Lecoq, Lauriane <br/><br/>
Structure of Enterococcus faeciuml,d-transpeptidase acylated by ertapenem provides insight into the inactivation mechanism.  [electronic resource] 

 -  ACS chemical biology  2013 
 - 1140-6 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>1554-8937 
<br/><br/><label>Standard No.: </label>10.1021/cb4001603  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Acetylation<br/>Anti-Bacterial Agents--pharmacology<br/>Enterococcus faecium--chemistry<br/>Ertapenem<br/>Gram-Positive Bacterial Infections--drug therapy<br/>Humans<br/>Models, Molecular<br/>Peptidyl Transferases--antagonists & inhibitors<br/>Protein Conformation--drug effects<br/>beta-Lactams--pharmacology