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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.
Publication status:
Published

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Publisher copy:
10.1002/cbic.201000641

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Journal:
Chembiochem : a European journal of chemical biology
Volume:
12
Issue:
4
Pages:
531-534
Publication date:
2011-03-01
DOI:
EISSN:
1439-7633
ISSN:
1439-4227
Source identifiers:
124597
Language:
English
Keywords:
Pubs id:
pubs:124597
UUID:
uuid:095b4ccb-bdaa-4648-95c0-34a596706a4f
Local pid:
pubs:124597
Deposit date:
2012-12-19

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