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

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

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 subfami...

Disgrifiad llawn

Manylion Llyfryddiaeth
Prif Awduron:	Mantri, M, Loik, N, Hamed, R, Claridge, T, McCullagh, J, Schofield, C
Fformat:	Journal article
Iaith:	English
Cyhoeddwyd:	2011

Eitemau Tebyg

Autocatalysed oxidative modifications to 2-oxoglutarate dependent oxygenases
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Autocatalysed oxidative modifications to 2-oxoglutarate dependent oxygenases
gan: Mantri, M, et al.
Cyhoeddwyd: (2012)

Autocatalysed oxidative modifications to 2-oxoglutarate dependent oxygenases.
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Non-enzymatic chemistry enables 2-hydroxyglutarate-mediated activation of 2-oxoglutarate oxygenases.
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2-oxoglutarate-dependent oxygenases
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Biochemical and structural investigations clarify the substrate selectivity of the 2-oxoglutarate oxygenase JMJD6.
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Structural analysis of the 2-oxoglutarate binding site of the circadian rhythm linked oxygenase JMJD5
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Inhibition of 2-oxoglutarate dependent oxygenases.
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The broad spectrum 2-oxoglutarate oxygenase inhibitor N-oxalylglycine is present in rhubarb and spinach leaves
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Crystal structure of the 2-oxoglutarate- and Fe(II)-dependent lysyl hydroxylase JMJD6.
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Crystal Structure of the 2-Oxoglutarate- and Fe(II)-Dependent Lysyl Hydroxylase JMJD6.
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Mechanistic studies on 2-oxoglutarate dependent oxygenases
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Inhibition of JMJD6 by 2-oxoglutarate mimics
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Structural studies on human 2-oxoglutarate dependent oxygenases.
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Self-hydroxylation of the splicing factor lysyl hydroxylase, JMJD6
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A fluorescence-based assay for 2-oxoglutarate-dependent oxygenases.
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Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes.
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Crystallographic studies on 2-oxoglutarate dependent oxygenases
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Mechanistic studies on 2-oxoglutarate dependent oxygenases
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Expanding chemical biology of 2-oxoglutarate oxygenases.
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Reducing agent-mediated nonenzymatic conversion of 2‐oxoglutarate to succinate: implications for oxygenase assays
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The role of iron and 2-oxoglutarate oxygenases in signalling.
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Exploring links between 2-oxoglutarate-dependent oxygenases and Alzheimer's disease
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Functional and inhibition studies on 2-oxoglutarate-dependent oxygenases
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Studies on deacetoxycephalosporin C synthase support a consensus mechanism for 2-oxoglutarate dependent oxygenases.
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Mechanistic studies on the application of DNA aptamers as inhibitors of 2-oxoglutarate-dependent oxygenases.
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Reporter ligand NMR screening method for 2-oxoglutarate oxygenase inhibitors.
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Structure of proline 3-hydroxylase. Evolution of the family of 2-oxoglutarate dependent oxygenases.
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Procollagen-lysine 2-oxoglutarate 5-dioxygenases are responsible for 5R-hydroxylysine modification of therapeutic T-cell bispecific monoclonal antibodies produced by Chinese hamster ovary cells
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Inhibitor scaffolds for 2-oxoglutarate-dependent histone lysine demethylases.
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Inhibitor scaffolds for 2-oxoglutarate-dependent histone lysine demethylases.
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Identification of inhibitors for a family of human oxoglutarate-dependent oxygenases
gan: Nowak, R
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NMR studies on 2-oxoglutarate oxygenases
gan: Leung, IKH
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2-Oxoglutarate oxygenases are inhibited by a range of transition metals.
gan: Sekirnik, R, et al.
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Investigations on the oxygen dependence of a 2-oxoglutarate histone demethylase.
gan: Sánchez-Fernández, E, et al.
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Hydroxylysine glycosides of corneal collagen
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The potential of 2-oxoglutarate oxygenases acting on nucleic acids as therapeutic targets
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The potential of 2-oxoglutarate oxygenases acting on nucleic acids as therapeutic targets
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Physiological and biochemical aspects of hydroxylations and demethylations catalyzed by human 2-oxoglutarate oxygenases.
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Fluorinated derivatives of pyridine-2,4-dicarboxylate are potent inhibitors of human 2-oxoglutarate dependent oxygenases
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