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

Guengerich FP
J Biol Chem. 2015 290 (34): 20700-20701

PMID: 26152720 · PMCID: PMC4543631 · DOI:10.1074/jbc.R115.675652

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.

© 2015 by The American Society for Biochemistry and Molecular Biology, Inc.

MeSH Terms (16)

5-Methylcytosine AlkB Homolog 4, Lysine Demethylase Dioxygenases DNA DNA Damage DNA Repair Epigenesis, Genetic Gene Expression Humans Iron Isoenzymes Ketoglutaric Acids Multigene Family Oxidation-Reduction Protein Processing, Post-Translational Thymine

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