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• W2316282170 abstract "Many cytochrome P450 enzymes (CYPs) exhibit allosteric behavior reflecting a complex ligand-binding process involving numerous factors: conformational selection, protein–protein interactions, substrate/effector/protein structure, and multiple-ligand binding. The interplay of CYP plasticity and rigidity contributes to substrate/product selectivity and to allosterism. Detailed evidence describing how protein motion modulates product selectivity is incomplete as are descriptions of effector-induced modulation of substrate dynamics. Our intent was to discover details of allosteric behavior and CYP3A4 flexibility and rigidity by investigating substrate motion using low-molecular weight ligands. Steady state kinetics and product ratios were measured for oxidation of m-xylene-2H3 and p-xylene; intramolecular isotope effects were measured for m-xylene-2H3 oxidation as a function of m-xylene-2H3 and p-xylene concentration. Biphasic kinetic plots indicated homotropic cooperative behavior with xylene isomers. Selectivity for aromatic hydroxylation over benzylic hydroxylation of m-xylene-2H3 supports a model in which the region near the CYP3A4 active oxidizing species limits substrate dynamics. p-Xylene impedes the motion of m-xylene-2H3 substrates that have access to the active oxidizing species: (kH/kD)obs values for m-xylene-2H3 decreased with p-xylene concentration. m-Xylene-2H3 and p-xylene do not have simultaneous access to the active oxidizing species: deuterium-labeled and unlabeled p-xylene exhibited similar effects on the (kH/kD)obs values for m-xylene-2H3 oxidation. p-Xylene and m-xylene-2H3 bind at different sites: m-xylene-2H3 oxidation rates and product selectivity were consistent across the p-xylene concentration range. Overall, this study indicates that the intramolecular isotope effect experimental design provides a unique opportunity to investigate allosteric mechanisms as it provides information about substrate motion when the enzyme is primed to oxidize substrates." @default.
• W2316282170 created "2016-06-24" @default.
• W2316282170 creator A5003816194 @default.
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• W2316282170 date "2014-02-06" @default.
• W2316282170 modified "2023-10-18" @default.
• W2316282170 title "Allosteric Modulation of Substrate Motion in Cytochrome P450 3A4-Mediated Xylene Oxidation" @default.
• W2316282170 cites W1493176169 @default.
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• W2316282170 cites W1676611497 @default.
• W2316282170 cites W1964858323 @default.
• W2316282170 cites W1969158793 @default.
• W2316282170 cites W1974543768 @default.
• W2316282170 cites W1975206909 @default.
• W2316282170 cites W1976582335 @default.
• W2316282170 cites W1982342550 @default.
• W2316282170 cites W1982736602 @default.
• W2316282170 cites W1984713897 @default.
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• W2316282170 cites W1989250130 @default.
• W2316282170 cites W1992475241 @default.
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• W2316282170 cites W2044793333 @default.
• W2316282170 cites W2046984971 @default.
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• W2316282170 doi "https://doi.org/10.1021/bi401472p" @default.
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