| http://purl.uniprot.org/citations/16837570 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16837570 | http://www.w3.org/2000/01/rdf-schema#comment | "Hydrolase activity from human liver and small intestine microsomes was compared with that of recombinant human carboxylesterases, hCE-1 and hCE-2. Although both hCE-1 and hCE-2 are present in human liver, the dominant component was found to be hCE-1, whereas the hydrolase activity of the human small intestine was found to be predominantly hCE-2. hCE-2 has a limited ability to hydrolyze large acyl compound substrates. Interestingly, propranolol derivatives, good substrates for hCE-2, were easily hydrolyzed by substitution of the methyl group on the 2-position of the acyl moiety, but were barely hydrolyzed when the methyl group was substituted on the 3-position. These findings suggest that hCE-2 does not easily form acylated intermediates because of conformational interference in its active site. In contrast, hCE-1 could hydrolyze a variety of substrates. The hydrolytic activity of hCE-2 increased with increasing alcohol chain length in benzoic acid derivative substrates, whereas hCE-1 preferentially catalyzed the hydrolysis of substrates with short alcohol chains. Kinetic data showed that the determining factor for the rate of hydrolysis of p-aminobenzoic acid esters was V(max) for hCE-1 and K(m) for hCE-2. Furthermore, the addition of hydrophobic alcohols to the reaction mixture with p-aminobenzoic acid propyl ester induced high and low levels of transesterification by hCE-1 and hCE-2, respectively. When considering the substrate specificities of hCE-1, it is necessary to consider the transesterification ability of hCE-1, in addition to the binding structure of the substrate in the active site of the enzyme."xsd:string |
| http://purl.uniprot.org/citations/16837570 | http://purl.org/dc/terms/identifier | "doi:10.1124/dmd.106.009381"xsd:string |
| http://purl.uniprot.org/citations/16837570 | http://purl.uniprot.org/core/author | "Imai T."xsd:string |
| http://purl.uniprot.org/citations/16837570 | http://purl.uniprot.org/core/author | "Hosokawa M."xsd:string |
| http://purl.uniprot.org/citations/16837570 | http://purl.uniprot.org/core/author | "Chiba K."xsd:string |
| http://purl.uniprot.org/citations/16837570 | http://purl.uniprot.org/core/author | "Taketani M."xsd:string |
| http://purl.uniprot.org/citations/16837570 | http://purl.uniprot.org/core/author | "Shii M."xsd:string |
| http://purl.uniprot.org/citations/16837570 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16837570 | http://purl.uniprot.org/core/name | "Drug Metab Dispos"xsd:string |
| http://purl.uniprot.org/citations/16837570 | http://purl.uniprot.org/core/pages | "1734-1741"xsd:string |
| http://purl.uniprot.org/citations/16837570 | http://purl.uniprot.org/core/title | "Substrate specificity of carboxylesterase isozymes and their contribution to hydrolase activity in human liver and small intestine."xsd:string |
| http://purl.uniprot.org/citations/16837570 | http://purl.uniprot.org/core/volume | "34"xsd:string |
| http://purl.uniprot.org/citations/16837570 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16837570 |
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| http://purl.uniprot.org/uniprot/P23141 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/16837570 |