Proteomics, modeling, and fluorescence assays delineate cytochrome b5 residues involved in binding and stimulation of cytochrome P450 17A1 17,20-lyase
Author:
Funder
Vanderbilt Institute of Chemical Biology, School of Medicine, Vanderbilt University
National Institutes of Health
Vanderbilt-Ingram Cancer Center
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference76 articles.
1. Cytochrome b5 as electron donor for oxy-cytochrome P-450;Noshiro;Eur. J. Biochem.,1981
2. Role of cytochrome b5 in the modulation of the enzymatic activities of cytochrome P450 17α-hydroxylase/17,20-lyase (P450 17A1);Bhatt;J. Steroid Biochem. Mol. Biol.,2017
3. Lack of electron transfer from cytochrome b5 in stimulation of catalytic activities of cytochrome P450 3A4. Characterization of a reconstituted cytochrome P450 3A4/NADPH-cytochrome P450 reductase system and studies with apo-cytochrome b5;Yamazaki;J. Biol. Chem.,1996
4. Cytochrome b5 augments the 17,20-lyase activity of human P450c17 without direct electron transfer;Auchus;J. Biol. Chem.,1998
5. Stimulation of cytochrome P450 reactions by apo-cytochrome b5: evidence against transfer of heme from cytochrome P450 3A4 to apo-cytochrome b5 or heme oxygenase;Yamazaki;J. Biol. Chem.,2001
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