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 Moonen, M. J. H.
Right arrow Articles by van Berkel, W. J. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Moonen, M. J. H.
Right arrow Articles by van Berkel, W. J. H.

 Previous Article  |  Next Article 

Journal of Bacteriology, August 2008, p. 5190-5198, Vol. 190, No. 15
0021-9193/08/$08.00+0     doi:10.1128/JB.01944-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Elucidation of the 4-Hydroxyacetophenone Catabolic Pathway in Pseudomonas fluorescens ACB{triangledown}

Mariëlle J. H. Moonen,1 Nanne M. Kamerbeek,2 Adrie H. Westphal,1 Sjef A. Boeren,1 Dick B. Janssen,2 Marco W. Fraaije,2 and Willem J. H. van Berkel1*

Laboratory of Biochemistry, Wageningen University, Dreijenlaan 3, 6703 HA Wageningen, The Netherlands,1 Laboratory of Biochemistry, Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands2

Received 14 December 2007/ Accepted 16 May 2008

The catabolism of 4-hydroxyacetophenone in Pseudomonas fluorescens ACB is known to proceed through the intermediate formation of hydroquinone. Here, we provide evidence that hydroquinone is further degraded through 4-hydroxymuconic semialdehyde and maleylacetate to β-ketoadipate. The P. fluorescens ACB genes involved in 4-hydroxyacetophenone utilization were cloned and characterized. Sequence analysis of a 15-kb DNA fragment showed the presence of 14 open reading frames containing a gene cluster (hapCDEFGHIBA) of which at least four encoded enzymes are involved in 4-hydroxyacetophenone degradation: 4-hydroxyacetophenone monooxygenase (hapA), 4-hydroxyphenyl acetate hydrolase (hapB), 4-hydroxymuconic semialdehyde dehydrogenase (hapE), and maleylacetate reductase (hapF). In between hapF and hapB, three genes encoding a putative intradiol dioxygenase (hapG), a protein of the Yci1 family (hapH), and a [2Fe-2S] ferredoxin (hapI) were found. Downstream of the hap genes, five open reading frames are situated encoding three putative regulatory proteins (orf10, orf12, and orf13) and two proteins possibly involved in a membrane efflux pump (orf11 and orf14). Upstream of hapE, two genes (hapC and hapD) were present that showed weak similarity with several iron(II)-dependent extradiol dioxygenases. Based on these findings and additional biochemical evidence, it is proposed that the hapC and hapD gene products are involved in the ring cleavage of hydroquinone.

* Corresponding author. Mailing address: Laboratory of Biochemistry, Wageningen University, Dreijenlaan 3, 6703 HA Wageningen, The Netherlands. Phone: 31 317 482861. Fax: 31 317 484801. E-mail: willem.vanberkel{at}wur.nl

{triangledown} Published ahead of print on 23 May 2008.

Journal of Bacteriology, August 2008, p. 5190-5198, Vol. 190, No. 15
0021-9193/08/$08.00+0     doi:10.1128/JB.01944-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Perez-Pantoja, D., Donoso, R. A., Sanchez, M. A., Gonzalez, B. (2009). Genuine genetic redundancy in maleylacetate-reductase-encoding genes involved in degradation of haloaromatic compounds by Cupriavidus necator JMP134. Microbiology 155: 3641-3651 [Abstract] [Full Text]  
  • Rehdorf, J., Zimmer, C. L., Bornscheuer, U. T. (2009). Cloning, Expression, Characterization, and Biocatalytic Investigation of the 4-Hydroxyacetophenone Monooxygenase from Pseudomonas putida JD1. Appl. Environ. Microbiol. 75: 3106-3114 [Abstract] [Full Text]  
  • Zhang, J.-J., Liu, H., Xiao, Y., Zhang, X.-E., Zhou, N.-Y. (2009). Identification and Characterization of Catabolic para-Nitrophenol 4-Monooxygenase and para-Benzoquinone Reductase from Pseudomonas sp. Strain WBC-3. J. Bacteriol. 191: 2703-2710 [Abstract] [Full Text]  
  • Moonen, M. J. H., Synowsky, S. A., van den Berg, W. A. M., Westphal, A. H., Heck, A. J. R., van den Heuvel, R. H. H., Fraaije, M. W., van Berkel, W. J. H. (2008). Hydroquinone Dioxygenase from Pseudomonas fluorescens ACB: a Novel Member of the Family of Nonheme-Iron(II)-Dependent Dioxygenases. J. Bacteriol. 190: 5199-5209 [Abstract] [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»