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Applied and Environmental Microbiology, May 2003, p. 2707-2711, Vol. 69, No. 5
0099-2240/03/$08.00+0     DOI: 10.1128/AEM.69.5.2707-2711.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Characterization of the 4-Hydroxybenzoyl-Coenzyme A Thioesterase from Arthrobacter sp. Strain SU

Zhihao Zhuang,1 Karl-Heinz Gartemann,2 Rudolf Eichenlaub,2 and Debra Dunaway-Mariano1*

Department of Chemistry, University of New Mexico, Albuquerque, New Mexico 87131,1 Department of Microbiology/Gene Technology, University of Bielefeld, 33615 Bielefeld, Germany2

Received 13 December 2002/ Accepted 20 February 2003

The Arthrobacter sp. strain SU 4-chlorobenzoate (4-CBA) dehalogenation pathway converts 4-CBA to 4-hydroxybenzoate (4-HBA). The pathway operon contains the genes fcbA, fcbB, and fcbC (A. Schmitz, K. H. Gartemann, J. Fiedler, E. Grund, and R. Eichenlaub, Appl. Environ. Microbiol. 58:4068-4071, 1992). Genes fcbA and fcbB encode 4-CBA-coenzyme A (CoA) ligase and 4-CBA-CoA dehalogenase, respectively, whereas the function of fcbC is not known. We subcloned fcbC and expressed it in Escherichia coli, and we purified and characterized the FcbC protein. A substrate activity screen identified benzoyl-CoA thioesters as the most active substrates. Catalysis of 4-HBA-CoA hydrolysis to 4-HBA and CoA occurred with a kcat of 6.7 s-1 and a Km of 1.2 µM. The kcat pH rate profile for 4-HBA-CoA hydrolysis indicated optimal activity over a pH range of 6 to 10. The amino acid sequence of the FcbC protein was compared to other sequences contained in the protein sequence data banks. A large number of sequence homologues of unknown function were identified. On the other hand, the 4-HBA-CoA thioesterases isolated from 4-CBA-degrading Pseudomonas strains did not share significant sequence identity with the FcbC protein, indicating early divergence of the thioesterase-encoding genes.

* Corresponding author. Mailing address: Department of Chemistry, University of New Mexico, Clark Hall 103, Albuquerque, NM 81713. Phone: (505) 277-3383. Fax: (505) 277-6202. E-mail: dd39{at}unm.edu.

Applied and Environmental Microbiology, May 2003, p. 2707-2711, Vol. 69, No. 5
0099-2240/03/$08.00+0     DOI: 10.1128/AEM.69.5.2707-2711.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Song, F., Zhuang, Z., Finci, L., Dunaway-Mariano, D., Kniewel, R., Buglino, J. A., Solorzano, V., Wu, J., Lima, C. D. (2006). Structure, Function, and Mechanism of the Phenylacetate Pathway Hot Dog-fold Thioesterase PaaI. J. Biol. Chem. 281: 11028-11038 [Abstract] [Full Text]  
  • Thoden, J. B., Zhuang, Z., Dunaway-Mariano, D., Holden, H. M. (2003). The Structure of 4-Hydroxybenzoyl-CoA Thioesterase from Arthrobacter sp. strain SU. J. Biol. Chem. 278: 43709-43716 [Abstract] [Full Text]  


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