Introduction: Metals in Biology: α-Ketoglutarate/Iron-Dependent Dioxygenases |
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Authors: | F Peter Guengerich |
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Institution: | From the Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0146 |
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Abstract: | Four minireviews deal with aspects of the α-ketoglutarate/iron-dependent dioxygenases in this eighth Thematic Series on Metals in Biology. The minireviews cover a general introduction and synopsis of the current understanding of mechanisms of catalysis, the roles of these dioxygenases in post-translational protein modification and de-modification, the roles of the ten-eleven translocation (Tet) dioxygenases in the modification of methylated bases (5mC, T) in DNA relevant to epigenetic mechanisms, and the roles of the AlkB-related dioxygenases in the repair of damaged DNA and RNA. The use of α-ketoglutarate (alternatively termed 2-oxoglutarate) as a co-substrate in so many oxidation reactions throughout much of nature is notable and has surprisingly emerged from biochemical and genomic analysis. About 60 of these enzymes are now recognized in humans, and a number have been identified as having critical functions. |
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Keywords: | dioxygenase DNA demethylation DNA repair histone demethylase hydroxylase iron post-translational modification (PTM) |
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