Reference : Characterization of the bifunctional glycosyltransferase/acyltransferase penicillin-bind...
Scientific journals : Article
Life sciences : Microbiology
http://hdl.handle.net/2268/13121
Characterization of the bifunctional glycosyltransferase/acyltransferase penicillin-binding protein 4 of Listeria monocytogenes
English
Zawadzka-Skomial, J. [> > > >]
Markiewicz, Z. [> > > >]
Nguyen-Disteche, M. [> > > >]
Devreese, B. [> > > >]
Frère, Jean-Marie mailto [Université de Liège - ULg > Département des sciences de la vie > Département des sciences de la vie >]
Terrak, Mohammed mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Mar-2006
Journal of Bacteriology
Amer Soc Microbiology
188
5
1875-1881
Yes (verified by ORBi)
International
0021-9193
Washington
[en] Multimodular penicillin-binding proteins (PBPs) are essential enzymes responsible for bacterial cell wall peptidoglycan (PG) assembly. Their glycosyltransferase activity catalyzes glycan chain elongation from lipid II substrate (undecaprenyl-pyrophosphoryi-N-acetylglucosamine-N-acetylmuramic acid-pentapeptide), and their transpeptidase activity catalyzes cross-linking between peptides carried by two adjacent glycan chains. Listeria monocytogenes is a food-borne pathogen which exerts its virulence through secreted and cell wall PG-associated virulence factors. This bacterium has five PBPs, including two bifunctional glycosyltransferase/transpeptidase class A PBPs, namely, PBP1 and PBP4. We have expressed and purified the latter and have shown that it binds penicillin and catalyzes in vitro glycan chain polymerization with an efficiency of 1,400 M-1 s(-1) from Escherichia coli lipid II substrate. PBP4 also catalyzes the aminolysis (D-Ala as acceptor) and hydrolysis of the thiolester donor substrate benzoyl-Gly-thioglycolate, indicating that PBP4 possesses both transpeptidase and carboxyeptidase activities. Disruption of the gene lmo2229 encoding PBP4 in L. monocytogenes EGD did not. p have any significant effect on growth rate, peptidoglycan composition, cell morphology, or sensitivity to beta-lactam antibiotics but did increase the resistance of the mutant to moenomycin.
Researchers ; Professionals ; Students
http://hdl.handle.net/2268/13121
10.1128/JB.188.5.1875-1881.2006
http://www.pubmedcentral.nih.gov/picrender.fcgi?artid=1426562&blobtype=pdf

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