The Chemical Biology of Human Metallo-β-Lactamase Fold Proteins

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 detox...

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Published inTrends in biochemical sciences (Amsterdam. Regular ed.) Vol. 41; no. 4; pp. 338 - 355
Main Authors Pettinati, Ilaria, Brem, Jürgen, Lee, Sook Y., McHugh, Peter J., Schofield, Christopher J.
Format Journal Article
LanguageEnglish
Published England Elsevier Ltd 01.04.2016
Elsevier Trends Journals
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Abstract 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. MBLs are mono- or di-zinc ion-dependent hydrolases that enable bacterial resistance to almost all β-lactam antibiotics. The αββα MBL core fold is widely distributed and supports a range of catalytic activities, including redox reactions. hMBL proteins are a small family of approximately 18 zinc- and iron-dependent proteins with roles in metabolism and/or detoxification and nucleic acid modification. In a notable parallel with the role of bacterial MBLs in antibiotic resistance, some hMBLf enzymes enable resistance to chemotherapy drugs, such as cisplatin and mitomycin C.
AbstractList 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. MBLs are mono- or di-zinc ion-dependent hydrolases that enable bacterial resistance to almost all β-lactam antibiotics. The αββα MBL core fold is widely distributed and supports a range of catalytic activities, including redox reactions. hMBL proteins are a small family of approximately 18 zinc- and iron-dependent proteins with roles in metabolism and/or detoxification and nucleic acid modification. In a notable parallel with the role of bacterial MBLs in antibiotic resistance, some hMBLf enzymes enable resistance to chemotherapy drugs, such as cisplatin and mitomycin C.
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.
Author Pettinati, Ilaria
Schofield, Christopher J.
Brem, Jürgen
Lee, Sook Y.
McHugh, Peter J.
AuthorAffiliation 1 Department of Chemistry, University of Oxford, 12 Mansfield Road, Oxford, OX1 3TA, UK
2 Weatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital, Oxford, OX3 9DS, UK
AuthorAffiliation_xml – name: 1 Department of Chemistry, University of Oxford, 12 Mansfield Road, Oxford, OX1 3TA, UK
– name: 2 Weatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital, Oxford, OX3 9DS, UK
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  surname: Pettinati
  fullname: Pettinati, Ilaria
  organization: Department of Chemistry, University of Oxford, 12 Mansfield Road, Oxford, OX1 3TA, UK
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  givenname: Jürgen
  surname: Brem
  fullname: Brem, Jürgen
  organization: Department of Chemistry, University of Oxford, 12 Mansfield Road, Oxford, OX1 3TA, UK
– sequence: 3
  givenname: Sook Y.
  surname: Lee
  fullname: Lee, Sook Y.
  organization: Weatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital, Oxford, OX3 9DS, UK
– sequence: 4
  givenname: Peter J.
  surname: McHugh
  fullname: McHugh, Peter J.
  organization: Weatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital, Oxford, OX3 9DS, UK
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  givenname: Christopher J.
  surname: Schofield
  fullname: Schofield, Christopher J.
  email: christopher.schofield@chem.ox.ac.uk
  organization: Department of Chemistry, University of Oxford, 12 Mansfield Road, Oxford, OX1 3TA, UK
BackLink https://www.ncbi.nlm.nih.gov/pubmed/26805042$$D View this record in MEDLINE/PubMed
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Issue 4
Keywords metallo β-lactamase fold protein
β-lactam antibiotic and cancer drug resistance
hydrogen sulphide metabolism
RNA processing
nuclease
DNA repair
Language English
License http://creativecommons.org/licenses/by/4.0
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Snippet 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...
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SubjectTerms Arabidopsis - enzymology
Arabidopsis - genetics
Bacteria - enzymology
Bacteria - genetics
beta-Lactamases - chemistry
beta-Lactamases - genetics
beta-Lactamases - metabolism
beta-Lactams - chemistry
beta-Lactams - metabolism
DNA repair
DNA Repair Enzymes - chemistry
DNA Repair Enzymes - genetics
DNA Repair Enzymes - metabolism
Exodeoxyribonucleases
Gene Expression
Humans
hydrogen sulphide metabolism
Hydrolysis
metallo β-lactamase fold protein
Mitochondrial Proteins - chemistry
Mitochondrial Proteins - genetics
Mitochondrial Proteins - metabolism
Muscle Proteins - chemistry
Muscle Proteins - genetics
Muscle Proteins - metabolism
Nuclear Proteins - chemistry
Nuclear Proteins - genetics
Nuclear Proteins - metabolism
nuclease
Nucleocytoplasmic Transport Proteins - chemistry
Nucleocytoplasmic Transport Proteins - genetics
Nucleocytoplasmic Transport Proteins - metabolism
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Folding
Protein Interaction Domains and Motifs
Review
RNA processing
Thiolester Hydrolases - chemistry
Thiolester Hydrolases - genetics
Thiolester Hydrolases - metabolism
Zinc - chemistry
Zinc - metabolism
β-lactam antibiotic and cancer drug resistance
Title The Chemical Biology of Human Metallo-β-Lactamase Fold Proteins
URI https://dx.doi.org/10.1016/j.tibs.2015.12.007
https://www.ncbi.nlm.nih.gov/pubmed/26805042
https://search.proquest.com/docview/1797868117
https://pubmed.ncbi.nlm.nih.gov/PMC4819959
Volume 41
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