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Gene Review

catB  -  muconate and chloromuconate cycloisomerase

Pseudomonas putida KT2440

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Disease relevance of catB


High impact information on catB


Chemical compound and disease context of catB


Biological context of catB

  • We report the presence of an additional binding site for CatR downstream of the catBCA promoter within the catB structural gene [6].
  • By deletion analysis and the use of pKT240 as a promoter probe vector, we located a single promoter region for the catBC operon upstream of catB [8].
  • Cloning and complete nucleotide sequence determination of the catB gene encoding cis,cis-muconate lactonizing enzyme [9].
  • By conjugation experiments, the genes conferring these growth abilities have been shown to be located on the bacterial chromosome, linked to vil and catB [10].
  • Comparison of the nucleotide and amino acid sequences for catB with the corresponding sequences of the clcB gene (K.L. Ngai, B.F., D.K. Chatterjee, L.N. Ornston, and A.M.C., unpublished), whose gene product catalyzes the analogous reaction in 3-chlorobenzoate degradation, showed significant homology [9].

Associations of catB with chemical compounds


Other interactions of catB

  • CatR binds to both a DNA fragment containing the catR-catB intergenic region and another DNA fragment containing catC [1].
  • This contrasts with the gene arrangement in other bacteria, in which catA lies several kilobases upstream from catB [1].

Analytical, diagnostic and therapeutic context of catB


  1. Discontinuities in the evolution of Pseudomonas putida cat genes. Houghton, J.E., Brown, T.M., Appel, A.J., Hughes, E.J., Ornston, L.N. J. Bacteriol. (1995) [Pubmed]
  2. Organization and nucleotide sequence determination of a gene cluster involved in 3-chlorocatechol degradation. Frantz, B., Chakrabarty, A.M. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  3. Mechanism of chloride elimination from 3-chloro- and 2,4-dichloro-cis,cis-muconate: new insight obtained from analysis of muconate cycloisomerase variant CatB-K169A. Kaulmann, U., Kaschabek, S.R., Schlömann, M. J. Bacteriol. (2001) [Pubmed]
  4. Cloning and sequence analysis of two catechol-degrading gene clusters from the aniline-assimilating bacterium Frateuria species ANA-18. Murakami, S., Takashima, A., Takemoto, J., Takenaka, S., Shinke, R., Aoki, K. Gene (1999) [Pubmed]
  5. Transcriptional activation of the catechol and chlorocatechol operons: variations on a theme. McFall, S.M., Chugani, S.A., Chakrabarty, A.M. Gene (1998) [Pubmed]
  6. Transcriptional repression mediated by LysR-type regulator CatR bound at multiple binding sites. Chugani, S.A., Parsek, M.R., Chakrabarty, A.M. J. Bacteriol. (1998) [Pubmed]
  7. Inability of muconate cycloisomerases to cause dehalogenation during conversion of 2-chloro-cis,cis-muconate. Vollmer, M.D., Fischer, P., Knackmuss, H.J., Schlömann, M. J. Bacteriol. (1994) [Pubmed]
  8. Transcriptional regulation, nucleotide sequence, and localization of the promoter of the catBC operon in Pseudomonas putida. Aldrich, T.L., Chakrabarty, A.M. J. Bacteriol. (1988) [Pubmed]
  9. Cloning and complete nucleotide sequence determination of the catB gene encoding cis,cis-muconate lactonizing enzyme. Aldrich, T.L., Frantz, B., Gill, J.F., Kilbane, J.J., Chakrabarty, A.M. Gene (1987) [Pubmed]
  10. Chromosomal location of TOL plasmid DNA in Pseudomonas putida. Sinclair, M.I., Maxwell, P.C., Lyon, B.R., Holloway, B.W. J. Bacteriol. (1986) [Pubmed]
  11. Substrate specificity of and product formation by muconate cycloisomerases: an analysis of wild-type enzymes and engineered variants. Vollmer, M.D., Hoier, H., Hecht, H.J., Schell, U., Gröning, J., Goldman, A., Schlömann, M. Appl. Environ. Microbiol. (1998) [Pubmed]
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