistry

Volumn 237, Issue 3, 1996, Pages 584-591

  Steinebach, Vincent ^a   Benen, Jac A E ^b   Bader, Rechien ^b   Postma, Pieter W ^b   De Vries, Simon ^a   Duine, Johannis A ^a  

^a DELFT UNIVERSITY OF TECHNOLOGY   (Netherlands)

^b UNIVERSITY OF AMSTERDAM   (Netherlands)

Author keywords

Amine oxidase; Enzyme characterization; Overexpression; Topaquinone

Indexed keywords

AMINE OXIDASE (COPPER CONTAINING);

ARTICLE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME PURIFICATION; ESCHERICHIA COLI; GENE EXPRESSION; ION EXCHANGE CHROMATOGRAPHY; MOLECULAR CLONING; PRIORITY JOURNAL; SPECTROPHOTOMETRY;

EID: 0029950157     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0584p.x     Document Type: Article

References (37)

1. Azakami, H., Yamashita, M., Roh, J., Suzuki, H., Kumagai, H. & Murooka, Y. (1994) Nucleotide sequence of the gene for monoamine oxidase (maoA) from Escherichia coli, J. Ferment. Bioeng. 77, 315-319.
2. Benen, J. A. E., van Berkel, W. J. H., van Dongen, W. M. A. M., Müller, F. & de Kok, A. (1989) Molecular cloning and sequence determination of the lpd gene encoding lipoamide dehydrogenase from Pseudomonas fluorescens, J. Gen. Microbiol. 135, 1787-1797.
3. Bossa, M., Morpurgo, G. O. & Morpurgo, L. (1994) Models and molecular orbital semiempirical calculations in the study of the spectroscopic properties of bovine serum amine oxidase quinone cofactor, Biochemistry 33, 4425-4431.
4. Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
5. Bruinenberg, P. G., Evers, M., Waterman, H. R., Kuipers, J., Arnberg, A. C. & Ab, G. (1989) Cloning and sequencing of the peroxisomal amine oxidase gene from Hansenula polymorpha, Biochim. Biophys. Acta 1008, 157-167.
6. Cai, D. & Klinman, J. P. (1994) Evidence for a self-catalytic mechanism of 2,4,5-trihydroxyphenylalanine quinone biogenesis in yeast copper amine oxidase, J. Biol. Chem. 269, 32039-32042.
7. Cooper, R. A., Knowles, P. F., Brown, D. E., McGuirl, M. A. & Dooley, D. M. (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.
8. Ehrenberg, A. & Reichard, P. (1972) Electron spin resonance of the iron-containing protein B2 from ribonucleotide reductase, J. Biol. Chem. 247, 3485-3488.
9. Fürste, J. P., Pansegrau, W., Frank, R., Blöcker, H., Scholz, P., Bagdasarian, M. & Lanka, E. (1986) Molecular cloning of the plasmid RP4 primase region in a multi-host-range tacP expression vector, Gene (Amst.) 48, 119-131.
10. Greenaway, F. T., O'Gara, C. Y., Marchena, J. M., Poku, J. W., Urtiaga, J. G. & Zou, Y. (1991) EPR studies of spin labeled bovine plasma amine oxidase: the nature of the substrate binding site, Arch. Biochem. Biophys. 285, 291-296.
11. Hanlon, S. P., Carpenter, K., Hassan, A. & Cooper, R. A. (1995) Formation in vitro of the 3,4,6-trihydroxyphenylalanine quinone cofactor, Biochem. J. 306, 627-630.
12. Haywood, G. W. & Large, P. J. (1981) Microbial oxidation of amines. Distribution, purification and properties of two primary-amine oxidases from the yeast Candida boidinii grown on amines as sole nitrogen source, Biochem. J. 199, 187-201.
13. Janes, S. M., Mu, D., Wemmer, D., Smith, A. J., Kaur, S., Maltby, D., Burlingume, A. L. & Klinman, J. P. (1990) A new redox cofactor in eukaryotic enzymes: 6-hydroxydopa at the active site of BSAO, Science 248, 981-987.
14. Janes, S. M. & Klinman, J. P. (1991) An investigation of BSAO active site stochiometry: evidence for an aminotransferase mechanism involving 2 carbonyl cofactors per enzyme dimer, Biochemistry 30, 4599-4605.
15. Klinman, J. P. & Mu, D. (1994) Quinoenzymes in biology, Annu. Rev. Biochem. 63, 299-344.
16. Kohara, Y., Akiyama, K. & Isono, K. (1987) The physical map of the whole E. coli chromosome: application of a new strategy for rapid analysis and sorting of a large genomic library, Cell 50, 495-508.
17. Maniatis, T., Fritsch, E. F. & Sambrook, J. (1989) Molecular cloning: a laboratory manual, 2nd edn. Cold Spring Harbor Laboratory Press, Cold Spring Harbor NY.
18. Matsuzaki, R., Fukui, T., Sato, H., Ozaki, Y. & Tanizawa, K. (1994) Generation of the topaquinone cofactor in bacterial monoamine oxidase by cupric ion-dependent autooxidation of a specific tyrosyl residue, FEBS Lett. 351, 360-364.
19. Matsuzaki, R., Suzuki, S., Yamaguchi, K., Fukui, T. & Tanizawa, K. (1995) Spectroscopic studies on the mechanism of the topaquinone generation in bacterial monoamine oxidase, Biochemistry 34, 4524-4530.
20. McIntire, W. S. & Hartmann, C. (1993) Copper-containing amine oxidases, in Principles and applications of quinoproteins (Davidson, V. L., ed.) pp. 97-171, Marcel Dekker, Inc., New York.
21. Moënne-Loccoz, P., Nakamura, N., Steinebach, V., Duine, J. A., Mure, M., Klinman, J. P. & Sanders-Loehr, J. (1995) Characterization of the topaquinone cofactor in amine oxidase from Escherichia coli by resonance Raman spectroscopy, Biochemistry 34, 7020-7026.
22. Morpurgo, L., Agostinelli, E., Mondovi, B., Avigliano, L., Silvestri, R., Stefancich, G. & Artico, M. (1992) BSAO: half-site reactivity with phenylhydrazine, semicarbazide and aromatic hydrazides, Biochemistry 31, 2615-2621.
23. Mu, D., Janes, S. M., Smith, A. J., Brown, D. E., Dooley, D. M. & Klinman, J. P. (1992) Tyrosine codon corresponds to topaquinone at the active site of copper amine oxidases, J. Biol. Chem. 267, 7979-7982.
24. Nordlund, P., Sjoberg, B. & Eklund, H. (1990) Three-dimensional structure of the free radical protein of ribonucleotide reductase, Nature 345, 593-598.
25. Roh, J. H., Suzuki, H., Azakami, H., Yamashita, M., Murooka, Y. & Kumagai, H. (1994) Crystallization and preliminiary X-ray analysis of copper amine oxidase from Escherichia coli K-12, Biosci. Biotech. Biochem. 58, 1652-1656.
26. Rudd, K. E. (1992) Alignment for E. coli DNA sequences to a revised, integrated genomic restriction map. in A short course in bacterial genetics: a laboratory manual and handbook for E. coli and related bacteria (Miller, J., ed.) pp. 2.3-2.43, Cold Spring Harbor Laboratory Press, Cold Spring Harbor NY.
27. Sanger, F., Nicklen, S. & Coulson, A. R. (1977) DNA sequencing with chain-terminating inhibitors, Proc. Natl Acad. Sci. USA 74, 549-556.
28. Shimizu, E., Ichise, H. & Yorifuji, T. (1990) Phenylethylamine oxidase, a novel enzyme of Arthrobacter globiformis, may be a quinoprotein, Agric. Biol. Chem. 54, 851-853.
29. Steinebach, V., Groen, B. W., Wijmenga, S. S., Niessen, W. M. A., Jongejan, J. A. & Duine, J. A. (1995) Identification of topaquinone, as illustrated for pig kidney diamine oxidase and Escherichia coli amine oxidase, Anal. Biochem. 230, 159-166.
30. Sugino, H., Sasaki, M., Azakami, H., Yamashita, M. & Murooka, Y. (1992) A monoamine-regulated Klebsiella aerogenes operon containing the monoamine oxidase structural gene (maoA) and the maoC gene, J. Bacteriol. 174, 2485-2492.
31. Tanizawa, K., Matsuzaki, R., Shimizu, E., Yorifuji, T. & Fukui, T. (1994) Cloning, sequencing of phenylethylamine oxidase from Arthrobacter globiformis and implication of Tyr-382 as the precursor to its covalently bound quinone cofactor, Biochem. Biophys. Res. Commun. 199, 1096-1102.
32. Turowski, P. N., McGuirl, M. A. & Dooley, D. M. (1993) Intramolecular electron transfer rate between active site copper and topaquinone in pea seedling amine oxidase, J. Biol. Chem. 268, 17680-17682.
33. van Iersel, J., Frank, J. & Duine, J. A. (1985) Determination of absorption coefficients of purified proteins by conventional ultraviolet spectrophotometry and chromatography combined with multiwavelength detection, Anal. Biochem. 151, 196-204.
34. van Iersel, J., van der Meer, R. A. & Duine, J. A. (1986) Methylamine oxidase from Arthrobacter P1. A bacterial copper-quinoprotein amine oxidase, Eur. J. Biochem. 161, 415-419.
35. Yamada, H., Adachi, O. & Ogata, K. (1965) Amine oxidases of microorganisms part II. Purification and crystallization of amine oxidases of Aspergillus niger, Agric. Biol. Chem. 33, 1707-1711.
36. Yannish-Perron, C., Vieira, J. & Messing, J. (1985) Improved M13 pliage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors, Gene (Amst.) 33, 103-119.
37. Zhang, X., Fuller, J. H. & McIntire, W. S. (1993) Cloning, sequencing, expression, and regulation of the structural gene for the copper/topaquinone-containing methylamine oxidase from Arthrobacter strain P1, a gram-positive facultative methylotroph, J. Bacteriol. 175, 5617-5627.