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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1993-4-23
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pubmed:abstractText |
A series of natural and unnatural stereoisomers of reduced folate coenzymes have been studied for their capacity to facilitate binding of 5-fluoro-2'-dUMP (FdUMP) to bacterial thymidylate synthase (TS). The natural cosubstrate for the enzyme, (6R)-5,10-methylene-tetrahydrofolate (CH2-H4-folate), was 4-fold more potent than the unnatural 6S-form in promoting FdUMP binding to TS, but in a racemic mixture the effect of the 6R-form was not affected by the 6S-form. FdUMP binding to TS was also stimulated by tetrahydrofolate and dihydrofolate (85% and 30% as compared to (6RS)-CH2-H4-folate, respectively), but not by the stereoisomers of 5-methyl-tetrahydrofolate and 5-formyl-tetrahydrofolate (leucovorin). These results suggest that folates, which are not a natural cosubstrate for TS, have an additional role in facilitating FdUMP binding to TS.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0006-2952
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
45
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1177-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading | |
pubmed:year |
1993
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pubmed:articleTitle |
Effect of folate diastereoisomers on the binding of 5-fluoro-2'-deoxyuridine-5'-monophosphate to thymidylate synthase.
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pubmed:affiliation |
Department of Oncology, Free University Hospital, Amsterdam, The Netherlands.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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