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...
| Main Authors: | , , , , |
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| Format: | Journal article |
| Language: | English |
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Elsevier
2016
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| _version_ | 1797088525316784128 |
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| author | Pettinati, I Brem, J Lee, S McHugh, P Schofield, C |
| author_facet | Pettinati, I Brem, J Lee, S McHugh, P Schofield, C |
| author_sort | Pettinati, I |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-07T02:51:19Z |
| format | Journal article |
| id | oxford-uuid:adc4dcac-6cd4-4319-96a5-9bc5a36f2381 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T02:51:19Z |
| publishDate | 2016 |
| publisher | Elsevier |
| record_format | dspace |
| spelling | oxford-uuid:adc4dcac-6cd4-4319-96a5-9bc5a36f23812022-03-27T03:38:04ZThe chemical biology of human metallo-β-lactamase fold proteins.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:adc4dcac-6cd4-4319-96a5-9bc5a36f2381EnglishSymplectic Elements at OxfordElsevier2016Pettinati, IBrem, JLee, SMcHugh, PSchofield, CThe 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. |
| spellingShingle | Pettinati, I Brem, J Lee, S McHugh, P Schofield, C The chemical biology of human metallo-β-lactamase fold proteins. |
| title | The chemical biology of human metallo-β-lactamase fold proteins. |
| title_full | The chemical biology of human metallo-β-lactamase fold proteins. |
| title_fullStr | The chemical biology of human metallo-β-lactamase fold proteins. |
| title_full_unstemmed | The chemical biology of human metallo-β-lactamase fold proteins. |
| title_short | The chemical biology of human metallo-β-lactamase fold proteins. |
| title_sort | chemical biology of human metallo β lactamase fold proteins |
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