| http://purl.uniprot.org/citations/12220180 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12220180 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12220180 | http://www.w3.org/2000/01/rdf-schema#comment | "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 C=O, which in turn interacts with the positive pole of an alpha-helix macrodipole. In this paper we report the results from spectral, mutagenesis, and kinetic studies which show (1) that substrate activation involves restricted thioester C=O conformational freedom and a modest enhancement of C=O 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 10(4), consistent with its proposed role of general base or nucleophile."xsd:string |
| http://purl.uniprot.org/citations/12220180 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi0262303"xsd:string |
| http://purl.uniprot.org/citations/12220180 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi0262303"xsd:string |
| http://purl.uniprot.org/citations/12220180 | http://purl.uniprot.org/core/author | "Dong J."xsd:string |
| http://purl.uniprot.org/citations/12220180 | http://purl.uniprot.org/core/author | "Dong J."xsd:string |
| http://purl.uniprot.org/citations/12220180 | http://purl.uniprot.org/core/author | "Archambault A."xsd:string |
| http://purl.uniprot.org/citations/12220180 | http://purl.uniprot.org/core/author | "Archambault A."xsd:string |
| http://purl.uniprot.org/citations/12220180 | http://purl.uniprot.org/core/author | "Carey P.R."xsd:string |
| http://purl.uniprot.org/citations/12220180 | http://purl.uniprot.org/core/author | "Carey P.R."xsd:string |
| http://purl.uniprot.org/citations/12220180 | http://purl.uniprot.org/core/author | "Dunaway-Mariano D."xsd:string |
| http://purl.uniprot.org/citations/12220180 | http://purl.uniprot.org/core/author | "Dunaway-Mariano D."xsd:string |
| http://purl.uniprot.org/citations/12220180 | http://purl.uniprot.org/core/author | "Song F."xsd:string |
| http://purl.uniprot.org/citations/12220180 | http://purl.uniprot.org/core/author | "Song F."xsd:string |
| http://purl.uniprot.org/citations/12220180 | http://purl.uniprot.org/core/author | "Taylor K."xsd:string |
| http://purl.uniprot.org/citations/12220180 | http://purl.uniprot.org/core/author | "Taylor K."xsd:string |
| http://purl.uniprot.org/citations/12220180 | http://purl.uniprot.org/core/author | "Zhang W."xsd:string |
| http://purl.uniprot.org/citations/12220180 | http://purl.uniprot.org/core/author | "Zhang W."xsd:string |
| http://purl.uniprot.org/citations/12220180 | http://purl.uniprot.org/core/author | "Zhuang Z."xsd:string |
| http://purl.uniprot.org/citations/12220180 | http://purl.uniprot.org/core/author | "Zhuang Z."xsd:string |
| http://purl.uniprot.org/citations/12220180 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/12220180 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/12220180 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/12220180 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |