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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Veröffentlicht in:	Angewandte Chemie International Edition 2013-02, Vol.52 (6), p.1700-1704
Hauptverfasser:	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.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence amino acids Ankyrins - analysis Ankyrins - chemistry Binding Sites Biocatalysis Biochemistry Catalytic Domain Crystallography Diols enzymes Hydroxylation Hypoxia-Inducible Factor 1 - antagonists & inhibitors Hypoxia-Inducible Factor 1 - metabolism Magnetic Resonance Spectroscopy Molecular Sequence Data oxidation oxygenase Peptides - metabolism Pictures Residues Selectivity Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Substrate Specificity
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Zusammenfassung:	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).
ISSN:	1433-7851 1521-3773
DOI:	10.1002/anie.201208046