PMID:12426329
| Citation |
Cheng, Q and Park, JT (2002) Substrate specificity of the AmpG permease required for recycling of cell wall anhydro-muropeptides. J. Bacteriol. 184:6434-6 |
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| Abstract |
AmpG was originally identified as a gene required for induction of beta-lactamase. Subsequently, we found AmpG to be a permease required for recycling of murein tripeptide and uptake of anhydro-muropeptides. We have now studied the specificity of the AmpG permease. The principal requirement is for the presence of the disaccharide, N-acetylglucosaminyl-beta-1,4-anhydro-N-acetylmuramic acid (GlcNAc-anhMurNAc). These unique substrates for AmpG, which contain murein peptides linked to GlcNAc-anhMurNAc, are produced by turnover of the cell wall during logarithmic growth. AmpG permease is sensitive to carbonylcyanide m-chlorophenylhydrazone, demonstrating that AmpG permease is a single-component permease and that transport is dependent on the proton motive force. |
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| Keywords |
Bacterial Proteins/metabolism; Bacteriological Techniques; Cell Wall; Escherichia coli/enzymology; Escherichia coli/growth & development; Freezing; Glucosamine/metabolism; Membrane Proteins/metabolism; Membrane Transport Proteins; Muramic Acids/chemistry; Muramic Acids/metabolism; Peptides/metabolism; Peptidoglycan/metabolism; Substrate Specificity; Tritium/metabolism |
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