Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1355369 | Bioorganic Chemistry | 2007 | 10 Pages |
In this study, the second-order rate constant k2 of base-catalyzed hydrolysis and the values of kcat, Km and kcat/Km of wild-type Pseudomonas sp. CBS3 4-hydroxybenzoyl coenzyme A (4-HBA-CoA) thioesterase-catalyzed hydrolysis of 4-HBA-CoA and its para-substituted analogs were measured. For the base-catalyzed hydrolysis, the plot of log k2 vs the σ value of the para-substituents was linear with a slope (ρ) of 1.5. In the case of the enzyme-catalyzed hydrolysis, the kcat/Km values measured for the para-substituted analogs defined substrate specificity. Asp32 was shown to play a key role in substrate recognition, and in particular, in the discrimination between the targeted substrate and other cellular benzoyl-CoA thioesters.
Graphical abstractThe base-catalyzed hydrolysis rate constant of benzoyl-CoAs with different para-substituents is depended upon the para-substituent σ value, while thioesterase-catalyzed hydrolysis rate constant is not.Figure optionsDownload full-size imageDownload as PowerPoint slide