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

Journal article

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: Mantri, M; Loik, N; Hamed, R; Claridge, T; McCullagh, J

• Publication status: Published
• Journal: Chembiochem : a European journal of chemical biology
• Volume: 12
• Issue: 4
• Pages: 531-534
• Publication date: 2011-03-01
• DOI: 10.1002/cbic.201000641
• EISSN: 1439-7633
• ISSN: 1439-4227
• Language: English
• Keywords: Hydroxylysine; Humans; Magnetic Resonance Spectroscopy; Jumonji Domain-Containing Histone Demethylases; Oxidation-Reduction; Stereoisomerism; Catalysis; Ketoglutaric Acids; Molecular Structure; Oxygenases; Animals