Characterizing dynamical differences between TEM-1 and TEM-52 beta-lactamases
Avery, Christopher Farmer, Jenny Tsilimigras, Matthew C. B. David, Charles Livesay, Dennis R. Jacobs, Donald J.
Avery, Christopher
Farmer, Jenny
Tsilimigras, Matthew C. B.
David, Charles
Livesay, Dennis R.
Jacobs, Donald J.
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2019-02-15
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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
Abstract
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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Cell Press
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Biophysical Journal;v.116:no.3:S1
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0006-3495