Journal
BIOCHEMICAL SOCIETY TRANSACTIONS
Volume 32, Issue -, Pages 943-945Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BST0320943
Keywords
epidermal growth factor (EGF); hydroxylation; hypoxia; iron; 2-oxoglutarate; oxygenase
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Funding
- Biotechnology and Biological Sciences Research Council [B18672, BBS/B/07683] Funding Source: Medline
- Biotechnology and Biological Sciences Research Council [B18672, BBS/B/07683] Funding Source: researchfish
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FIH (Factor inhibiting hypoxia-inducible factor), an asparaginyl beta-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 beta-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 beta-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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