Inhibition of peptidoglycan synthesis in ether-permeabilized Escherichia coli cells by structural analogs of D-alanyl-D-alanine.
Several analogs of D-alanyl-D-alanine have been proved to be competitive inhibitors of murein (cross-linked peptidoglycan) synthesis in either-permeabilized cells of Escherichia coli. Some analogs, distinguished from D-alanyl-D-alanine only by minor structural deviations, were incorporated into a murein-like sodium dodecyl sulfate-insoluble material in place of the natural substrate. These analogs therefore could be designated as competitive substrates of the cross-linked end product of murein synthesis. In contrast, others, even those containing bulky residues at the methyl group of the amino-terminal D-alanine, exhibited inhibition of murein synthesis. The last-mentioned group of analogs also inhibited a blank value which seems to be a characteristic feature of this system without added D-alanyl-D-alanine. From this data, a steady-state concentration of D-alanyl-D-alanine or D-alanine or both in growing cells of E. coli could be calculated as approximately 0.4 x 10(-3) M.
D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D004151:Dipeptides / Q000494:pharmacology*; D004926:Escherichia coli / Q000187:drug effects / Q000378:metabolism*; D004987:Ethers; D007700:Kinetics; D010457:Peptidoglycan / Q000096:biosynthesis*; D013329:Structure-Activity Relationship
D000900:Anti-Bacterial Agents; D004151:Dipeptides; D004987:Ethers; D010457:Peptidoglycan; C002956:alanylalanine