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Structural, Molecular and Kinetic Characterization of Metallo-Beta-Lactamases

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Chemical Biology".

Deadline for manuscript submissions: closed (31 December 2021) | Viewed by 442

Special Issue Editors

Department of Biotechnological and Applied Clinical Sciences, University of L’Aquila, L’Aquila, Italy
Interests: molecular and epidemiological characterization of mechanisms of resistance to antibiotics in Gram-negative pathogens; mobile genetic elements; beta-lactamases; beta-lactamase inhibitors; mechanisms of serine- and metallo-beta-lactamases
Department of Biotechnological and Applied Clinical Sciences, University of L’Aquila, 67100 L’Aquila, Italy
Interests: molecular and epidemiological characterization of mechanisms of resistance to antibiotics in Gram-negatove pathogens; mobile genetic elements; beta-lactamases; beta-lactamase inhibitors; mechanisms of serine- and metallo-beta-lactamases
Special Issues, Collections and Topics in MDPI journals
Department of Biotechnological and Applied Clinical Sciences, University of L’Aquila, 67100 L’Aquila, Italy
Interests: enzymes; PCR; microbiology; cloning; biochemistry; electrophoresis; SDS-PAGE; protein expression; next generation sequencing; antibiotic resistance
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Metallo-β-lactamases (MBLs) are Zn2+-dependent enzymes that are able to hydrolyze most β-lactams, including carbapenems, but not monobactams. On the basis of the sequences, three subclasses of class B β-lactamases (B1, B2, and B3) were identified. There is a relatively low-sequence identity (<20%) between the subclasses. Enzymes of subclasses B1 and B3 are broad spectrum enzymes that hydrolyze most β-lactam antibiotics, including carbapenems, and the active site contains two zinc ions. The subclass B2 enzymes are strictly carbapenemases, and their active site contains only one zinc. MBLs have been identified in various Gram-negative clinical isolates, including several species of Enterobacteriaceae, Pseudomonas aeruginosa, and Acinetobacter spp. The more geographically widespread MBLs include IMP, VIM, and NDM. Actually, one of the most difficult problems is related to the absence of inhibitors for MBLs in clinical therapy. The development of new non-β-lactam inhibitors would provide a new opportunity for the treatment of bacterial infections with existing antibiotics.

The following topics will be considered:

  • Structure and function of MBLs;
  • Kinetic and molecular aspects of MBLs;
  • New MBLs inhibitors.

Prof. Dr. Gianfranco Amicosante
Prof. Dr. Mariagrazia Perilli
Dr. Alessandra Piccirilli
Guest Editors

Manuscript Submission Information

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Published Papers

There is no accepted submissions to this special issue at this moment.
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