| pubmed-article:10362535 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10362535 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:10362535 | lifeskim:mentions | umls-concept:C0014942 | lld:lifeskim |
| pubmed-article:10362535 | lifeskim:mentions | umls-concept:C0027303 | lld:lifeskim |
| pubmed-article:10362535 | lifeskim:mentions | umls-concept:C0301630 | lld:lifeskim |
| pubmed-article:10362535 | lifeskim:mentions | umls-concept:C0046725 | lld:lifeskim |
| pubmed-article:10362535 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:10362535 | lifeskim:mentions | umls-concept:C0720298 | lld:lifeskim |
| pubmed-article:10362535 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:10362535 | pubmed:dateCreated | 1999-6-28 | lld:pubmed |
| pubmed-article:10362535 | pubmed:abstractText | Human estrogenic 17beta-hydroxysteroid dehydrogenase (17beta-HSD1) plays a crucial role in the last step of the synthesis of estrogens. A detailed kinetic study demonstrated that the enzyme shows about 240 fold higher specificity towards estrone reduction than estradiol oxidation at physiological pH using tri-phosphate cofactors. The kcat/Km values are 96 +/- 10 and 0.4 +/- 0.1 s-1 (microM)-1 respectively for the above two reactions. However, it has been shown that this difference is closely linked to the use of NADPH and NADP cofactors. A binding study using equilibrium dialysis indicated similar KD (equilibrium dissociation constant) of 11 +/- 1 and 4.7 +/- 0.9 microM for estrone and estradiol, respectively. The binding affinity of 17beta-HSD1 to estrone was significantly increased with a KD of 1.6 +/- 0.2 microM in the presence of NADP, the latter used as an analogue of the NADPH. The results of binding studies agree with the steady-state kinetics, which showed that the Km of estrone is 12-fold lower when using NADPH as a cofactor than when using NADH. These results strongly suggest that the cofactor plays a crucial role in the stimulation of the specificity for estrogen reduction. | lld:pubmed |
| pubmed-article:10362535 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10362535 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10362535 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10362535 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10362535 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10362535 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10362535 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10362535 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10362535 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10362535 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10362535 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:10362535 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:10362535 | pubmed:author | pubmed-author:ChuP KPK | lld:pubmed |
| pubmed-article:10362535 | pubmed:author | pubmed-author:LimS WSW | lld:pubmed |
| pubmed-article:10362535 | pubmed:copyrightInfo | Copyright 1999 Academic Press. | lld:pubmed |
| pubmed-article:10362535 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10362535 | pubmed:day | 7 | lld:pubmed |
| pubmed-article:10362535 | pubmed:volume | 259 | lld:pubmed |
| pubmed-article:10362535 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10362535 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10362535 | pubmed:pagination | 489-93 | lld:pubmed |
| pubmed-article:10362535 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:10362535 | pubmed:meshHeading | pubmed-meshheading:10362535... | lld:pubmed |
| pubmed-article:10362535 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10362535 | pubmed:articleTitle | Human estrogenic 17beta-hydroxysteroid dehydrogenase: predominance of estrone reduction and its induction by NADPH. | lld:pubmed |
| pubmed-article:10362535 | pubmed:affiliation | CHUL Research Center, Laval University, Quebec, Quebec, G1V 4G2, Canada. | lld:pubmed |
| pubmed-article:10362535 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10362535 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10362535 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10362535 | lld:pubmed |
