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

Chembiochem. 2011 Mar 7;12(4):531-4. doi: 10.1002/cbic.201000641. Epub 2011 Jan 18.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Catalysis
  • Humans
  • Hydroxylysine / chemistry*
  • Jumonji Domain-Containing Histone Demethylases / chemistry*
  • Ketoglutaric Acids / chemistry*
  • Magnetic Resonance Spectroscopy
  • Molecular Structure
  • Oxidation-Reduction
  • Oxygenases / chemistry*
  • Stereoisomerism

Substances

  • Ketoglutaric Acids
  • Hydroxylysine
  • Oxygenases
  • JMJD6 protein, human
  • Jumonji Domain-Containing Histone Demethylases