Ureases and metallo-β-lactamases are amide hydrolases closely related in function and
structure. However, one major difference between them is that the former uses two nickel …

Herein we briefly review theoretical contributions that have increased our understanding of
the structure and function of metallo‐β‐lactamases and ureases. Both are bimetallic …

Metallo-β-lactamases can hydrolyze and deactivate lactam-containing antibiotics, which is
the major mechanism for causing drug resistance in the treatment of bacterial infections …

Metallo-enzymes play an indispensible role in many biological functions, and their modes of
substrate binding and catalysis differ considerably from those of metal-free enzymes. A …

A dizinc β-lactamase (L1 from Stenotrophomonas maltophilia) complexed with an antibiotic
compound (moxalactam) has been studied using a hybrid quantum mechanical/molecular …

We present both experimental and theoretical results on simple model systems of zinc-β-
lactamases. Kinetic studies show that the rate of degradation of β-lactam antibiotics in the …

Emergence of antibiotic resistance due to New Delhi metallo-β-lactamase (NDM-1) bacterial
enzymes is of great concern due to their ability to hydrolyze a wide range of antibiotics …

Metallo β-lactamases (MβL) are enzymes naturally evolved by bacterial strains under the
evolutionary pressure of β-lactam antibiotic clinical use. They have a broad substrate …

Based on hybrid QM/MM molecular dynamics simulation and density functional theoretical
(DFT) calculations, we investigate the mechanistic and energetic features of the catalytic …

Metallo-β-lactamases are bacterial enzymes that may function with either one or two zinc
ions bound in the active site. In this work, the binding of benzylpenicillin to mono-zinc …