The 2-oxoglutarate-dependent oxygenase JMJD6 catalyses oxidation of lysine residues to give 5S-hydroxylysine residues.

@article{Mantri2011The2O,
  title={The 2-oxoglutarate-dependent oxygenase JMJD6 catalyses oxidation of lysine residues to give 5S-hydroxylysine residues.},
  author={Monica Mantri and Nikita D. Loik and Refaat B Hamed and Timothy D W Claridge and James McCullagh and Christopher J. Schofield},
  journal={Chembiochem : a European journal of chemical biology},
  year={2011},
  volume={12 4},
  pages={531-4}
}
Amino acid analyses reveal that JMJD6-catalysed hydroxylation of RNA-splicing regulatory protein fragments occurs to give hydroxylysine products with 5S stereochemistry. This contrasts with collagen lysyl hydroxylases, which give 5R-hydroxylated products. The work suggests that more than one subfamily of lysyl hydroxylases has evolved and illustrates the importance of stereochemical assignments in proteomic analyses. 

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