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Gene Review

catA  -  catechol 1,2-dioxygenase

Acinetobacter sp. ADP1

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Disease relevance of catA

  • On the basis of the constitutive phenotypes of two catM mutants of Acinetobacter calcoaceticus, the CatM protein was proposed to repress expression of two different loci involved in catechol degradation, catA and catBCIJFD (E. Neidle, C. Hartnett, and L. N. Ornston, J. Bacteriol. 171:5410-5421, 1989) [1].
  • The similarly sized Pseudomonas clcA gene encodes catechol 1,2-dioxygenase II, an enzyme with relatively broad substrate specificity and relatively low catalytic efficiency [2].
  • When the catA-containing fragment was placed under the control of the lac promoter on pUC19 and induced with isopropylthiogalactopyranoside, catechol dioxygenase was formed in E. coli at twice the level found in fully induced cultures of A. calcoaceticus [3].
  • Two copies of the Klebsiella pneumoniae aroZ gene encoding DHS dehydratase were inserted into the E. coli chromosome, while the K. pneumoniae aroY gene encoding PCA decarboxylase and the Acinetobacter calcoaceticus catA gene encoding catechol 1,2-dioxygenase were expressed from an extrachromosomal plasmid [4].

High impact information on catA


Chemical compound and disease context of catA


Biological context of catA

  • The DNA sequence of a 1.6-kilobase-pair SalI-KpnI Acinetobacter calcoaceticus restriction fragment carrying catA, the structural gene for catechol 1,2-dioxygenase I, was determined [2].
  • The 3.8-kbp sequence revealed that directly downstream from catA and potentially transcribed in the same direction were two open reading frames encoding polypeptides of 48 and 36 kilodaltons (kDa) [10].
  • Comparison of the catA and clcA sequences demonstrated their common ancestry and suggested that acquisitions of direct and inverted sequence repetitions of 6 to 10 base pairs were frequent events in their evolutionary divergence [2].
  • The latter procedure was also used to identify a single amino acid substitution in PcaG that conferred activity towards catechol sufficient for growth with benzoate in a strain in which catechol 1,2-dioxygenase was inactivated [11].
  • Two catA genes, catA1 and catA2, encoding by CD I1 and CD I2, respectively, were isolated from the A. lwoffii K24 genomic library by using colony hybridization and PCR [12].

Associations of catA with chemical compounds


Other interactions of catA

  • In a catM-disrupted strain, BenM was able to induce higher levels of catA expression than catB expression [13].

Analytical, diagnostic and therapeutic context of catA


  1. catM encodes a LysR-type transcriptional activator regulating catechol degradation in Acinetobacter calcoaceticus. Romero-Arroyo, C.E., Schell, M.A., Gaines, G.L., Neidle, E.L. J. Bacteriol. (1995) [Pubmed]
  2. DNA sequence of the Acinetobacter calcoaceticus catechol 1,2-dioxygenase I structural gene catA: evidence for evolutionary divergence of intradiol dioxygenases by acquisition of DNA sequence repetitions. Neidle, E.L., Hartnett, C., Bonitz, S., Ornston, L.N. J. Bacteriol. (1988) [Pubmed]
  3. Cloning and expression of Acinetobacter calcoaceticus catechol 1,2-dioxygenase structural gene catA in Escherichia coli. Neidle, E.L., Ornston, L.N. J. Bacteriol. (1986) [Pubmed]
  4. Benzene-free synthesis of adipic acid. Niu, W., Draths, K.M., Frost, J.W. Biotechnol. Prog. (2002) [Pubmed]
  5. Genome plasticity in Acinetobacter: new degradative capabilities acquired by the spontaneous amplification of large chromosomal segments. Reams, A.B., Neidle, E.L. Mol. Microbiol. (2003) [Pubmed]
  6. Genetic organization, nucleotide sequence and regulation of expression of genes encoding phenol hydroxylase and catechol 1,2-dioxygenase in Acinetobacter calcoaceticus NCIB8250. Ehrt, S., Schirmer, F., Hillen, W. Mol. Microbiol. (1995) [Pubmed]
  7. pWW174: a large plasmid from Acinetobacter calcoaceticus encoding benzene catabolism by the beta-ketoadipate pathway. Winstanley, C., Taylor, S.C., Williams, P.A. Mol. Microbiol. (1987) [Pubmed]
  8. Benzoate and muconate, structurally dissimilar metabolites, induce expression of catA in Acinetobacter calcoaceticus. Neidle, E.L., Ornston, L.N. J. Bacteriol. (1987) [Pubmed]
  9. Degradation of non-phenolic beta-o-4 lignin substructure model compounds by Acinetobacter sp. Vasudevan, N., Mahadevan, A. Res. Microbiol. (1992) [Pubmed]
  10. Characterization of Acinetobacter calcoaceticus catM, a repressor gene homologous in sequence to transcriptional activator genes. Neidle, E.L., Hartnett, C., Ornston, L.N. J. Bacteriol. (1989) [Pubmed]
  11. Substitution, insertion, deletion, suppression, and altered substrate specificity in functional protocatechuate 3,4-dioxygenases. D'Argenio, D.A., Vetting, M.W., Ohlendorf, D.H., Ornston, L.N. J. Bacteriol. (1999) [Pubmed]
  12. Cloning and characterization of two catA genes in Acinetobacter lwoffii K24. Kim, S.I., Leem, S.H., Choi, J.S., Chung, Y.H., Kim, S., Park, Y.M., Park, Y.K., Lee, Y.N., Ha, K.S. J. Bacteriol. (1997) [Pubmed]
  13. Regulation of benzoate degradation in Acinetobacter sp. strain ADP1 by BenM, a LysR-type transcriptional activator. Collier, L.S., Gaines, G.L., Neidle, E.L. J. Bacteriol. (1998) [Pubmed]
  14. Proteomic analysis of the benzoate degradation pathway in Acinetobacter sp. KS-1. Kim, S.I., Song, S.Y., Kim, K.W., Ho, E.M., Oh, K.H. Res. Microbiol. (2003) [Pubmed]
  15. Structural roles of the active site iron(III) ions in catechol 1,2-dioxygenases and differential secondary structure changes in isoenzymes A and B from Acinetobacter radioresistens S13. Di Nardo, G., Tilli, S., Pessione, E., Cavaletto, M., Giunta, C., Briganti, F. Arch. Biochem. Biophys. (2004) [Pubmed]
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