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Journal of Bacteriology, January 2004, p. 393-399, Vol. 186, No. 2
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.2.393-399.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

The BH1999 Protein of Bacillus halodurans C-125 Is Gentisyl-Coenzyme A Thioesterase

Zhihao Zhuang,1 Feng Song,1 Hideto Takami,2 and Debra Dunaway-Mariano1*

Department of Chemistry, University of New Mexico, Albuquerque, New Mexico 87131 ,1 Microbial Genome Research Group, Japan Marine Science and Technology Center, 2-15 Natsushima, Yokosuka, 237-0061 Japan2

Received 20 June 2003/ Accepted 10 October 2003

In this study, we have shown that recombinant BH1999 from Bacillus halodurans catalyzes the hydrolysis of gentisyl coenzyme A (CoA) (2,5-dihydroxybenzoyl-coenzyme A) at physiological pH with a kcat/Km of 1.6 x 106 M-1 s-1 and the hydrolysis of 3-hydroxybenzoyl-CoA with a kcat/Km of 3.0 x 105 M-1 s-1. All other acyl-CoA thioesters tested had low or no substrate activity. The BH1999 gene is juxtaposed with a gene cluster that contains genes believed to function in gentisate oxidative degradation. It is hypothesized that BH1999 functions as a gentisyl-CoA thioesterase. Gentisyl-CoA thioesterase shares the backbone fold and the use of an active site aspartate residue to mediate catalysis with the 4-hydroxybenzoyl-CoA thioesterase of the hotdog fold enzyme superfamily. A comparative study of these two enzymes showed that they differ greatly in the rate contribution made by the catalytic aspartate, in the pH dependence of catalysis, and in substrate specificity.

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

Journal of Bacteriology, January 2004, p. 393-399, Vol. 186, No. 2
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.2.393-399.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

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