PMID:11257015
| Citation |
Apfel, CM, Evers, S, Hubschwerlen, C, Pirson, W, Page, MG and Keck, W (2001) Peptide deformylase as an antibacterial drug target: assays for detection of its inhibition in Escherichia coli cell homogenates and intact cells. Antimicrob. Agents Chemother. 45:1053-7 |
|---|---|
| Abstract |
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. |
| Links |
PubMed PMC90424 Online version:10.1128/AAC.45.4.1053-1057.2001 |
| Keywords |
Amidohydrolases; Aminopeptidases/antagonists & inhibitors; Anti-Bacterial Agents/pharmacology; Bacterial Proteins/drug effects; Cell Extracts/analysis; Enzyme Inhibitors/pharmacology; Escherichia coli/drug effects; Escherichia coli/enzymology; Methionine/metabolism; Microbial Sensitivity Tests/methods; Protein Biosynthesis/drug effects; Transcription, Genetic/drug effects |
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