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    Characterizing dynamical differences between TEM-1 and TEM-52 beta-lactamases

    Date
    2019-02-15
    Author
    Avery, Christopher
    Farmer, Jenny
    Tsilimigras, Matthew C. B.
    David, Charles
    Livesay, Dennis R.
    Jacobs, Donald J.
    Metadata
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    Citation
    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.
    Description
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    URI
    https://doi.org/10.1016/j.bpj.2018.11.1869
    http://hdl.handle.net/10057/16006
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