Autocatalysed oxidative modifications to 2-oxoglutarate dependent oxygenases.
Ferrous iron and 2-oxoglutarate-dependent oxygenases and related enzymes catalyse a range of oxidative reactions, possibly the widest of any enzyme family. Their catalytic flexibility is proposed to be related to their nonhaem iron-binding site, which utilizes two or three protein-based ligands. A p...
| Main Authors: | , , , |
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| Format: | Journal article |
| Language: | English |
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2012
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| _version_ | 1797089222057787392 |
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| author | Mantri, M Zhang, Z McDonough, M Schofield, C |
| author_facet | Mantri, M Zhang, Z McDonough, M Schofield, C |
| author_sort | Mantri, M |
| collection | OXFORD |
| description | Ferrous iron and 2-oxoglutarate-dependent oxygenases and related enzymes catalyse a range of oxidative reactions, possibly the widest of any enzyme family. Their catalytic flexibility is proposed to be related to their nonhaem iron-binding site, which utilizes two or three protein-based ligands. A possible penalty for this flexibility is that they may be more prone to oxidative damage than the P450 oxidases, where the iron is arguably located in a more controlled environment. We review the evidence for autocatalysed oxidative modifications to 2-oxoglutarate-dependent oxygenases, including the recently reported studies on human enzymes, as well as the oxidative fragmentations observed in the case of the plant ethylene-forming enzyme (1-aminocyclopropane-1-carboxylic acid oxidase). |
| first_indexed | 2024-03-07T03:01:18Z |
| format | Journal article |
| id | oxford-uuid:b10cee21-71c2-4327-a028-ee36cd77655f |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T03:01:18Z |
| publishDate | 2012 |
| record_format | dspace |
| spelling | oxford-uuid:b10cee21-71c2-4327-a028-ee36cd77655f2022-03-27T04:00:59ZAutocatalysed oxidative modifications to 2-oxoglutarate dependent oxygenases.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:b10cee21-71c2-4327-a028-ee36cd77655fEnglishSymplectic Elements at Oxford2012Mantri, MZhang, ZMcDonough, MSchofield, CFerrous iron and 2-oxoglutarate-dependent oxygenases and related enzymes catalyse a range of oxidative reactions, possibly the widest of any enzyme family. Their catalytic flexibility is proposed to be related to their nonhaem iron-binding site, which utilizes two or three protein-based ligands. A possible penalty for this flexibility is that they may be more prone to oxidative damage than the P450 oxidases, where the iron is arguably located in a more controlled environment. We review the evidence for autocatalysed oxidative modifications to 2-oxoglutarate-dependent oxygenases, including the recently reported studies on human enzymes, as well as the oxidative fragmentations observed in the case of the plant ethylene-forming enzyme (1-aminocyclopropane-1-carboxylic acid oxidase). |
| spellingShingle | Mantri, M Zhang, Z McDonough, M Schofield, C Autocatalysed oxidative modifications to 2-oxoglutarate dependent oxygenases. |
| title | Autocatalysed oxidative modifications to 2-oxoglutarate dependent oxygenases. |
| title_full | Autocatalysed oxidative modifications to 2-oxoglutarate dependent oxygenases. |
| title_fullStr | Autocatalysed oxidative modifications to 2-oxoglutarate dependent oxygenases. |
| title_full_unstemmed | Autocatalysed oxidative modifications to 2-oxoglutarate dependent oxygenases. |
| title_short | Autocatalysed oxidative modifications to 2-oxoglutarate dependent oxygenases. |
| title_sort | autocatalysed oxidative modifications to 2 oxoglutarate dependent oxygenases |
| work_keys_str_mv | AT mantrim autocatalysedoxidativemodificationsto2oxoglutaratedependentoxygenases AT zhangz autocatalysedoxidativemodificationsto2oxoglutaratedependentoxygenases AT mcdonoughm autocatalysedoxidativemodificationsto2oxoglutaratedependentoxygenases AT schofieldc autocatalysedoxidativemodificationsto2oxoglutaratedependentoxygenases |