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.

@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}
}
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 oxygenase family catalyze prolyl hydroxylation with differing selectivity for CODD and NODD. Sequence analysis of the catalytic domains of… CONTINUE READING

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