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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2008-1-9
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pubmed:abstractText |
The mechanism of the C-methylation reaction was studied with the allylic substrate analog 24-fluorocycloartenol 10 assayed with soybean sterol C24-methyltransferase (SMT). 10 is an effective competitive inhibitor (Ki = 32 microM) of the SMT, and the electron-withdrawing alpha-fluorine substituent was shown to suppress the rate of the C-methylation reaction by one order of magnitude relative to the natural cycloartenol substrate, kcat = 0.02 min(-1) versus 0.6 min(-1); alternately 10 can prevent the critical hydride shift of H24 to C25 to afford time-dependent inactivation of SMT (k(inact) = 0.32 min(-1)).
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1464-3405
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
18
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
232-5
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pubmed:meshHeading |
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pubmed:year |
2008
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pubmed:articleTitle |
Sterol C24-methyltransferase: mechanistic studies of the C-methylation reaction with 24-fluorocycloartenol.
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pubmed:affiliation |
Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX 79409-1061, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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