PMID:8807054
| Citation |
Brandish, PE, Kimura, KI, Inukai, M, Southgate, R, Lonsdale, JT and Bugg, TD (1996) Modes of action of tunicamycin, liposidomycin B, and mureidomycin A: inhibition of phospho-N-acetylmuramyl-pentapeptide translocase from Escherichia coli. Antimicrob. Agents Chemother. 40:1640-4 |
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| Abstract |
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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| Keywords |
Aminoglycosides; Anti-Bacterial Agents/pharmacology; Bacterial Proteins/antagonists & inhibitors; Bacterial Proteins/metabolism; Binding, Competitive; Enzyme Inhibitors/pharmacology; Escherichia coli/drug effects; Escherichia coli/enzymology; Kinetics; Nucleosides/pharmacology; Transferases (Other Substituted Phosphate Groups)/antagonists & inhibitors; Transferases (Other Substituted Phosphate Groups)/metabolism; Tunicamycin/pharmacology |
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