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<Structure load='1ke4' size='400' frame='true' color='white' align='right' caption='AmpC Class C Beta-lactamase' />

== Function and Mechanism ==

[[Image:Beta-lactam.jpg|200px|thumb|left|A β-lactam antibiotic (Penicillin)]]Clinically, β-lactam antibiotics, characterized by their central chemical structure, are utilized to combat bacterial infections by targeting penicillin-binding proteins (PBPs), also known as transpeptidases. PBPs are enzymes that are located in the cell membrane and function in cross-linking to form the peptidoglycan layer. PBPs have a deprotonated serine which executes nucleophilic attack on the carbonyl carbon. The PBP is then covalently attached to one unit of peptidoglycan. The amino group of an alanine on a second unit of peptidoglycan then performs a second nucleophilic attack on the carbonyl carbon, resulting in two covalently cross-linked peptidoglycan units and the regeneration of the catalytic PBP.<ref>"Peptidoglycan cell wall." The University of Warwick. n.d. Web. 25 Jan 15</ref>

With the mechanistic knowledge of β-lactamases, there are two apparent options for clinical treatment of β-lactam resistant bacteria. Scientists could either (a) design an entirely new class of antibiotic that are not reliant on the chemical structure of the β-lactam ring, or (b) use the current arsenal of antibiotics in combination with an inhibitor that will deactivate the β-lactamase. A β-lactamase inhibitor is a compound that could form a tight complex to the active site of the enzyme and causes the β-lactamase to be unable to bind and inactivate another antibiotic molecule. Links to examples Class C β-lactamases, both with and without clinical inhibitors bound, are provided.  

==References==

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