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• W2023442875 startingPage "1066" @default.
• W2023442875 abstract "Mouse CYP2C38 and CYP2C39 are two closely related enzymes with 91.8% sequence identity. But they exhibit different substrate binding features. In this study, three-dimensional models of CYP2C38 and CYP2C39 were constructed using X-ray crystal structure of human CYP2C8 as the template based on homology modeling methods and molecular dynamics simulations. Tolbutamide as the common substrate of CYP2C38 and CYP2C39 was docked into them and positioned in their active sites with different orientation. All-trans retinoic acid (atRA) is a specific substrate for CYP2C39 and not catalyzed by CYP2C38. By comparison of active site architectures between CYP2C38 and CYP2C39, the possible reasons affecting their substrate binding were proposed. In addition, Arg241, Glu300, Leu366 and Leu476 are identified as critical residue for substrates binding." @default.
• W2023442875 created "2016-06-24" @default.
• W2023442875 creator A5007844508 @default.
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• W2023442875 date "2009-07-01" @default.
• W2023442875 modified "2023-10-18" @default.
• W2023442875 title "A comparative analysis of binding sites between mouse CYP2C38 and CYP2C39 based on homology modeling, molecular dynamics simulation and docking studies" @default.
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• W2023442875 doi "https://doi.org/10.1016/j.bbapap.2009.03.021" @default.
• W2023442875 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19358898" @default.
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