This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Mars, A. E.
Right arrow Articles by Janssen, D. B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mars, A. E.
Right arrow Articles by Janssen, D. B.

 Previous Article  |  Next Article 

Journal of Bacteriology, February 1999, p. 1309-1318, Vol. 181, No. 4
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Conversion of 3-Chlorocatechol by Various Catechol 2,3-Dioxygenases and Sequence Analysis of the Chlorocatechol Dioxygenase Region of Pseudomonas putida GJ31

Astrid E. Mars,1 Jaap Kingma,1 Stefan R. Kaschabek,2 Walter Reineke,2 and Dick B. Janssen1,*

Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9747 AG Groningen, The Netherlands,1 and Chemische Mikrobiologie, Bergische Universität---Gesamthochschule Wuppertal, D-42097 Wuppertal, Germany2

Received 20 July 1998/Accepted 3 December 1998

Pseudomonas putida GJ31 contains an unusual catechol 2,3-dioxygenase that converts 3-chlorocatechol and 3-methylcatechol, which enables the organism to use both chloroaromatics and methylaromatics for growth. A 3.1-kb region of genomic DNA of strain GJ31 containing the gene for this chlorocatechol 2,3-dioxygenase (cbzE) was cloned and sequenced. The cbzE gene appeared to be plasmid localized and was found in a region that also harbors genes encoding a transposase, a ferredoxin that was homologous to XylT, an open reading frame with similarity to a protein of a meta-cleavage pathway with unknown function, and a 2-hydroxymuconic semialdehyde dehydrogenase. CbzE was most similar to catechol 2,3-dioxygenases of the 2.C subfamily of type 1 extradiol dioxygenases (L. D. Eltis and J. T. Bolin, J. Bacteriol. 178:5930-5937, 1996). The substrate range and turnover capacity with 3-chlorocatechol were determined for CbzE and four related catechol 2,3-dioxygenases. The results showed that CbzE was the only enzyme that could productively convert 3-chlorocatechol. Besides, CbzE was less susceptible to inactivation by methylated catechols. Hybrid enzymes that were made of CzbE and the catechol 2,3-dioxygenase of P. putida UCC2 (TdnC) showed that the resistance of CbzE to suicide inactivation and its substrate specificity were mainly determined by the C-terminal region of the protein.


* Corresponding author. Mailing address: Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands. Phone: 31-503634008. Fax: 31-503634165. E-mail: D.B.Janssen{at}chem.rug.nl.


Journal of Bacteriology, February 1999, p. 1309-1318, Vol. 181, No. 4
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.



This article has been cited by other articles:

  • Liu, S., Ogawa, N., Senda, T., Hasebe, A., Miyashita, K. (2005). Amino Acids in Positions 48, 52, and 73 Differentiate the Substrate Specificities of the Highly Homologous Chlorocatechol 1,2-Dioxygenases CbnA and TcbC. J. Bacteriol. 187: 5427-5436 [Abstract] [Full Text]  
  • Okuta, A., Ohnishi, K., Harayama, S. (2004). Construction of Chimeric Catechol 2,3-Dioxygenase Exhibiting Improved Activity against the Suicide Inhibitor 4-Methylcatechol. Appl. Environ. Microbiol. 70: 1804-1810 [Abstract] [Full Text]  
  • Alfreider, A., Vogt, C., Babel, W. (2003). Expression of Chlorocatechol 1,2-Dioxygenase and Chlorocatechol 2,3-Dioxygenase Genes in Chlorobenzene-Contaminated Subsurface Samples. Appl. Environ. Microbiol. 69: 1372-1376 [Abstract] [Full Text]  
  • Dinkla, I. J. T., Gabor, E. M., Janssen, D. B. (2001). Effects of Iron Limitation on the Degradation of Toluene by Pseudomonas Strains Carrying the TOL (pWWO) Plasmid. Appl. Environ. Microbiol. 67: 3406-3412 [Abstract] [Full Text]  
  • Boon, N., Goris, J., De Vos, P., Verstraete, W., Top, E. M. (2000). Bioaugmentation of Activated Sludge by an Indigenous 3-Chloroaniline-Degrading Comamonas testosteroni Strain, I2gfp. Appl. Environ. Microbiol. 66: 2906-2913 [Abstract] [Full Text]  
  • Davis, J. K., Paoli, G. C., He, Z., Nadeau, L. J., Somerville, C. C., Spain, J. C. (2000). Sequence Analysis and Initial Characterization of Two Isozymes of Hydroxylaminobenzene Mutase from Pseudomonas pseudoalcaligenes JS45. Appl. Environ. Microbiol. 66: 2965-2971 [Abstract] [Full Text]  
  • Arai, H., Ohishi, T., Chang, M. Y., Kudo, T. (2000). Arrangement and regulation of the genes for meta-pathway enzymes required for degradation of phenol in Comamonas testosteroni TA441. Microbiology 146: 1707-1715 [Abstract] [Full Text]