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 Schühle, K.
Right arrow Articles by Fuchs, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Schühle, K.
Right arrow Articles by Fuchs, G.

 Previous Article  |  Next Article 

Journal of Bacteriology, September 2001, p. 5268-5278, Vol. 183, No. 18
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.18.5268-5278.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Two Similar Gene Clusters Coding for Enzymes of a New Type of Aerobic 2-Aminobenzoate (Anthranilate) Metabolism in the Bacterium Azoarcus evansii

Karola Schühle,1 Martina Jahn,1 Sandro Ghisla,2 and Georg Fuchs1,*

Mikrobiologie, Institut für Biologie II, Albert-Ludwigs-Universität Freiburg, Freiburg,1 and Fakultät Biologie, Universität Konstanz, Konstanz, Germany2

Received 16 April 2001/Accepted 18 June 2001

In the beta -proteobacterium Azoarcus evansii, the aerobic metabolism of 2-aminobenzoate (anthranilate), phenylacetate, and benzoate proceeds via three unprecedented pathways. The pathways have in common that all three substrates are initially activated to coenzyme A (CoA) thioesters and further processed in this form. The two initial steps of 2-aminobenzoate metabolism are catalyzed by a 2-aminobenzoate-CoA ligase forming 2-aminobenzoyl-CoA and by a 2-aminobenzoyl-CoA monooxygenase/reductase (ACMR) forming 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA. Eight genes possibly involved in this pathway, including the genes encoding 2-aminobenzoate-CoA ligase and ACMR, were detected, cloned, and sequenced. The sequence of the ACMR gene showed that this enzyme is an 87-kDa fusion protein of two flavoproteins, a monooxygenase (similar to salicylate monooxygenase) and a reductase (similar to old yellow enzyme). Besides the genes for the initial two enzymes, genes for three enzymes of a beta -oxidation pathway were found. A substrate binding protein of an ABC transport system, a MarR-like regulator, and a putative translation inhibitor protein were also encoded by the gene cluster. The data suggest that, after monooxygenation/reduction of 2-aminobenzoyl-CoA, the nonaromatic CoA thioester intermediate is metabolized further by beta -oxidation. This implies that all subsequent intermediates are CoA thioesters and that the alicyclic carbon ring is not cleaved oxygenolytically. Surprisingly, the cluster of eight genes, which form an operon, is duplicated. The two copies differ only marginally within the coding regions but differ substantially in the respective intergenic regions. Both copies of the genes are coordinately expressed in cells grown aerobically on 2-aminobenzoate.

* Corresponding author. Mailing address: Mikrobiologie, Institut für Biologie II, Universität Freiburg, Schänzlestr. 1, D-79104 Freiburg, Germany. Phone: 49-761-203-2649. Fax: 49-761-203-2626. E-mail: fuchsgeo{at}uni-freiburg.de.

Journal of Bacteriology, September 2001, p. 5268-5278, Vol. 183, No. 18
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.18.5268-5278.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Carmona, M., Zamarro, M. T., Blazquez, B., Durante-Rodriguez, G., Juarez, J. F., Valderrama, J. A., Barragan, M. J. L., Garcia, J. L., Diaz, E. (2009). Anaerobic Catabolism of Aromatic Compounds: a Genetic and Genomic View. Microbiol. Mol. Biol. Rev. 73: 71-133 [Abstract] [Full Text]  
  • Coleman, J. P., Hudson, L. L., McKnight, S. L., Farrow, J. M. III, Calfee, M. W., Lindsey, C. A., Pesci, E. C. (2008). Pseudomonas aeruginosa PqsA Is an Anthranilate-Coenzyme A Ligase. J. Bacteriol. 190: 1247-1255 [Abstract] [Full Text]  
  • Park, M., Jeon, Y., Jang, H. H., Ro, H.-S., Park, W., Madsen, E. L., Jeon, C. O. (2007). Molecular and Biochemical Characterization of 3-Hydroxybenzoate 6-Hydroxylase from Polaromonas naphthalenivorans CJ2. Appl. Environ. Microbiol. 73: 5146-5152 [Abstract] [Full Text]  
  • Parschat, K., Overhage, J., Strittmatter, A. W., Henne, A., Gottschalk, G., Fetzner, S. (2007). Complete Nucleotide Sequence of the 113-Kilobase Linear Catabolic Plasmid pAL1 of Arthrobacter nitroguajacolicus Ru61a and Transcriptional Analysis of Genes Involved in Quinaldine Degradation. J. Bacteriol. 189: 3855-3867 [Abstract] [Full Text]  
  • Huang, Y., Zhao, K.-X., Shen, X.-H., Chaudhry, M. T., Jiang, C.-Y., Liu, S.-J. (2006). Genetic Characterization of the Resorcinol Catabolic Pathway in Corynebacterium glutamicum. Appl. Environ. Microbiol. 72: 7238-7245 [Abstract] [Full Text]  
  • Gescher, J., Ismail, W., Olgeschlager, E., Eisenreich, W., Worth, J., Fuchs, G. (2006). Aerobic Benzoyl-Coenzyme A (CoA) Catabolic Pathway in Azoarcus evansii: Conversion of Ring Cleavage Product by 3,4-Dehydroadipyl-CoA Semialdehyde Dehydrogenase.. J. Bacteriol. 188: 2919-2927 [Abstract] [Full Text]  
  • Jeon, C. O., Park, M., Ro, H.-S., Park, W., Madsen, E. L. (2006). The Naphthalene Catabolic (nag) Genes of Polaromonas naphthalenivorans CJ2: Evolutionary Implications for Two Gene Clusters and Novel Regulatory Control. Appl. Environ. Microbiol. 72: 1086-1095 [Abstract] [Full Text]  
  • Barragan, M. J. L., Carmona, M., Zamarro, M. T., Thiele, B., Boll, M., Fuchs, G., Garcia, J. L., Diaz, E. (2004). The bzd Gene Cluster, Coding for Anaerobic Benzoate Catabolism, in Azoarcus sp. Strain CIB. J. Bacteriol. 186: 5762-5774 [Abstract] [Full Text]  
  • Ishiyama, D., Vujaklija, D., Davies, J. (2004). Novel Pathway of Salicylate Degradation by Streptomyces sp. Strain WA46. Appl. Environ. Microbiol. 70: 1297-1306 [Abstract] [Full Text]  
  • Shinoda, Y., Sakai, Y., Uenishi, H., Uchihashi, Y., Hiraishi, A., Yukawa, H., Yurimoto, H., Kato, N. (2004). Aerobic and Anaerobic Toluene Degradation by a Newly Isolated Denitrifying Bacterium, Thauera sp. Strain DNT-1. Appl. Environ. Microbiol. 70: 1385-1392 [Abstract] [Full Text]  
  • Schuhle, K., Gescher, J., Feil, U., Paul, M., Jahn, M., Schagger, H., Fuchs, G. (2003). Benzoate-Coenzyme A Ligase from Thauera aromatica: an Enzyme Acting in Anaerobic and Aerobic Pathways. J. Bacteriol. 185: 4920-4929 [Abstract] [Full Text]  
  • Gescher, J., Zaar, A., Mohamed, M., Schagger, H., Fuchs, G. (2002). Genes Coding for a New Pathway of Aerobic Benzoate Metabolism in Azoarcus evansii. J. Bacteriol. 184: 6301-6315 [Abstract] [Full Text]  
  • Williams, R. E., Bruce, N. C. (2002). 'New uses for an Old Enzyme' - the Old Yellow Enzyme family of flavoenzymes. Microbiology 148: 1607-1614 [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»