PMID:16484198
| Citation |
Zawadzka-Skomial, J, Markiewicz, Z, Nguyen-Distèche, M, Devreese, B, Frère, JM and Terrak, M (2006) Characterization of the bifunctional glycosyltransferase/acyltransferase penicillin-binding protein 4 of Listeria monocytogenes. J. Bacteriol. 188:1875-81 |
|---|---|
| Abstract |
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-pyrophosphoryl-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 carboxypeptidase activities. Disruption of the gene lmo2229 encoding PBP4 in L. monocytogenes EGD did not 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. |
| Links |
PubMed PMC1426562 Online version:10.1128/JB.188.5.1875-1881.2006 |
| Keywords |
Acyltransferases/metabolism; Amino Acid Sequence; Drug Resistance; Glycosyltransferases/metabolism; Listeria monocytogenes/drug effects; Listeria monocytogenes/enzymology; Molecular Sequence Data; Oligosaccharides/pharmacology; Penicillin-Binding Proteins/genetics; Penicillin-Binding Proteins/metabolism; Penicillin-Binding Proteins/physiology; Penicillins/metabolism; Peptidoglycan/metabolism; Polymers/metabolism; Polysaccharides/metabolism; Sequence Alignment; Thioglycolates/metabolism; Uridine Diphosphate N-Acetylmuramic Acid/analogs & derivatives; Uridine Diphosphate N-Acetylmuramic Acid/metabolism |
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