Literature DB >> 22238144

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

Monica Mantri1, Nikita D Loik, Refaat B Hamed, Timothy D W Claridge, James S O McCullagh, Christopher J Schofield.   

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.
Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

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Year:  2011        PMID： 22238144     DOI： 10.1002/cbic.201000641

Source DB:  PubMed          Journal:  Chembiochem        ISSN： 1439-4227            Impact factor:   3.164


  25 in total

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9.  Lysyl 5-hydroxylation, a novel histone modification, by Jumonji domain containing 6 (JMJD6).

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