Reference : Characterization of the bifunctional glycosyltransferase/acyltransferase penicillin-b...
Scientific journals : Article
Life sciences : Microbiology
Characterization of the bifunctional glycosyltransferase/acyltransferase penicillin-binding protein 4 of Listeria monocytogenes
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 >]
Journal of Bacteriology
Amer Soc Microbiology
Yes (verified by ORBi)
[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

File(s) associated to this reference

Fulltext file(s):

Restricted access
PBP4 Lmg.pdfAuthor postprint204.91 kBRequest copy

Bookmark and Share SFX Query

All documents in ORBi are protected by a user license.