| http://purl.uniprot.org/citations/14617621 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/14617621 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/14617621 | http://www.w3.org/2000/01/rdf-schema#comment | "The reaction mechanism of the esterase 2 (EST2) from Alicyclobacillus acidocaldarius was studied at the kinetic and structural level to shed light on the mechanism of activity and substrate specificity increase previously observed in its double mutant M211S/R215L. In particular, the values of kinetic constants (k1, k(-1), k2, and k3) along with activation energies (E1, E(-1), E2, and E3) were measured for wild type and mutant enzyme. The previously suggested substrate-induced switch in the reaction mechanism from kcat=k3 with a short acyl chain substrate (p-nitrophenyl hexanoate) to kcat=k2 with a long acyl chain substrate (p-nitrophenyl dodecanoate) was validated. The inhibition afforded by an irreversible inhibitor (1-hexadecanesulfonyl chloride), structurally related to p-nitrophenyl dodecanoate, was studied by kinetic analysis. Moreover the three-dimensional structure of the double mutant bound to this inhibitor was determined, providing essential information on the enzyme mechanism. In fact, structural analysis explained the observed substrate-induced switch because of an inversion in the binding mode of the long acyl chain derivatives with respect to the acyl- and alcohol-binding sites."xsd:string |
| http://purl.uniprot.org/citations/14617621 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.M307738200"xsd:string |
| http://purl.uniprot.org/citations/14617621 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m307738200"xsd:string |
| http://purl.uniprot.org/citations/14617621 | http://purl.uniprot.org/core/author | "Febbraio F."xsd:string |
| http://purl.uniprot.org/citations/14617621 | http://purl.uniprot.org/core/author | "Febbraio F."xsd:string |
| http://purl.uniprot.org/citations/14617621 | http://purl.uniprot.org/core/author | "Rossi M."xsd:string |
| http://purl.uniprot.org/citations/14617621 | http://purl.uniprot.org/core/author | "Rossi M."xsd:string |
| http://purl.uniprot.org/citations/14617621 | http://purl.uniprot.org/core/author | "Manco G."xsd:string |
| http://purl.uniprot.org/citations/14617621 | http://purl.uniprot.org/core/author | "Manco G."xsd:string |
| http://purl.uniprot.org/citations/14617621 | http://purl.uniprot.org/core/author | "Mandrich L."xsd:string |
| http://purl.uniprot.org/citations/14617621 | http://purl.uniprot.org/core/author | "Mandrich L."xsd:string |
| http://purl.uniprot.org/citations/14617621 | http://purl.uniprot.org/core/author | "De Simone G."xsd:string |
| http://purl.uniprot.org/citations/14617621 | http://purl.uniprot.org/core/author | "De Simone G."xsd:string |
| http://purl.uniprot.org/citations/14617621 | http://purl.uniprot.org/core/author | "Pedone C."xsd:string |
| http://purl.uniprot.org/citations/14617621 | http://purl.uniprot.org/core/author | "Pedone C."xsd:string |
| http://purl.uniprot.org/citations/14617621 | http://purl.uniprot.org/core/author | "Menchise V."xsd:string |
| http://purl.uniprot.org/citations/14617621 | http://purl.uniprot.org/core/author | "Menchise V."xsd:string |
| http://purl.uniprot.org/citations/14617621 | http://purl.uniprot.org/core/author | "Giordano V."xsd:string |
| http://purl.uniprot.org/citations/14617621 | http://purl.uniprot.org/core/author | "Giordano V."xsd:string |
| http://purl.uniprot.org/citations/14617621 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/14617621 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/14617621 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/14617621 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |