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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
1996-11-22
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pubmed:abstractText |
Using a continuous fluorescence-based enzyme assay, we have characterized the antibacterial agents tumicamycin and liposidomycin B as inhibitors of solubilized Escherichia coli phospho-N-acetylmuramyl-pentapeptide translocase. Tunicamycin exhibited reversible inhibition (Ki = 0.55 +/- 0.1 microM) which was noncompetitive with respect to the lipid acceptor substrate and competitive with respect to the fluorescent substrate analog, dansyl-UDPMurNAc-pentapeptide. Liposidomycin B exhibited slow-binding inhibition (Ki = 80 +/- 15 nM) which was competitive with respect to the lipid acceptor substrate and noncompetitive with respect to dansyl-UDPMurNAc-pentapeptide. These results provide insight into the molecular mechanisms of action of these two classes of nucleoside antibiotics.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8807054-106855,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8807054-1436736,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8807054-1509257,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8807054-1902646,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8807054-2464586,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8807054-2498273,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8807054-2498275,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8807054-3843705,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8807054-4077739,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8807054-444447,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8807054-5231417,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8807054-5781013,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8807054-5938956,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8807054-8146133,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8807054-8517724,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8807054-8631795
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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 |
Jul
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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 |
40
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1640-4
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:8807054-Aminoglycosides,
pubmed-meshheading:8807054-Anti-Bacterial Agents,
pubmed-meshheading:8807054-Bacterial Proteins,
pubmed-meshheading:8807054-Binding, Competitive,
pubmed-meshheading:8807054-Enzyme Inhibitors,
pubmed-meshheading:8807054-Escherichia coli,
pubmed-meshheading:8807054-Kinetics,
pubmed-meshheading:8807054-Nucleosides,
pubmed-meshheading:8807054-Transferases (Other Substituted Phosphate Groups),
pubmed-meshheading:8807054-Tunicamycin
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pubmed:year |
1996
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pubmed:articleTitle |
Modes of action of tunicamycin, liposidomycin B, and mureidomycin A: inhibition of phospho-N-acetylmuramyl-pentapeptide translocase from Escherichia coli.
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pubmed:affiliation |
Department of Chemistry, University of Southampton, Highfield, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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