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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2001-3-21
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pubmed:abstractText |
An assay was developed to determine the activity of peptide deformylase (PDF) inhibitors under conditions as close as possible to the physiological situation. The assay principle is the detection of N-terminal [35S]methionine labeling of a protein that contains no internal methionine. If PDF is active, the deformylation of the methionine renders the peptide a substrate for methionine aminopeptidase, resulting in the removal of the N-terminal methionine label. In the presence of a PDF inhibitor, the deformylation is blocked so that the N-formylated peptide is not processed and the label is detected. Using this assay, it is possible to determine the PDF activity under near-physiological conditions in a cell-free transcription-translation system as well as in intact bacterial cells.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11257015-10395817,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11257015-10428776,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11257015-10882358,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11257015-11257016,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11257015-1624424,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11257015-2246265,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11257015-2544569,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11257015-4585977,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11257015-4973445,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11257015-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11257015-6546423,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11257015-7961514,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11257015-8112305,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11257015-8199241
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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 |
Apr
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pubmed:issn |
0066-4804
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pubmed:author |
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pubmed:issnType |
Print
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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 |
1053-7
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:11257015-Amidohydrolases,
pubmed-meshheading:11257015-Aminopeptidases,
pubmed-meshheading:11257015-Anti-Bacterial Agents,
pubmed-meshheading:11257015-Bacterial Proteins,
pubmed-meshheading:11257015-Cell Extracts,
pubmed-meshheading:11257015-Enzyme Inhibitors,
pubmed-meshheading:11257015-Escherichia coli,
pubmed-meshheading:11257015-Methionine,
pubmed-meshheading:11257015-Microbial Sensitivity Tests,
pubmed-meshheading:11257015-Protein Biosynthesis,
pubmed-meshheading:11257015-Transcription, Genetic
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pubmed:year |
2001
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pubmed:articleTitle |
Peptide deformylase as an antibacterial drug target: assays for detection of its inhibition in Escherichia coli cell homogenates and intact cells.
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pubmed:affiliation |
Pharma Research Basel, F. Hoffmann-La Roche Ltd., CH-4070 Basel, Switzerland. christian.apfel@roche.com
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pubmed:publicationType |
Journal Article
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