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Journal of Bacteriology, September 2001, p. 5122-5127, Vol. 183, No. 17
INSERM E0004-LRMA, UFR Broussais-Hôtel
Dieu, Université Paris VI, 75270 Paris,1
and Biochimie Moléculaire et Cellulaire, UMR 8619 CNRS,
Université Paris-Sud, 91405 Orsay Cedex,2
France
Received 20 February 2001/Accepted 13 June 2001
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
0021-9193/01/$04.00+0 DOI: 10.1128/JB.183.17.5122-5127.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Identification of the
UDP-MurNAc-Pentapeptide:L-Alanine Ligase for Synthesis of
Branched Peptidoglycan Precursors in Enterococcus
faecalis
-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.
*
Corresponding author. Mailing address: LRMA,
Université Paris VI, 15 rue de l'Ecole de Médecine, 75270 Paris Cedex 06, France. Phone: 33 (0)1 43 25 00 33. Fax: 33 (0)1 43 25 68 12. E-mail: michel.arthur{at}bhdc.jussieu.fr.
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