Characterizing dynamical differences between TEM-1 and TEM-52 beta-lactamases
Tsilimigras, Matthew C. B.
Livesay, Dennis R.
Jacobs, Donald J.
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Avery, Christopher; Farmer, Jenny; Tsilimigras, Matthew C. B.; David, Charles; Livesay, Dennis R.; Jacobs, Donald J. 2019. Characterizing dynamical differences between TEM-1 and TEM-52 beta-lactamases. Biophysical Journal, vol. 116:no. 3:S1:pp 343a
Beta-lactamase, produced in bacteria, defends against beta-lactam antibiotics such as penicillin and cephalosporins by hydrolyzing the beta-lactam ring. This is a primary cause of antibiotic resistance to beta-lactam antibiotics. The most common beta-lactamase, TEM-1, hydrolyze penicillin and first-generation cephalosporins. Within the TEM family alone there are over 400 sequences differing from the TEM-1 sequence by point mutations. Some of these mutations have conferred the beta-lactamase enzymes with extended substrate specificity which allow the hydrolysis of a wider range of beta-lactam antibiotics. These enzymes are known as extended spectrum beta-lactamases (ESBL), and they present a major challenge to the design of new antibiotics While the chemical mechanism of beta-lactamase resistance is well-known, the dynamics of sequence mutants conferring extended spectrum activity is not yet understood. In this work we aim to characterize differences in dynamics.
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