Cloning of a gene encoding 4-amino-3-hydroxybenzoate 2,3-dioxygenase from Bordetella sp. 10d

Biochemical and Biophysical Research Communications

Volumn 314, Issue 2, 2004, Pages 489-494

  Murakami, Shuichiro ^a   Sawami, Yoshimitsu ^a   Takenaka, Shinji ^a   Aoki, Kenji ^a  

^a KOBE UNIVERSITY   (Japan)

Author keywords

2 Aminophenol derivatives; 4 Amino 3 hydroxybenzoate 2,3 dioxygenase; 4 Amino 3 hydroxybenzoate degrading bacterium; Bordetella; LysR family regulator; Meta cleavage pathway

Indexed keywords

4 AMINO 3 HYDROXYBENZOATE 2,3 DIOXYGENASE; BENZOIC ACID DERIVATIVE; OXYGENASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BORDETELLA; CONTROLLED STUDY; DNA BINDING MOTIF; EUKARYOTE; GENE EXPRESSION; METABOLISM; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; OPEN READING FRAME; PRIORITY JOURNAL; PROKARYOSIS; PROTEIN EXPRESSION; PROTEIN MOTIF; REDUCTION; REGULATORY MECHANISM; START CODON; TRANSCRIPTION INITIATION SITE;

BACTERIA (MICROORGANISMS); BORDETELLA; BORDETELLA SP.; BORDETELLA SP. 10D; EUKARYOTA; PROKARYOTA;

EID: 0347004630     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2003.12.111     Document Type: Article

References (22)

1. Nakai C., Horiike K., Kuramitsu S., Kagamiyama H., Nozaki M. Three isozymes of catechol 1,2-dioxygenase (pyrocatechase), αα , αβ , and ββ , from Pseudomonas arvilla C-1 J. Biol. Chem. 265:1990;660-665.
2. Murakami S., Nakanishi Y., Kodama N., Takenaka S., Shinke R., Aoki K. Purification, characterization, and gene analysis of catechol 2,3-dioxygenase from the aniline-assimilating bacterium Pseudomonas species AW-2. Biosci. Biotechnol. Biochem. 62:1998;747-752.
3. Fujisawa H., Hayashibara O. Protocatechuate 3,4-dioxygenase. I. Crystallization and characterization. J. Biol. Chem. 243:1968;2673-2681.
4. Harpel M.R., Lipscomb J.D. Gentisate 1,2-dioxygenase from Pseudomonas: purification, characterization, and comparison of the enzymes from Pseudomonas testosteroni and Pseudomonas acidovorans. J. Biol. Chem. 265:1990;6301-6311.
5. Golovleva L.A., Zaborina O., Pertsova R., Baskunov B., Schurukhin Y., Kuzmin S. Degradation of polychlorinated phenols by Streptomyces rochei 303. Biodegradation. 2:1991;201-208.
6. Lendenmann U., Spain J.C. 2-Aminophenol 1,6-dioxygenase: a novel aromatic ring-cleavage enzyme purified from Pseudomonas pseudoalcaligenes JS45. J. Bacteriol. 178:1996;6227-6232.
7. Takenaka S., Murakami S., Shinke R., Hatakeyama K., Yukawa H., Aoki K. Novel genes encoding 2-aminohenol 1,6-dioxygense from Pseudomonas sp. AP-3 growing on 2-aminophenol and catalytic properties of the purified enzyme. J. Biol. Chem. 272:1997;14727-14732.
8. Hinter J.P., Lechner C., Riegert U., Kuhm A.E., Storm T., Reemtsma T., Stolz A. Direct ring fission of salicylate by a salicylate 1,2-dioxygenase activity from Pseudoaminobacter salicylatoxidans. J. Bacteriol. 183:2001;6936-6942.
9. Muraki T., Taki M., Hasegawa Y., Iwaki H., Lau P.C.K. Prokaryotic homologs of the eukaryotic 3-hydroxyanthranilate 3,4-dioxygenase and 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase in the 2-nitrobenzoate degradation pathway of Pseudomonas fluorescens strain KU-7. Appl. Environ. Microbiol. 69:2003;1564-1572.
10. Takenaka S., Asami T., Orii C., Murakami S., Aoki K. A novel meta-cleavage dioxygenase that cleaves a carboxyl-group-substituted 2-aminophenol. Eur. J. Biochem. 269:2002;5871-5877.
11. Sambrook J., Fritsch E.F., Maniatis T. Molecular Cloning. A Laboratory Manual. second ed. 1989;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
12. + aniline-assimilating Rhodococcus erythropolis AN-13. Gene. 185:1997;49-54.
13. Murakami S., Takashima A., Takemoto J., Takenaka S., Shinke R., Aoki K. Cloning and sequence analysis of two catechol-degrading gene clusters from the aniline-assimilating bacterium Frateuria sp. ANA-18. Gene. 226:1999;189-198.
14. Lowry O.H., Rosebrough N.J., Farr A.L., Randall R.J. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193:1951;265-275.
15. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
16. Shell M.A. Molecular biology of the LysR family of transcriptional regulators. Annu. Rev. Microbiol. 47:1993;597-626.
17. Goethals K., Van Montagu M., Holsters M. Conserved motifs in a divergent nod box of Azorhizobium caulinodans ORS571 reveal a common structure in promoters regulated by LysR-type proteins. Proc. Natl. Acad. Sci. USA. 89:1992;1646-1650.
18. Parsek M.R., Ye R.W., Pun P., Chakrabarty A.M. Critical nucleotides in the interaction of a LysR-type regulator with its target promoter region. J. Biol. Chem. 269:1994;11279-11284.
19. Shingler V., Powlowski J., Marklund U. Nucleotide sequence and functional analysis of the complete phenol/3,4-dimethylphenol catabolic pathway of Pseudomonas sp. strain CF600. J. Bacteriol. 174:1992;711-724.
20. Takeo M., Fujii T., Maeda Y. Sequence analysis of the genes encoding a multicomponent dioxygenase involved in oxidation of aniline and. o -toluidine in Acinetobacter sp. strain YAA J. Ferment. Bioeng. 85:1998;17-24.
21. Takeo M., Fujii T., Takenaka K., Maeda Y. Cloning and sequencing of a gene cluster for the meta-cleavage pathway of aniline degradation in Acinetobacter sp. strain YAA. J. Ferment. Bioeng. 85:1998;514-517.
22. Takenaka S., Murakami S., Kim Y.-J., Aoki K. Complete nucleotide sequence and functional analysis of the genes for 2-aminophenol metabolism from Pseudomonas sp. AP-3. Arch. Microbiol. 174:2000;265-272.