Kinetic rationale for selectivity toward N- and C-terminal oxygen-dependent degradation domain substrates mediated by a loop region of hypoxia-inducible factor prolyl hydroxylases.

Abstract

Hydroxylation of two conserved prolyl residues in the N- and C-terminal oxygen-dependent degradation domains (NODD and CODD) of the alpha-subunit of hypoxia-inducible factor (HIF) signals for its degradation via the ubiquitin-proteasome pathway. In human cells, three prolyl hydroxylases (PHDs 1-3) belonging to the Fe(II) and 2-oxoglutarate (2OG)-dependent… (More)

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@article{Flashman2008KineticRF, title={Kinetic rationale for selectivity toward N- and C-terminal oxygen-dependent degradation domain substrates mediated by a loop region of hypoxia-inducible factor prolyl hydroxylases.}, author={Emily Flashman and Eleanor A. L. Bagg and Rasheduzzaman Chowdhury and Jasmin Mecinovi{\'c} and Christoph Loenarz and Michael A McDonough and Kirsty S. Hewitson and Christopher J. Schofield}, journal={The Journal of biological chemistry}, year={2008}, volume={283 7}, pages={3808-15} }