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Review
. 2015 Aug 21;290(34):20700-20701.
doi: 10.1074/jbc.R115.675652. Epub 2015 Jul 7.

Introduction: Metals in Biology: α-Ketoglutarate/Iron-Dependent Dioxygenases

F Peter Guengerich  1
Affiliations
Review

Introduction: Metals in Biology: α-Ketoglutarate/Iron-Dependent Dioxygenases

F Peter Guengerich. J Biol Chem. .

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.

Keywords: DNA demethylation; DNA repair; dioxygenase; histone demethylase; hydroxylase; iron; post-translational modification (PTM).

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Figures

FIGURE 1.
FIGURE 1.
Stoichiometry of α-ketoglutarate/iron-dependent dioxygenases. R, substrate; R*O, product; *O, 18O tagging.
See this image and copyright information in PMC

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