| pubmed-article:12083921 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12083921 | lifeskim:mentions | umls-concept:C0079870 | lld:lifeskim |
| pubmed-article:12083921 | lifeskim:mentions | umls-concept:C0205681 | lld:lifeskim |
| pubmed-article:12083921 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
| pubmed-article:12083921 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:12083921 | lifeskim:mentions | umls-concept:C0060072 | lld:lifeskim |
| pubmed-article:12083921 | pubmed:issue | 26 | lld:pubmed |
| pubmed-article:12083921 | pubmed:dateCreated | 2002-6-26 | lld:pubmed |
| pubmed-article:12083921 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12083921 | pubmed:abstractText | Incubation of farnesyl diphosphate (1) with the W308F or W308F/H309F mutants of pentalenene synthase, an enzyme from Streptomyces UC5319, yielded pentalenene (2), accompanied by varying proportions of (+)-germacrene A (7) with relatively minor changes in k(cat) and k(cat)/K(m). By contrast, single H309 mutants gave rise to both (+)-germacrene A (7) and protoilludene (8) in addition to pentalenene (2). Mutation to glutamate of each of the three aspartate residues in the Mg(2+)-binding aspartate-rich domain, (80)DDLFD, resulted in reduction in the k(cat)/K(m) for farnesyl diphosphate and formation of varying proportions of pentalenene and (+)-germacrene A (7). Formation of (+)-germacrene A (7) by the various pentalenene synthase mutants is the result of a derailment of the natural anti-Markovnikov cyclization reaction, and not simply the consequence of trapping of a normally cryptic, carbocationic intermediate. Both the N219A and N219L mutants of pentalenene synthase were completely inactive, while the corresponding N219D mutant had a k(cat)/K(m) which was 3300-fold lower than that of the wild-type synthase, and produced a mixture of pentalenene (2) (91%) and the aberrant cyclization product beta-caryophyllene (9) (9%). Finally, the F77Y mutant had a k(cat)/K(m) which was reduced by 20-fold compared to that of the wild-type synthase. | lld:pubmed |
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| pubmed-article:12083921 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12083921 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12083921 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12083921 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12083921 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12083921 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:12083921 | pubmed:issn | 0002-7863 | lld:pubmed |
| pubmed-article:12083921 | pubmed:author | pubmed-author:CaneDavid EDE | lld:pubmed |
| pubmed-article:12083921 | pubmed:author | pubmed-author:ChristiansonD... | lld:pubmed |
| pubmed-article:12083921 | pubmed:author | pubmed-author:de... | lld:pubmed |
| pubmed-article:12083921 | pubmed:author | pubmed-author:SeemannMyriam... | lld:pubmed |
| pubmed-article:12083921 | pubmed:author | pubmed-author:ZhaiGuangzhiG | lld:pubmed |
| pubmed-article:12083921 | pubmed:author | pubmed-author:PaschallChian... | lld:pubmed |
| pubmed-article:12083921 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12083921 | pubmed:day | 3 | lld:pubmed |
| pubmed-article:12083921 | pubmed:volume | 124 | lld:pubmed |
| pubmed-article:12083921 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12083921 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12083921 | pubmed:pagination | 7681-9 | lld:pubmed |
| pubmed-article:12083921 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:12083921 | pubmed:meshHeading | pubmed-meshheading:12083921... | lld:pubmed |
| pubmed-article:12083921 | pubmed:meshHeading | pubmed-meshheading:12083921... | lld:pubmed |
| pubmed-article:12083921 | pubmed:meshHeading | pubmed-meshheading:12083921... | lld:pubmed |
| pubmed-article:12083921 | pubmed:meshHeading | pubmed-meshheading:12083921... | lld:pubmed |
| pubmed-article:12083921 | pubmed:meshHeading | pubmed-meshheading:12083921... | lld:pubmed |
| pubmed-article:12083921 | pubmed:meshHeading | pubmed-meshheading:12083921... | lld:pubmed |
| pubmed-article:12083921 | pubmed:meshHeading | pubmed-meshheading:12083921... | lld:pubmed |
| pubmed-article:12083921 | pubmed:meshHeading | pubmed-meshheading:12083921... | lld:pubmed |
| pubmed-article:12083921 | pubmed:meshHeading | pubmed-meshheading:12083921... | lld:pubmed |
| pubmed-article:12083921 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12083921 | pubmed:articleTitle | Pentalenene synthase. Analysis of active site residues by site-directed mutagenesis. | lld:pubmed |
| pubmed-article:12083921 | pubmed:affiliation | Department of Chemistry, Box H, Brown University, Providence, Rhode Island 02912-9108, USA. | lld:pubmed |
| pubmed-article:12083921 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12083921 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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