Structural and Functional Aspects of Extended-Spectrum AmpC Cephalosporinases

Rachel      A. Powers

Abstract

β-lactam antibiotics have revolutionized modern medicine, but resistance to these drugs is a major public health crisis. Traditionally, class C β-lactamases were referred to as cephalosporinases due to their substrate preference for this particular class of β-lactams. However, the emergence of AmpC enzymes with extended-spectrum activity (extended-spectrum cephalosporinases or ESACs) is particularly worrisome, especially given that most clinical β-lactamase inhibitors are ineffective against these enzymes. This review summarizes structures of several extended spectrum class C β-lactamases and analyzes the structure-function relationship observed among them.

Keywords: β-Lactamase, cephalosporinase, extended-spectrum, structure-function, X-ray crystal structures.

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Current Drug Targets

Title:Structural and Functional Aspects of Extended-Spectrum AmpC Cephalosporinases

Volume: 17 Issue: 9

Author(s): Rachel A. Powers

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Keywords: β-Lactamase, cephalosporinase, extended-spectrum, structure-function, X-ray crystal structures.

Abstract: β-lactam antibiotics have revolutionized modern medicine, but resistance to these drugs is a major public health crisis. Traditionally, class C β-lactamases were referred to as cephalosporinases due to their substrate preference for this particular class of β-lactams. However, the emergence of AmpC enzymes with extended-spectrum activity (extended-spectrum cephalosporinases or ESACs) is particularly worrisome, especially given that most clinical β-lactamase inhibitors are ineffective against these enzymes. This review summarizes structures of several extended spectrum class C β-lactamases and analyzes the structure-function relationship observed among them.

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Cite this article as:

A. Powers Rachel, Structural and Functional Aspects of Extended-Spectrum AmpC Cephalosporinases, Current Drug Targets 2016; 17 (9) . https://dx.doi.org/10.2174/1573399811666150615144707

DOI https://dx.doi.org/10.2174/1573399811666150615144707	Print ISSN 1389-4501
Publisher Name Bentham Science Publisher	Online ISSN 1873-5592

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