| pubmed-article:15544342 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15544342 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:15544342 | lifeskim:mentions | umls-concept:C0010762 | lld:lifeskim |
| pubmed-article:15544342 | lifeskim:mentions | umls-concept:C1136012 | lld:lifeskim |
| pubmed-article:15544342 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
| pubmed-article:15544342 | lifeskim:mentions | umls-concept:C0534137 | lld:lifeskim |
| pubmed-article:15544342 | lifeskim:mentions | umls-concept:C0450442 | lld:lifeskim |
| pubmed-article:15544342 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:15544342 | pubmed:issue | 46 | lld:pubmed |
| pubmed-article:15544342 | pubmed:dateCreated | 2004-11-16 | lld:pubmed |
| pubmed-article:15544342 | pubmed:abstractText | The epothilones are a new class of highly promising anticancer agents with a mode of action akin to that of paclitaxel but with distinct advantages over that drug. The principal natural compounds are epothilones A and B, which have an epoxide in the macrocyclic lactone ring, and C and D, which have a double bond instead of the epoxide group. The epoxidation of epothilones C and D to A and B, respectively, is mediated by EpoK, a cytochrome P450 enzyme encoded in the epothilone gene cluster. Here we report high-yield expression of EpoK, characterization of the protein, demonstration that the natural substrate can prevent-and even reverse-denaturation of the protein, identification of ligands and surrogate substrates, development of a high-throughput fluorescence activity assay based on the H(2)O(2)-dependent oxidation of 7-ethoxy-4-trifluoromethylcoumarin, and identification of effective inhibitors of the enzyme. These results will facilitate improvements in the yields of epothilones C and D and the engineering of EpoK to prepare novel epothilone analogues. Furthermore, the finding that the denatured enzyme is rescued by the substrate offers a potential paradigm for control of the P450 catalytic function. | lld:pubmed |
| pubmed-article:15544342 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15544342 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15544342 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15544342 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15544342 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15544342 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15544342 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15544342 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15544342 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15544342 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15544342 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15544342 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15544342 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15544342 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15544342 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15544342 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15544342 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15544342 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15544342 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15544342 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15544342 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:15544342 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:15544342 | pubmed:author | pubmed-author:Ortiz de... | lld:pubmed |
| pubmed-article:15544342 | pubmed:author | pubmed-author:OguraHiroshiH | lld:pubmed |
| pubmed-article:15544342 | pubmed:author | pubmed-author:NishidaClinto... | lld:pubmed |
| pubmed-article:15544342 | pubmed:author | pubmed-author:DawsonJohn... | lld:pubmed |
| pubmed-article:15544342 | pubmed:author | pubmed-author:PereraRoshanR | lld:pubmed |
| pubmed-article:15544342 | pubmed:author | pubmed-author:HochUte RUR | lld:pubmed |
| pubmed-article:15544342 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15544342 | pubmed:day | 23 | lld:pubmed |
| pubmed-article:15544342 | pubmed:volume | 43 | lld:pubmed |
| pubmed-article:15544342 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15544342 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15544342 | pubmed:pagination | 14712-21 | lld:pubmed |
| pubmed-article:15544342 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:15544342 | pubmed:meshHeading | pubmed-meshheading:15544342... | lld:pubmed |
| pubmed-article:15544342 | pubmed:meshHeading | pubmed-meshheading:15544342... | lld:pubmed |
| pubmed-article:15544342 | pubmed:meshHeading | pubmed-meshheading:15544342... | lld:pubmed |
| pubmed-article:15544342 | pubmed:meshHeading | pubmed-meshheading:15544342... | lld:pubmed |
| pubmed-article:15544342 | pubmed:meshHeading | pubmed-meshheading:15544342... | lld:pubmed |
| pubmed-article:15544342 | pubmed:meshHeading | pubmed-meshheading:15544342... | lld:pubmed |
| pubmed-article:15544342 | pubmed:meshHeading | pubmed-meshheading:15544342... | lld:pubmed |
| pubmed-article:15544342 | pubmed:meshHeading | pubmed-meshheading:15544342... | lld:pubmed |
| pubmed-article:15544342 | pubmed:meshHeading | pubmed-meshheading:15544342... | lld:pubmed |
| pubmed-article:15544342 | pubmed:meshHeading | pubmed-meshheading:15544342... | lld:pubmed |
| pubmed-article:15544342 | pubmed:meshHeading | pubmed-meshheading:15544342... | lld:pubmed |
| pubmed-article:15544342 | pubmed:meshHeading | pubmed-meshheading:15544342... | lld:pubmed |
| pubmed-article:15544342 | pubmed:meshHeading | pubmed-meshheading:15544342... | lld:pubmed |
| pubmed-article:15544342 | pubmed:meshHeading | pubmed-meshheading:15544342... | lld:pubmed |
| pubmed-article:15544342 | pubmed:meshHeading | pubmed-meshheading:15544342... | lld:pubmed |
| pubmed-article:15544342 | pubmed:meshHeading | pubmed-meshheading:15544342... | lld:pubmed |
| pubmed-article:15544342 | pubmed:meshHeading | pubmed-meshheading:15544342... | lld:pubmed |
| pubmed-article:15544342 | pubmed:meshHeading | pubmed-meshheading:15544342... | lld:pubmed |
| pubmed-article:15544342 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15544342 | pubmed:articleTitle | EpoK, a cytochrome P450 involved in biosynthesis of the anticancer agents epothilones A and B. Substrate-mediated rescue of a P450 enzyme. | lld:pubmed |
| pubmed-article:15544342 | pubmed:affiliation | Department of Pharmaceutical Chemistry, University of California, 600 16th Street, San Francisco, California 94143-2280, USA. | lld:pubmed |
| pubmed-article:15544342 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15544342 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15544342 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15544342 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15544342 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15544342 | lld:pubmed |
