FIH (Factor inhibiting hypoxia-inducible factor), an asparaginyl β-hydroxylase belonging to the super-family of 2-oxoglutarate and Fe(II)-dependent dioxygenases, catalyses hydroxylation of Asn-803 of hypoxia-inducible factor, a transcription factor that regulates the mammalian hypoxic response. Only one other asparaginyl β-hydroxylase, which catalyses hydroxylation of both aspartyl and asparaginyl residues in EGF (epidermal growth factor)-like domains, has been characterized. In the light of recent crystal structures of FIH, we compare FIH with the EGFH (EGF β-hydroxylase) and putative asparagine/asparaginyl hydroxylases. Sequence analyses imply that EGFH does not contain the HXD/E iron-binding motif characteristic of most of the 2-oxoglutarate oxygenases.
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November 2004
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Conference Article|
October 26 2004
Factor inhibiting hypoxia-inducible factor (FIH) and other asparaginyl hydroxylases
D.E. Lancaster;
D.E. Lancaster
1Department of Chemistry and the Oxford Centre for Molecular Sciences, Chemistry Research Laboratory, Mansfield Road, Oxford OX1 3TA, U.K.
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M.A. McDonough;
M.A. McDonough
1
1Department of Chemistry and the Oxford Centre for Molecular Sciences, Chemistry Research Laboratory, Mansfield Road, Oxford OX1 3TA, U.K.
1Correspondence may be addressed to either of these authors (email christopher.schofield@chem.ox.ac.uk and michael.mcdonough@chem.ox.ac.uk).
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C.J. Schofield
C.J. Schofield
1
1Department of Chemistry and the Oxford Centre for Molecular Sciences, Chemistry Research Laboratory, Mansfield Road, Oxford OX1 3TA, U.K.
1Correspondence may be addressed to either of these authors (email christopher.schofield@chem.ox.ac.uk and michael.mcdonough@chem.ox.ac.uk).
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Biochem Soc Trans (2004) 32 (6): 943–945.
Article history
Received:
July 19 2004
Citation
D.E. Lancaster, M.A. McDonough, C.J. Schofield; Factor inhibiting hypoxia-inducible factor (FIH) and other asparaginyl hydroxylases. Biochem Soc Trans 1 November 2004; 32 (6): 943–945. doi: https://doi.org/10.1042/BST0320943
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