Structural and Functional Aspects of Extended-Spectrum AmpC Cephalosporinases

Author(s): Rachel A. Powers

Volume 17, Issue 9, 2016

Page: [1051 - 1060] Pages: 10

DOI: 10.2174/1573399811666150615144707

Price: $65

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.

Graphical Abstract

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