Colicin M hydrolyses branched lipids II from Gram-positive bacteria.
Lipids II found in some Gram-positive bacteria were prepared in radioactive form from l-lysine-containing UDP-MurNAc-pentapeptide. The specific lateral chains of Enterococcus faecalis, Enterococcus faecium and Staphylococcus aureus (di-L-alanine, D-isoasparagine, and pentaglycine, respectively) were introduced by chemical peptide synthesis using the Fmoc chemistry. The branched nucleotides obtained were converted into the corresponding lipids II by enzymatic synthesis using the MraY and MurG enzymes. All of the lipids were hydrolysed by Escherichia coli colicin M at approximately the same rate as the meso-diaminopimelate-containing lipid II found in Gram-negative bacteria, thereby opening the way to the use of this enzyme as a broad spectrum antibacterial agent.
Univ Paris-Sud, Laboratoire des Enveloppes Bactériennes et Antibiotiques, UMR 8619, Orsay, F-91405, France.
Delphine
D
Patin
Hélène
H
Barreteau
Geneviève
G
Auger
Sophie
S
Magnet
Muriel
M
Crouvoisier
Ahmed
A
Bouhss
Thierry
T
Touzé
Michel
M
Arthur
Dominique
D
Mengin-Lecreulx
Didier
D
Blanot
D000215:Acylation; D000596:Amino Acids / Q000737:chemistry; D055162:Biocatalysis; D003087:Colicins / Q000737:chemistry*; D004952:Esters / Q000737:chemistry; D005449:Fluorenes / Q000737:chemistry; D006017:Glycolipids / Q000138:chemical synthesis / Q000737:chemistry*; D006020:Glycopeptides / Q000138:chemical synthesis / Q000737:chemistry*; D006094:Gram-Positive Bacteria; D006868:Hydrolysis; D013379:Substrate Specificity; D014538:Uridine Diphosphate N-Acetylmuramic Acid / Q000031:analogs & derivatives / Q000737:chemistry
D000596:Amino Acids; D003087:Colicins; D004952:Esters; D005449:Fluorenes; D006017:Glycolipids; D006020:Glycopeptides; C016456:N(alpha)-fluorenylmethyloxycarbonylamino acids; D014538:Uridine Diphosphate N-Acetylmuramic Acid; C010762:peptidoglycolipids; C002225:UDP-N-acetylmuramic acid pentapeptide