Substrate selectivity analyses of factor inhibiting hypoxia-inducible factor.
Substrate specificity: Biochemical and crystallographic analyses reveal the hypoxia-inducible factor hydroxylase (FIH) as being promiscuous with respect to the residues that it can hydroxylate in β-position, which in addition to Asn, Asp, and His include Leu and Ser residues. The Ser substrate is ox...
المؤلفون الرئيسيون: | Yang, M, Hardy, A, Chowdhury, R, Loik, N, Scotti, J, McCullagh, J, Claridge, T, McDonough, M, Ge, W, Schofield, C |
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التنسيق: | Journal article |
اللغة: | English |
منشور في: |
2013
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مواد مشابهة
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Investigating the contribution of the active site environment to the slow reaction of hypoxia-inducible factor prolyl hydroxylase domain 2 with oxygen.
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Factor inhibiting hypoxia-inducible factor (FIH) and other asparaginyl hydroxylases.
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Disruption of dimerization and substrate phosphorylation inhibit factor inhibiting hypoxia-inducible factor (FIH) activity.
حسب: Lancaster, D, وآخرون
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Factor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domains.
حسب: Yang, M, وآخرون
منشور في: (2011) -
Selective inhibition of factor inhibiting hypoxia-inducible factor.
حسب: McDonough, M, وآخرون
منشور في: (2005)