期刊
JOURNAL OF BACTERIOLOGY
卷 186, 期 2, 页码 393-399出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.186.2.393-399.2004
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资金
- NIGMS NIH HHS [R01 GM028688, GM28688] Funding Source: Medline
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM028688] Funding Source: NIH RePORTER
In this study, we have shown that recombinant BH1999 from Bacillus halodurans catalyzes the hydrolysis of gentisyl coenzyme A (CoA) (2,5-dihydroxybenzoyi-coenzyme A) at physiological pH with a k(cat)/K-m of 1.6 x 10(6) M-1 s(-1) and the hydrolysis of 3-hydroxybenzoyl-CoA with a k(cat)/K-m of 3.0 x 10(5) 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-hydroxybenzoyi-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.
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