Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

The αββα metallo β-lactamase (MBL) fold (MBLf) was first observed in bacterial enzymes that catalyze the hydrolysis of almost all β-lactam antibiotics, but is now known to be widely distributed. The MBL core protein fold is present in human enzymes with diverse biological roles, including cell detoxification pathways and enabling resistance to clinically important anticancer medicines. Human (h)MBLf enzymes can bind metals, including zinc and iron ions, and catalyze a range of chemically interesting reactions, including both redox (e.g., ETHE1) and hydrolytic processes (e.g., Glyoxalase II, SNM1 nucleases, and CPSF73). With a view to promoting basic research on MBLf enzymes and their medicinal targeting, here we summarize current knowledge of the mechanisms and roles of these important molecules.

Original publication

DOI

10.1016/j.tibs.2015.12.007

Type

Journal article

Journal

Trends Biochem Sci

Publication Date

04/2016

Volume

41

Pages

338 - 355

Keywords

DNA repair, RNA processing, hydrogen sulphide metabolism, metallo β-lactamase fold protein, nuclease, β-lactam antibiotic and cancer drug resistance, Arabidopsis, Bacteria, DNA Repair Enzymes, Gene Expression, Humans, Hydrolysis, Mitochondrial Proteins, Muscle Proteins, Nuclear Proteins, Nucleocytoplasmic Transport Proteins, Protein Binding, Protein Conformation, alpha-Helical, Protein Conformation, beta-Strand, Protein Folding, Protein Interaction Domains and Motifs, Thiolester Hydrolases, Zinc, beta-Lactamases, beta-Lactams