Substrate Positioning by Gln239 Stimulates Turnover in Factor Inhibiting HIF, an αKG-Dependent Hydroxylase
Author:
Affiliation:
1. Department of Chemistry, University of Massachusetts at Amherst, Amherst, Massachusetts 01003, United States
2. School of Natural Science, Hampshire College, Amherst, Massachusetts 01002, United States
Funder
National Institute of General Medical Sciences
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi500703s
Reference60 articles.
1. Fe(II)/α-Ketoglutarate-Dependent Hydroxylases and Related Enzymes
2. The diverse and pervasive chemistries of the α-keto acid dependent enzymes
3. Targeting of HIF-α to the von Hippel-Lindau Ubiquitylation Complex by O 2 -Regulated Prolyl Hydroxylation
4. Asparagine Hydroxylation of the HIF Transactivation Domain: A Hypoxic Switch
5. Reversal of DNA alkylation damage by two human dioxygenases
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1. Dynamic Domain Links Substrate Binding and Catalysis in the Factor-Inhibiting-HIF-1;Biochemistry;2023-08-01
2. The facial triad in the α-ketoglutarate dependent oxygenase FIH: A role for sterics in linking substrate binding to O2 activation;Journal of Inorganic Biochemistry;2017-01
3. Substrate Promotes Productive Gas Binding in the α-Ketoglutarate-Dependent Oxygenase FIH;Biochemistry;2016-01-05
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