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Unusual substrate specificity of the peptidoglycan MurE ligase from Erysipelothrix rhusiopathiaePatin, Delphine ...Erysipelothrix rhusiopathiae is a Gram-positive bacterium pathogenic to many species of birds and mammals, including humans. The main feature of its peptidoglycan is the presence of l-alanine at ... position 3 of the peptide stem. In the present work, we cloned the murE gene from E. rhusiopathiae and purified the corresponding protein as His6-tagged form. Enzymatic assays showed that E. rhusiopathiae MurE was indeed an l-alanine-adding enzyme. Surprisingly, it was also able, although to a lesser extent, to add meso-diaminopimelic acid, the amino acid found at position 3 in many Gram-negative bacteria, Bacilli and Mycobacteria. Sequence alignment of MurE enzymes from E. rhusiopathiae and Escherichia coli revealed that the DNPR motif that is characteristic of meso-diaminopimelate-adding enzymes was replaced by HDNR. The role of the latter motif in the interaction with l-alanine and meso-diaminopimelic acid was demonstrated by site-directed mutagenesis experiments and the construction of a homology model. The over expression of the E. rhusiopathiae murE gene in E. coli resulted in the incorporation of l-alanine at position 3 of the peptide part of peptidoglycan.Source: Biochimie. - ISSN 0300-9084 (Vol. 121, Feb. 2016, str. 209-218)Type of material - article, component part ; adult, seriousPublish date - 2016Language - englishCOBISS.SI-ID - 4008817
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Links to authors' personal bibliographies | Links to information on researchers in the SICRIS system |
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Patin, Delphine | ![]() |
Turk, Samo, farmacevt | 29773 |
Barreteau, Hélène | ![]() |
Mainardi, Jean-Luc | ![]() |
Arthur, Michel | ![]() |
Gobec, Stanislav, 1970- | 15284 |
Mengin-Lecreulx, Dominique | ![]() |
Blanot, Didier | ![]() |
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