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The 2‐Oxoglutarate‐Dependent Oxygenase JMJD6 Catalyses Oxidation of Lysine Residues to give 5 S ‐Hydroxylysine Residues
Author(s) -
Mantri Monica,
Loik Nikita D.,
Hamed Refaat B.,
Claridge Timothy D. W.,
McCullagh James S. O.,
Schofield Christopher J.
Publication year - 2011
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201000641
Subject(s) - hydroxylysine , hydroxylation , lysine , chemistry , biochemistry , stereochemistry , amino acid , oxygenase , subfamily , enzyme , gene
Amino acid analyses reveal that JMJD6‐catalysed hydroxylation of RNA‐splicing regulatory protein fragments occurs to give hydroxylysine products with 5 S stereochemistry. This contrasts with collagen lysyl hydroxylases, which give 5 R ‐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.