ArticleThe Journal of biological chemistry2014
Catalytically relevant electrostatic interactions of cytochrome P450c17 (CYP17A1) and cytochrome b5.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Maternal exposure to biosolids reshapes chemical burden and steroidogenic pathways to promote adipogenic differentiation in a sheep model.Environment international · 2026Article
- The regulatory potential of cytochrome P450-adrenodoxin interactions: Insights toward understanding redox partner regulation in drug metabolizing enzymes.Drug metabolism and disposition: the biological fate of chemicals · 2026Review
- Mechanistic and spectroscopic characterization of human CYP17A1 in Nanodiscs.Journal of inorganic biochemistry · 2026Review
- Updates on Mechanisms of Cytochrome P450 Catalysis of Complex Steroid Oxidations.International journal of molecular sciences · 2024Review
- Tracking protein-protein interactions by NMR: conformational selection in human steroidogenic cytochrome P450 CYP17A1 induced by cytochromePhysical chemistry chemical physics : PCCP · 2024Article
- The Multienzyme Complex Nature of Dehydroepiandrosterone Sulfate Biosynthesis.International journal of molecular sciences · 2024Article
- Non-steroidal CYP17A1 Inhibitors: Discovery and Assessment.Journal of medicinal chemistry · 2023Review
- Steroid 17α-hydroxylase/17, 20-lyase (cytochrome P450 17A1).Methods in enzymology · 2023Article
- On 'Evidence for the participation of cytochrome b5 in hepatic microsomal mixed-function oxidation reactions' by Alfred Hildebrandt and Ronald W. Estabrook.Archives of biochemistry and biophysics · 2022Article
- Clinical characteristics and molecular etiology of partial 17α-hydroxylase deficiency diagnosed in 46,XX patients.Frontiers in endocrinology · 2022Article
- Progesterone receptor membrane component 1 (PGRMC1) binds and stabilizes cytochromes P450 through a heme-independent mechanism.The Journal of biological chemistry · 2021Article
- CytochromeDrug metabolism and disposition: the biological fate of chemicals · 2021Article
- Targeted RNA sequencing of adrenal zones using immunohistochemistry-guided capture of formalin-fixed paraffin-embedded tissue.Molecular and cellular endocrinology · 2021Article
- Mechanisms of Cytochrome P450-Catalyzed Oxidations.ACS catalysis · 2018Article
- Formation and Cleavage of C-C Bonds by Enzymatic Oxidation-Reduction Reactions.Chemical reviews · 2018Review
- A challenging case of primary amenorrhoea.BMJ case reports · 2018Article
- Catalytic modulation of human cytochromes P450 17A1 and P450 11B2 by phospholipid.The Journal of steroid biochemistry and molecular biology · 2018Article
- Inherent steroid 17α,20-lyase activity in defunct cytochrome P450 17A enzymes.The Journal of biological chemistry · 2018Article
- Molecular Recognition in Mitochondrial Cytochromes P450 That Catalyze the Terminal Steps of Corticosteroid Biosynthesis.Biochemistry · 2017Article
- Steroid 17-hydroxylase and 17,20-lyase deficiencies, genetic and pharmacologic.The Journal of steroid biochemistry and molecular biology · 2017Review
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6 authors.
Funding
Abstract
Two acidic residues, Glu-48 and Glu-49, of cytochrome b5 (b5) are essential for stimulating the 17,20-lyase activity of cytochrome P450c17 (CYP17A1). Substitution of Ala, Gly, Cys, or Gln for these two glutamic acid residues abrogated all capacity to stimulate 17,20-lyase activity. Mutations E49D and E48D/E49D retained 23 and 38% of wild-type activity, respectively. Using the zero-length cross-linker ethyl-3-(3-dimethylaminopropyl)carbodiimide, we obtained cross-linked heterodimers of b5 and CYP17A1, wild-type, or mutations R347K and R358K. In sharp contrast, the b5 double mutation E48G/E49G did not form cross-linked complexes with wild-type CYP17A1. Mass spectrometric analysis of the CYP17A1-b5 complexes identified two cross-linked peptide pairs as follows: CYP17A1-WT: (84)EVLIKK(89)-b5: (53)EQAGGDATENFEDVGHSTDAR(73) and CYP17A1-R347K: (341)TPTISDKNR(349)-b5: (40)FLEEHPGGEEVLR(52). Using these two sites of interaction and Glu-48/Glu-49 in b5 as constraints, protein docking calculations based on the crystal structures of the two proteins yielded a structural model of the CYP17A1-b5 complex. The appositional surfaces include Lys-88, Arg-347, and Arg-358/Arg-449 of CYP17A1, which interact with Glu-61, Glu-42, and Glu-48/Glu-49 of b5, respectively. Our data reveal the structural basis of the electrostatic interactions between these two proteins, which is critical for 17,20-lyase activity and androgen biosynthesis.
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