ArticleBiochemistry2007
Unusual regioselectivity and active site topology of human cytochrome P450 2J2.
Article in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 58 citations in OpenAlex.
- Construction of a CYP2J2-Template System and Its Application for Ligand Metabolism Prediction.Food safety (Tokyo, Japan) · 2024Article
- Elucidating the Mechanism of Metabolism of Cannabichromene by Human Cytochrome P450s.Journal of natural products · 2024Article
- Pharmacogenetic Variation in Neanderthals and Denisovans and Implications for Human Health and Response to Medications.Genome biology and evolution · 2023Article
- Molecular determinant of substrate binding and specificity of cytochrome P450 2J2.Scientific reports · 2020Article
- CYP2J2 Molecular Recognition: A New Axis for Therapeutic Design.Pharmacology & therapeutics · 2020Review
- Molecular dynamics simulations of the interaction of wild type and mutant human CYP2J2 with polyunsaturated fatty acids.BMC research notes · 2019Article
- Biochemical Characterization of the α-l-RhamnosidaseACS omega · 2019Article
- Role of Arginine 117 in Substrate Recognition by Human Cytochrome P450 2J2.International journal of molecular sciences · 2018Article
- Arachidonic Acid Metabolism by Human Cardiovascular CYP2J2 Is Modulated by Doxorubicin.Biochemistry · 2017Article
- Heme Modification Contributes to the Mechanism-Based Inactivation of Human Cytochrome P450 2J2 by Two Terminal Acetylenic Compounds.Drug metabolism and disposition: the biological fate of chemicals · 2017Article
- Cytochrome P450 2U1, a very peculiar member of the human P450s family.Cellular and molecular life sciences : CMLS · 2017Review
- Computational modelling of the binding of arachidonic acid to the human monooxygenase CYP2J2.Journal of molecular modeling · 2016Article
- Incorporation of charged residues in the CYP2J2 F-G loop disrupts CYP2J2-lipid bilayer interactions.Biochimica et biophysica acta · 2015Article
- Structural basis for cooperative binding of azoles to CYP2E1 as interpreted through guided molecular dynamics simulations.Journal of molecular graphics & modelling · 2015Article
- A comprehensive test set of epoxidation rate constants for iron(iv)-oxo porphyrin cation radical complexes.Chemical science · 2015Article
- Differences and comparisons of the properties and reactivities of iron(III)-hydroperoxo complexes with saturated coordination sphere.Chemistry (Weinheim an der Bergstrasse, Germany) · 2015Article
- Endocannabinoids anandamide and 2-arachidonoylglycerol are substrates for human CYP2J2 epoxygenase.The Journal of pharmacology and experimental therapeutics · 2014Article
- Structural control of cytochrome P450-catalyzed ω-hydroxylation.Archives of biochemistry and biophysics · 2011Review
- Structural and biochemical characterization of Mycobacterium tuberculosis CYP142: evidence for multiple cholesterol 27-hydroxylase activities in a human pathogen.The Journal of biological chemistry · 2010Article
- The Structure of Mycobacterium tuberculosis CYP125: molecular basis for cholesterol binding in a P450 needed for host infection.The Journal of biological chemistry · 2009Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
The oxidation of six derivatives of terfenadone by recombinant human CYP2J2 (CYP = cytochrome P450) was studied by high-performance liquid chromatography coupled to mass spectrometry (MS) using tandem MS techniques and by 1H NMR spectroscopy. CYP2J2 exhibited a surprising regioselectivity in favor of the hydroxylation of the substrate terminal chain at the weakly reactive homobenzylic position. In contrast, hydroxylation of the same substrates by CYP3A4 mainly occurred on the most chemically reactive sites of the substrates (N-oxidation and benzylic hydroxylation). A 3D homology model of CYP2J2 was constructed using recently published structures of CYP2A6, CYP2B4, CYP2C8, CYP2C9, and CYP2D6 as templates. In contrast with other CYP2 structures, it revealed an active site cavity with a severely restricted access of substrates to the heme through a narrow hydrophobic channel. Dynamic docking of terfenadone derivatives in the CYP2J2 active site allowed one to interpret the unexpected regioselectivity of the hydroxylation of these substrates by CYP2J2, which is mainly based on this restricted access to the iron. The structural features that have been found to be important for recognition of substrates or inhibitors by CYP2J2 were also interpreted on the basis of CYP2J2-substrate interactions in this model.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.