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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.sbi.2016.05.013

Type

Journal article

Journal

Trends in biochemical sciences

Publication Date

21/01/2016

Volume

41

Pages

338 - 355

Addresses

Department of Chemistry, University of Oxford, 12 Mansfield Road, Oxford, OX1 3TA, UK.