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...

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Bibliographic Details
Main Authors: Yang, M, Hardy, A, Chowdhury, R, Loik, N, Scotti, J, McCullagh, J, Claridge, T, McDonough, M, Ge, W, Schofield, C
Format: Journal article
Language:English
Published: 2013
Description
Summary: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 oxidized to an epimeric β-geminal diol product (see picture). Copyright © 2013 WILEY-VCH Verlag GmbH and Co. KGaA, Weinheim.