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J Biol Chem. 2015 Aug 21;290(34):20712-22. doi: 10.1074/jbc.R115.662627. Epub 2015 Jul 7.

Protein Hydroxylation Catalyzed by 2-Oxoglutarate-dependent Oxygenases.

Author information

1
From the Chemistry Research Laboratory, University of Oxford, Mansfield Road, Oxford, OX1 3TA, United Kingdom.
2
From the Chemistry Research Laboratory, University of Oxford, Mansfield Road, Oxford, OX1 3TA, United Kingdom sarah.wilkins@chem.ox.ac.uk.
3
From the Chemistry Research Laboratory, University of Oxford, Mansfield Road, Oxford, OX1 3TA, United Kingdom christopher.schofield@chem.ox.ac.uk.

Abstract

The post-translational hydroxylation of prolyl and lysyl residues, as catalyzed by 2-oxoglutarate (2OG)-dependent oxygenases, was first identified in collagen biosynthesis. 2OG oxygenases also catalyze prolyl and asparaginyl hydroxylation of the hypoxia-inducible factors that play important roles in the adaptive response to hypoxia. Subsequently, they have been shown to catalyze N-demethylation (via hydroxylation) of N(ϵ)-methylated histone lysyl residues, as well as hydroxylation of multiple other residues. Recent work has identified roles for 2OG oxygenases in the modification of translation-associated proteins, which in some cases appears to be conserved from microorganisms through to humans. Here we give an overview of protein hydroxylation catalyzed by 2OG oxygenases, focusing on recent discoveries.

KEYWORDS:

2-oxoglutarate; chemical biology; dioxygenase; enzyme catalysis; gene expression; hydroxylase; hydroxylation; post-translational modification (PTM); protein chemical modification; protein synthesis

PMID:
26152730
PMCID:
PMC4543633
DOI:
10.1074/jbc.R115.662627
[Indexed for MEDLINE]
Free PMC Article

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