Factor inhibiting hypoxia-inducible factor (FIH) and other asparaginyl hydroxylases.

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. O...

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المؤلفون الرئيسيون: Lancaster, D, McDonough, M, Schofield, C
التنسيق: Journal article
اللغة:English
منشور في: 2004
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author Lancaster, D
McDonough, M
Schofield, C
author_facet Lancaster, D
McDonough, M
Schofield, C
author_sort Lancaster, D
collection OXFORD
description 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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spelling oxford-uuid:cedf0bd7-764c-41b9-a5fa-7a3fa88e39022022-03-27T07:38:27ZFactor inhibiting hypoxia-inducible factor (FIH) and other asparaginyl hydroxylases.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:cedf0bd7-764c-41b9-a5fa-7a3fa88e3902EnglishSymplectic Elements at Oxford2004Lancaster, DMcDonough, MSchofield, CFIH (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.
spellingShingle Lancaster, D
McDonough, M
Schofield, C
Factor inhibiting hypoxia-inducible factor (FIH) and other asparaginyl hydroxylases.
title Factor inhibiting hypoxia-inducible factor (FIH) and other asparaginyl hydroxylases.
title_full Factor inhibiting hypoxia-inducible factor (FIH) and other asparaginyl hydroxylases.
title_fullStr Factor inhibiting hypoxia-inducible factor (FIH) and other asparaginyl hydroxylases.
title_full_unstemmed Factor inhibiting hypoxia-inducible factor (FIH) and other asparaginyl hydroxylases.
title_short Factor inhibiting hypoxia-inducible factor (FIH) and other asparaginyl hydroxylases.
title_sort factor inhibiting hypoxia inducible factor fih and other asparaginyl hydroxylases
work_keys_str_mv AT lancasterd factorinhibitinghypoxiainduciblefactorfihandotherasparaginylhydroxylases
AT mcdonoughm factorinhibitinghypoxiainduciblefactorfihandotherasparaginylhydroxylases
AT schofieldc factorinhibitinghypoxiainduciblefactorfihandotherasparaginylhydroxylases