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Protein Hydroxylation Catalyzed by 2-Oxoglutarate-dependent Oxygenases.

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(?)-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.

SUBMITTER: Markolovic S

PROVIDER: S-EPMC4543633 | biostudies-literature | 2015 Aug

REPOSITORIES: biostudies-literature

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Protein Hydroxylation Catalyzed by 2-Oxoglutarate-dependent Oxygenases.

Markolovic Suzana S Wilkins Sarah E SE Schofield Christopher J CJ

The Journal of biological chemistry 20150707 34

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 ot ...[more]

PMID: 26152730

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