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

Autor: Mantri M; Department of Chemistry, Oxford University, Mansfield Road, Oxford OX1 3TA, UK., Loik ND, Hamed RB, Claridge TD, McCullagh JS, Schofield CJ
Jazyk: angličtina
Zdroj: Chembiochem : a European journal of chemical biology [Chembiochem] 2011 Mar 07; Vol. 12 (4), pp. 531-4. Date of Electronic Publication: 2011 Jan 18.
DOI: 10.1002/cbic.201000641
Abstrakt: 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.)
Databáze: MEDLINE
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