title: The 2-oxoglutarate-dependent oxygenase JMJD6 catalyses oxidation of lysine residues to give 5S-hydroxylysine residues.
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.
authors.affiliation: Department of Chemistry, Oxford University, Mansfield Road, Oxford OX1 3TA, UK.
authors.forename: Monica
authors.initials: M
authors.lastname: Mantri
authors.forename: Nikita D
authors.initials: ND
authors.lastname: Loik
authors.forename: Refaat B
authors.initials: RB
authors.lastname: Hamed
authors.forename: Timothy D W
authors.initials: TD
authors.lastname: Claridge
authors.forename: James S O
authors.initials: JS
authors.lastname: McCullagh
authors.forename: Christopher J
authors.initials: CJ
authors.lastname: Schofield
mesh_terms: D000818:Animals; D002384:Catalysis; D006801:Humans; D006901:Hydroxylysine / Q000737:chemistry*; D056484:Jumonji Domain-Containing Histone Demethylases / Q000737:chemistry*; D007656:Ketoglutaric Acids / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D010084:Oxidation-Reduction; D010105:Oxygenases / Q000737:chemistry*; D013237:Stereoisomerism
chemical_list: D007656:Ketoglutaric Acids; D006901:Hydroxylysine; D010105:Oxygenases; C498707:JMJD6 protein, human; D056484:Jumonji Domain-Containing Histone Demethylases