Unusual substrate specificity of the peptidoglycan MurE ligase from Erysipelothrix rhusiopathiae
详细信息 查看全文
- 作者：Delphine Patina ; delphine.patin@i2bc.paris-saclay.fr" class="auth_mail" title="E-mail the corresponding author ; Samo Turkb ; 1 ; Hé ; lè ; ne Barreteaua ; Jean-Luc Mainardic ; d ; e ; Michel Arthurc ; d ; e ; Stanislav Gobecb ; Dominique Mengin-Lecreulxa ; Didier Blanota
- 关键词：l-alanine-adding enzyme ; meso-diaminopimelate-adding enzyme ; Erysipelothrix rhusiopathiae ; MurE ; Peptidoglycan
- 刊名：Biochimie
- 出版年：2016
- 出版时间：February 2016
- 年：2016
- 卷：121
- 期：Complete
- 页码：209-218
- 全文大小：1187 K
文摘
- class="listitem" id="list_ulist0010">
- class="label">•
Peptidoglycan from E. rhusiopathiae contains class="smallcaps">l-Ala at position 3 of the peptide stem.
- class="label">•
The substrate specificity of MurE from E. rhusiopathiae was studied.
- class="label">•
class="smallcaps">l-Ala was a substrate for MurEEr, but also meso-diaminopimelate in vitro.
- class="label">•
A HDNR motif was involved in the unusual substrate specificity of MurEEr.
- class="label">•
Upon MurEEr production, E. coli incorporated class="smallcaps">l-Ala into peptidoglycan at position 3.