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Substrate Selectivity Analyses of Factor Inhibiting Hypoxia‐Inducible Factor
Author(s) -
Yang Ming,
Hardy Adam P.,
Chowdhury Rasheduzzaman,
Loik Nikita D.,
Scotti John S.,
McCullagh James S. O.,
Claridge Timothy D. W.,
McDonough Michael A.,
Ge Wei,
Schofield Christopher J.
Publication year - 2013
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201208046
Subject(s) - geminal , substrate (aquarium) , chemistry , computer science , combinatorial chemistry , stereochemistry , biochemistry , information retrieval , computational biology , biology , ecology
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).