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- W2101295502 abstract "4-Hydroxybenzoyl-coenzyme A (4-HBA-CoA) thioesterase catalyzes the hydrolysis of 4-HBA-CoA to 4-hydroxybenzoate and CoA. X-ray crystallographic analysis of the liganded enzyme has shown that the benzoyl thioester and pantetheine moieties of the substrate ligand are bound in a narrow crevice while the nucleotide moiety rests on the protein surface (Thoden, J. B., Holden, H. M., Zhuang, Z. and Dunaway-Mariano, D. (2002) X-ray Crystallographic Analyses of Inhibitor and Substrate Complexes of Wild-type and Mutant 4-Hydroxybenzoyl-CoA Thioesterase, J. Biol. Chem., in press). Asp17 is positioned in the crevice, close to the substrate thioester CO, which in turn interacts with the positive pole of an α-helix macrodipole. In this paper we report the results from spectral, mutagenesis, and kinetic studies which show (1) that substrate activation involves restricted thioester CO conformational freedom and a modest enhancement of CO bond polarization, (2) that the nucleotide unit of the substrate is bound through interaction with the protein surface, and (3) that Asp17 contributes a rate factor of 104, consistent with its proposed role of general base or nucleophile." @default.
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- W2101295502 date "2002-08-22" @default.
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- W2101295502 title "Kinetic, Raman, NMR, and Site-Directed Mutagenesis Studies of the <i>Pseudomonas</i> Sp. Strain CBS3 4-Hydroxybenzoyl-CoA Thioesterase Active Site" @default.
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- W2101295502 doi "https://doi.org/10.1021/bi0262303" @default.
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