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- W1978705055 abstract "Cytochrome P450 3A4 (CYP3A4), a major member of cytochrome P450 isoenzymes, metabolizes the majority of steroids in 6β-position. For the purpose of determining requisite structural features of a series of structurally related steroids for CYP3A4-mediated metabolism, three-dimensional pharmacophore modeling as well as electrotopological state map were conducted for 15 steroids. Though prior studies speculated that the chemical reactivity of the allylic 6β-position might have a greater influence on CYP3A4 selective 6-hydroxylation than steric constraints in the enzyme, our results reveal that for CYP3A4 steroidal substrates, it is not the chemical reactivity of atoms at 6β-site, but the pharmacophoric features, i.e. the two hydrophobic rings together with two H-bond donors, that act as the key factors responsible for determining the CYP3A4 selective 6-hydroxylation of steroids." @default.
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- W1978705055 date "2004-11-01" @default.
- W1978705055 modified "2023-10-11" @default.
- W1978705055 title "Structural determinants of steroids for cytochrome P450 3A4-mediated metabolism" @default.
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- W1978705055 doi "https://doi.org/10.1016/j.theochem.2004.09.013" @default.
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