Editing Beta-lactamase (section)

== Mechanism of action ==
The two types of beta-lactamases work on the basis of the two basic mechanisms of opening the β-lactam ring.<ref name=":0" />

The SBLs are similar in structure and mechanistically to the β-lactam target penicillin-binding proteins (PBPs) which are necessary for cell wall building and modifying. SBLs and PBPs both covalently change an active site serine residue. The difference between the PBPs and SBLs is that the latter generates free enzyme and inactive antibiotic by the very quick hydrolysis of the acyl-enzyme intermediate.{{citation needed|date=March 2023}}

The MBLs use the Zn<sup>2+</sup> ions to activate a binding site water molecule for the hydrolysis of the β-lactam ring. Zinc chelators have recently been investigated as metallo-β-lactamase inhibitors, as they are often able to restore carbapenem susceptibility.<ref>{{Cite journal |last1=Principe |first1=Luigi |last2=Vecchio |first2=Graziella |last3=Sheehan |first3=Gerard |last4=Kavanagh |first4=Kevin |last5=Morroni |first5=Gianluca |last6=Viaggi |first6=Valentina |last7=di Masi |first7=Alessandra |last8=Giacobbe |first8=Daniele Roberto |last9=Luzzaro |first9=Francesco |last10=Luzzati |first10=Roberto |last11=Di Bella |first11=Stefano |date=2020-10-01 |title=Zinc Chelators as Carbapenem Adjuvants for Metallo-β-Lactamase-Producing Bacteria: In Vitro and In Vivo Evaluation |url=https://www.liebertpub.com/doi/10.1089/mdr.2020.0037 |journal=Microbial Drug Resistance |language=en |volume=26 |issue=10 |pages=1133–1143 |doi=10.1089/mdr.2020.0037 |pmid=32364820 |s2cid=218504647 |issn=1076-6294}}</ref>