Studies on the catalytic domains of multiple JmjC oxygenases using peptide substrates

@inproceedings{Williams2014StudiesOT,
  title={Studies on the catalytic domains of multiple JmjC oxygenases using peptide substrates},
  author={Sophie T Williams and Louise J Walport and Richard J Hopkinson and Sarah Madden and Rasheduzzaman Chowdhury and Christopher J. Schofield and Akane Kawamura},
  booktitle={Epigenetics},
  year={2014}
}
The JmjC-domain-containing 2-oxoglutarate-dependent oxygenases catalyze protein hydroxylation and N(ϵ)-methyllysine demethylation via hydroxylation. A subgroup of this family, the JmjC lysine demethylases (JmjC KDMs) are involved in histone modifications at multiple sites. There are conflicting reports as to the substrate selectivity of some JmjC oxygenases with respect to KDM activities. In this study, a panel of modified histone H3 peptides was tested for demethylation against 15 human JmjC… CONTINUE READING
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