Catechol dioxygenases from Escherichia coli (MhpB) and Alcaligenes eutrophus (MpcI): Sequence analysis and biochemical properties of a third family of extradiol dioxygenases

Journal of Bacteriology

Volumn 178, Issue 17, 1996, Pages 5249-5256

  Spence, Emma L ^a   Kawamukai, Makoto ^b   Sanvoisin, Jonathan ^a   Braven, Helen ^a   Bugg, Timothy D H ^a  

^a UNIVERSITY OF SOUTHAMPTON   (United Kingdom)

^b SHIMANE UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

3 HYDROXYANTHRANILATE 3,4 DIOXYGENASE; 3,4 DIHYDROXYPHENYLACETATE 2,3 DIOXYGENASE; BACTERIAL ENZYME; CATECHOL 1,2 DIOXYGENASE; CATECHOL DERIVATIVE; CYSTEINE; EXTRADIOL DIOXYGENASE; HISTIDINE; OXYGENASE; PROTOCATECHUATE 4,5 DIOXYGENASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CHEMICAL MODIFICATION; CONTROLLED STUDY; ENZYME ANALYSIS; ENZYME SPECIFICITY; ESCHERICHIA COLI; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PSEUDOMONAS; SEQUENCE HOMOLOGY; WAUTERSIA EUTROPHA;

ALCALIGENES; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; PSEUDOMONAS; SPHINGOMONAS PAUCIMOBILIS; WAUTERSIA EUTROPHA;

EID: 0029789393     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.17.5249-5256.1996     Document Type: Article

References (24)

1. Asturias, J. A., L. D. Eltis, M. Prucha, and K. N. Timmis. 1994. Analysis of three 2,3-dihydroxybiphenyl 1,2-dioxygenases found in Rhodococcus globerulus P6. J. Biol. Chem. 269:7807-7815.
2. Blakley, E. R., and J. F. Simpson. 1963. The microbial metabolism of cinnamic acid. Can. J. Microbiol. 10:175-185.
3. 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.
4. Bugg, T. D. H. 1993. Overproduction, purification and properties of 2,3-dihydroxyphenylpropionate 1,2-dioxygenase from Escherichia coli. Biochim. Biophys. Acta 1202:258-264.
5. Burlingame, R. 1983. Ph.D. thesis. University of Minnesota, Minneapolis.
6. Burlingame, R., and P. J. Chapman. 1983. Catabolism of phenylpropionic acid and its 3-hydroxy derivative by Escherichia coli. J. Bacterial. 155:113-121.
7. Candidus, S., K. H. van Pee, and F. Lingens. 1994. The catechol 2,3-dioxygenase gene of Rhodococcus rhodochrous CTM: nucleotide sequence, comparison with isofunctional dioxygenases and evidence for an active-site histidine. Microbiology 140:321-330.
8. Christiansen, W. G. 1926. Some derivatives of gallic acid and pyrogallol. J. Am. Chem. Soc. 48:1358-1365.
9. Doolittle, R. F. 1987. Of URFs and ORFs: a primer on how to analyze derived amino acid sequences, p. 10-17. University Science Books. Mill Valley, Calif.
10. Han, S., L. D. Eltis, K. N. Timmis, S. W. Muchmore, and J. T. Bolin. 1995. Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading Pseudomonad. Science 270:976-980.
11. Harayama, S., M. Kok, and E. L. Neidle. 1992. Functional and evolutionary relationships among diverse oxygenases. Annu. Rev. Microbiol. 46:565-601.
12. Harayama, S., and M. Rekik. 1989. Bacterial aromatic ring-cleavage enzymes are classified into two different gene families. J. Biol. Chem. 264: 15328-15333.
13. Heiss, G., A. Stolz, A. E. Kuhm, C. Müller, J. Klein, J. Altenbuchner, and H. J. Knackmuss. 1995. Characterization of a 2,3-dihydroxybiphenyl dioxygenase from the naphthalene sulfonate-degrading bacterium strain BN6. J. Bacteriol. 177:5865-5871.
14. Kabisch, M., and P. Fortnagel. 1990. Nucleotide sequence of metapyrocatechase I (catechol 2,3-oxygenase I) gene mpcI from Alcaligenes eutrophus JMP222. Nucleic Acids Res. 18:3405-3406.
15. Kohara, Y., K. Akiyama, and K. Isono, 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.
16. Malherbe, P., C. Köhler, M. Da Prada, G. Lang, V. Kiefer, R. Schwarcz, H. W. Lahm, and A. M. Cesura. 1994. Molecular cloning and functional expression of human 3-hydroxyanthranilic acid dioxygenase. J. Biol. Chem. 269:13792-13797.
17. Noda, Y., S. Nishikawa, K. I. Shiozuka, H. Kadokura, H. Nakajima, K. Yuda, Y. Katayama, N. Morohoshi, T. Haraguchi, and M. Yamasaki. 1990. Molecular cloning of the protocatechuate 4,5-dioxygenase genes of Pseudomonas paucimobilis. J. Bacteriol. 172:2704-2709.
18. Pascal, R. A., Jr., and D. S. Huang. 1986. Reactions of 3-ethyl-catechol and 3-(methylthio)-catechol with catechol dioxygenases. Arch. Biochem. Biophys. 248:130-137.
19. Roper, D. I., and R. A. Cooper. 1990. Subcloning and nucleotide sequence of the 3,4-dihydroxyphenylacetate (homoprotocatechuate) 2,3-dioxygenase gene from Escherichia coli C. FEBS Lett. 275:53-57.
20. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
21. Sanger, F., S. Nicklen, and A. R. Coulson. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74:5463-5467.
22. Segel, I. H. 1993. Enzyme kinetics, p. 371-385. Wiley-Interscience, New York.
23. Spence, E. L., G. J. Langley, and T. D. H. Bugg. Cis-trans isomerisation of a cyclopropyl radical trap catalysed by extradiol catechol dioxygenases: evidence for a semiquinone intermediate. J. Am. Chem. Soc., in press.
24. Vogel, A. I. 1989. Vogel's textbook of practical organic chemistry, 5th ed., p. 695-701. Longman, Harlow, United Kingdom.