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Substrate Selectivity Analyses of Factor Inhibiting Hypoxia-Inducible Factor

DOI: 10.1002/anie.201208046 DOI Help
PMID: 23296631 PMID Help

Authors: Ming Yang (University of Oxford) , Adam P. Hardy (University of Oxford) , Rasheduzzaman Chowdhury (Department of Chemistry, University of Oxford) , Nikita D. Loik (University of Oxford) , John Scotti (University of Oxford) , James S. O. Mccullagh (University of Oxford) , Timothy D. W. Claridge (University of Oxford) , Michael A. Mcdonough (University of Oxford) , Wei Ge (University of Oxford) , Christopher J. Schofield (University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Angewandte Chemie International Edition

State: Published (Approved)
Published: January 2013

Abstract: 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 ?-position, which in addition to Asn, Asp, and His include Leu and Ser residues. The Ser substrate is oxidized to an epimeric ?-geminal diol product (see picture).

Journal Keywords: Ankyrins; Binding; Biocatalysis; Catalytic; Hydroxylation; Hypoxia-Inducible; Magnetic; Molecular; Peptides; Spectrometry; Mass; Matrix-Assisted; Substrate Specificity

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I03-Macromolecular Crystallography