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Title: Identification of the UDP-MurNAc-pentapeptide:L-alanine ligase for synthesis of branched peptidoglycan precursors in Enterococcus faecalis. Author: Bouhss A, Josseaume N, Allanic D, Crouvoisier M, Gutmann L, Mainardi JL, Mengin-Lecreulx D, van Heijenoort J, Arthur M. Journal: J Bacteriol; 2001 Sep; 183(17):5122-7. PubMed ID: 11489865. Abstract: Many species of gram-positive bacteria produce branched peptidoglycan precursors resulting from the transfer of various L-amino acids or glycine from amino acyl-tRNA to the epsilon-amino group of L-lysine. The UDP-MurNAc-pentapeptide:L-alanine ligase and alanyl-tRNA synthetase genes from Enterococcus faecalis were identified, cloned, and overexpressed in Escherichia coli. The purified enzymes were necessary and sufficient for tRNA-dependent addition of L-alanine to UDP-MurNAc-pentapeptide in vitro. The ligase belonged to the Fem family of proteins, which were initially identified genetically as factors essential for methicillin resistance in Staphylococcus aureus.[Abstract] [Full Text] [Related] [New Search]