{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T04:49:21Z","timestamp":1791866961832,"version":"4.3.4"},"reference-count":34,"publisher":"American Society for Microbiology","issue":"5","license":[{"start":{"date-parts":[[2006,3,1]],"date-time":"2006-03-01T00:00:00Z","timestamp":1141171200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2006,3]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            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            <jats:italic>N<\/jats:italic>\n            -acetylglucosamine-\n            <jats:italic>N<\/jats:italic>\n            -acetylmuramic acid-pentapeptide), and their transpeptidase activity catalyzes cross-linking between peptides carried by two adjacent glycan chains.\n            <jats:italic>Listeria monocytogenes<\/jats:italic>\n            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\n            <jats:sup>\u22121<\/jats:sup>\n            s\n            <jats:sup>\u22121<\/jats:sup>\n            from\n            <jats:italic>Escherichia coli<\/jats:italic>\n            lipid II substrate. PBP4 also catalyzes the aminolysis (\n            <jats:sc>d<\/jats:sc>\n            -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\n            <jats:italic>lmo2229<\/jats:italic>\n            encoding PBP4 in\n            <jats:italic>L. monocytogenes<\/jats:italic>\n            EGD did not have any significant effect on growth rate, peptidoglycan composition, cell morphology, or sensitivity to \u03b2-lactam antibiotics but did increase the resistance of the mutant to moenomycin.\n          <\/jats:p>","DOI":"10.1128\/jb.188.5.1875-1881.2006","type":"journal-article","created":{"date-parts":[[2006,2,16]],"date-time":"2006-02-16T02:38:02Z","timestamp":1140057482000},"page":"1875-1881","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":39,"title":["Characterization of the Bifunctional Glycosyltransferase\/Acyltransferase Penicillin-Binding Protein 4 of\n            <i>Listeria monocytogenes<\/i>"],"prefix":"10.1128","volume":"188","author":[{"given":"Joanna","family":"Zawadzka-Skomia\u0142","sequence":"first","affiliation":[{"name":"Institute of Microbiology, Warsaw University, Miecznikowa 1, 02-096 Warsaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zdzislaw","family":"Markiewicz","sequence":"additional","affiliation":[{"name":"Institute of Microbiology, Warsaw University, Miecznikowa 1, 02-096 Warsaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Martine","family":"Nguyen-Diste\u0300che","sequence":"additional","affiliation":[{"name":"Centre d'Inge\u0301nierie des Prote\u0301ines, Universite\u0301 de Lie\u0300ge, Institut de Chimie, B6a, B-4000 Sart-Tilman, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bart","family":"Devreese","sequence":"additional","affiliation":[{"name":"Laboratory of Protein Biochemistry and Protein Engineering, Ghent University, KL Ledeganckstraat 35, B-9000 Gent, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jean-Marie","family":"Fre\u0300re","sequence":"additional","affiliation":[{"name":"Centre d'Inge\u0301nierie des Prote\u0301ines, Universite\u0301 de Lie\u0300ge, Institut de Chimie, B6a, B-4000 Sart-Tilman, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mohammed","family":"Terrak","sequence":"additional","affiliation":[{"name":"Centre d'Inge\u0301nierie des Prote\u0301ines, Universite\u0301 de Lie\u0300ge, Institut de Chimie, B6a, B-4000 Sart-Tilman, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1042\/bj2790601","volume":"279","year":"1991","unstructured":"Adam, M., C. 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