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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 oxygenase family catalyze prolyl hydroxylation with differing selectivity for CODD and NODD. Sequence analysis of the catalytic domains of ...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.m707411200

Authors


Flashman, E More by this author
Chowdhury, R More by this author
Mecinović, J More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Organic Chemistry
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Journal:
The Journal of biological chemistry
Volume:
283
Issue:
7
Pages:
3808-3815
Publication date:
2008-02-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:b1c3959f-027c-4d39-a399-7112a3b56630
Source identifiers:
34069
Local pid:
pubs:34069

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