| pubmed-article:16837570 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16837570 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:16837570 | lifeskim:mentions | umls-concept:C0021852 | lld:lifeskim |
| pubmed-article:16837570 | lifeskim:mentions | umls-concept:C0023884 | lld:lifeskim |
| pubmed-article:16837570 | lifeskim:mentions | umls-concept:C0022173 | lld:lifeskim |
| pubmed-article:16837570 | lifeskim:mentions | umls-concept:C0054741 | lld:lifeskim |
| pubmed-article:16837570 | lifeskim:mentions | umls-concept:C0038592 | lld:lifeskim |
| pubmed-article:16837570 | lifeskim:mentions | umls-concept:C1149632 | lld:lifeskim |
| pubmed-article:16837570 | lifeskim:mentions | umls-concept:C1880177 | lld:lifeskim |
| pubmed-article:16837570 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:16837570 | pubmed:dateCreated | 2006-9-21 | lld:pubmed |
| pubmed-article:16837570 | pubmed:abstractText | 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. | lld:pubmed |
| pubmed-article:16837570 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16837570 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16837570 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16837570 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16837570 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16837570 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:16837570 | pubmed:issn | 0090-9556 | lld:pubmed |
| pubmed-article:16837570 | pubmed:author | pubmed-author:ImaiTerukoT | lld:pubmed |
| pubmed-article:16837570 | pubmed:author | pubmed-author:ChibaKanK | lld:pubmed |
| pubmed-article:16837570 | pubmed:author | pubmed-author:HosokawaMasak... | lld:pubmed |
| pubmed-article:16837570 | pubmed:author | pubmed-author:TaketaniMegum... | lld:pubmed |
| pubmed-article:16837570 | pubmed:author | pubmed-author:ShiiMayumiM | lld:pubmed |
| pubmed-article:16837570 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16837570 | pubmed:volume | 34 | lld:pubmed |
| pubmed-article:16837570 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16837570 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16837570 | pubmed:pagination | 1734-41 | lld:pubmed |
| pubmed-article:16837570 | pubmed:dateRevised | 2010-5-20 | lld:pubmed |
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| pubmed-article:16837570 | pubmed:meshHeading | pubmed-meshheading:16837570... | lld:pubmed |
| pubmed-article:16837570 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16837570 | pubmed:articleTitle | Substrate specificity of carboxylesterase isozymes and their contribution to hydrolase activity in human liver and small intestine. | lld:pubmed |
| pubmed-article:16837570 | pubmed:affiliation | Graduate School of Pharmaceutical Sciences, Kumamoto University, 5-1 Oe-Honmachi, Kumamoto 862-0973, Japan. iteruko@gpo.kumamoto-u.ac.jp | lld:pubmed |
| pubmed-article:16837570 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16837570 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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