TY - JOUR
AU - 
AB - THE JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 275, No. 22, Issue of June 2, pp. 16490 –16496, 2000 © 2000 by The American Society for Biochemistry and Molecular Biology, Inc. Printed in U.S.A. Novel Mechanism of b-Lactam Resistance Due to Bypass of DD-Transpeptidation in Enterococcus faecium* Received for publication, December 6, 1999, and in revised form, March 10, 2000 Published, JBC Papers in Press, March 19, 2000, DOI 10.1074/jbc.M909877199 Jean-Luc Mainardi‡§, Raymond Legrand¶, Michel Arthuri, Bernard Schoot¶, Jean van Heijenoorti, and Laurent Gutmann‡ From the ‡L.R.M.A., UFR Broussais-Ho ˆ tel Dieu, Universite ´ Paris VI, 75270 Paris, France, the ¶Physics Department, Hoechst Marion Roussel, Romainville, 93235 France, and the iBiochimie Mole ´culaire et Cellulaire, CNRS, Orsay, 91405 France The peptidoglycan structure of in vitro selected ampi- such as penicillin and ampicillin, are structural analogs of the cillin-resistant mutant Enterococcus faecium D344M512 C-terminal D-Ala -D-Ala end of peptidoglycan precursors and 4 5 and of the susceptible parental strain D344S was deter- act as suicide substrates in a similar acylation reaction (4). The mined by reverse phase high performance liquid chroma- second step of the transpeptidation reaction results in a cross- tography and mass spectrometry. The muropeptide linking and release of the 
TI - Novel Mechanism of β-Lactam Resistance Due to Bypass of DD-Transpeptidation in Enterococcus faecium
JF - Journal of Biological Chemistry
DO - 10.1074/jbc.m909877199
DA - 2000-06-01
UR - https://www.deepdyve.com/lp/unpaywall/novel-mechanism-of-lactam-resistance-due-to-bypass-of-dd-BkBcqa4DBr
DP - DeepDyve
ER -