Myriam Delaire

Learn More
Arginine 244 is a highly conserved residue in Class A beta-lactamases, while methionine 69 is not. Informational suppression experiments show that replacement of M69 by a leucine, or that of R244 by most other amino acids lead to clavulanic acid-resistant phenotypes. The arginyl 244 side chain is tightly held in a network of interactions within the active(More)
Class A beta-lactamases are the major cause of bacterial resistance to beta-lactam antibiotics. In these active-site serine hydrolases, glutamic acid 166 has been hypothesized to act as a general acid-base catalyst. Replacing this residue by tyrosine in TEM-1 beta-lactamase yields an enzyme the activity of which is substantially lowered and strongly(More)
Container-content compatibility studies are required as part of the submission of a new product market authorization file or for a change relating to the primary product-contact packaging. Many regulatory publications and guidances are available in the USA, Europe, and Japan. However these publications and guidances are not sufficiently precise enough to(More)
The E166Y and the E166Y/R164S TEM-1 beta-lactamase mutant enzymes display extended spectrum substrate specificities. Electrospray mass spectrometry demonstrates that, with penicillin G as substrate, the rate-limiting step in catalysis is the hydrolysis of the E166Y acyl-enzyme complex. Comparison of the 1.8-A resolution x-ray structures of the wild-type and(More)
Future broadband integrated services digital networks (B-ISDN) are expected to use the Asyn-chronous Transfer Mode (ATM) technology and support multiple services. In this multiple service context, three Connection Admission Control (CAC) strategies which guarantee Grade of Services (GoS) in terms of call block: Complete Sharing (CS), Complete Sharing with(More)
When ferric ion was added to solutions of the enzyme dextransucrase, first-order followed by second-order inactivation behavior was observed. The initial rapid activity loss was attributed to a ferric ion interacting with the thiol group of the native monomer to form a less active enzyme-ion complex; the second inactivation stage involved enzyme-ion complex(More)
  • 1