Inhibition of peptidoglycan synthesis in ether-permeabilized Escherichia coli cells by structural analogs of D-alanyl-D-alanine.

Antimicrobial Agents and Chemotherapy
H Pelzer, W Reuter

Abstract

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.

References

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Dec 1, 1973·Journal of Medicinal Chemistry·H Gershon, M W McNeil

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Citations

Dec 1, 1983·Archives of Microbiology·R MetzW P Hammes
Jan 1, 1981·Pharmacology & Therapeutics·F C Neuhaus, W P Hammes
Mar 1, 1982·Analytical Biochemistry·H Felix
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Nov 10, 2006·Journal of Biomolecular Screening·Ramesh K Jha, Sunita M de Sousa
May 11, 2016·Journal of Bacteriology·Takahiro ShimosakaHaruyuki Atomi
Jun 4, 2014·Journal of Bacteriology·Yu WangRobert H White
Dec 18, 2012·Journal of Bacteriology·Cheryl N MillerThomas H Kawula
Sep 1, 1982·Journal of Bacteriology·D Mengin-LecreulxJ van Heijenoort

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