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• W2002154346 abstract "ObjectiveTo investigate the role of serine–threonine phosphorylation on the activity of human P450c17.DesignIn vitro study.SettingAcademic basic research laboratory.Patient(s)None.Intervention(s)P450c17 expression constructs with a FLAG-tag on either the C-terminus or N-terminus of the protein were generated. Human C-terminal FLAG-tagged P450c17 chromosomal DNA was subjected to site-directed mutagenesis. Serine 258 and threonine 260 each were mutated to alanine and aspartic acid. The mutant P450c17s were expressed in COS-7 cells, and the enzymatic activities were measured.Main Outcome Measure(s)17α-Hydroxylase and C17–20 lyase activities of human P450c17.Result(s)C-terminal FLAG-tagged P450c17 functioned indistinguishably from the wild-type P450c17. Mutants S258A, S258D, and T260D had significantly less 17α-hydroxylase and C17–20 lyase activities than the wild type.Conclusion(s)Adding an epitope tag to the C-terminus of the P450c17 protein does not interfere with its activities and will be a useful tool to isolate human P450c17 protein from cultured cells. Phosphorylation of serine 258 but not threonine 260 may act as a physiologic regulator of both enzymatic activities through interaction with obligatory redox partners. To investigate the role of serine–threonine phosphorylation on the activity of human P450c17. In vitro study. Academic basic research laboratory. None. P450c17 expression constructs with a FLAG-tag on either the C-terminus or N-terminus of the protein were generated. Human C-terminal FLAG-tagged P450c17 chromosomal DNA was subjected to site-directed mutagenesis. Serine 258 and threonine 260 each were mutated to alanine and aspartic acid. The mutant P450c17s were expressed in COS-7 cells, and the enzymatic activities were measured. 17α-Hydroxylase and C17–20 lyase activities of human P450c17. C-terminal FLAG-tagged P450c17 functioned indistinguishably from the wild-type P450c17. Mutants S258A, S258D, and T260D had significantly less 17α-hydroxylase and C17–20 lyase activities than the wild type. Adding an epitope tag to the C-terminus of the P450c17 protein does not interfere with its activities and will be a useful tool to isolate human P450c17 protein from cultured cells. Phosphorylation of serine 258 but not threonine 260 may act as a physiologic regulator of both enzymatic activities through interaction with obligatory redox partners." @default.
• W2002154346 created "2016-06-24" @default.
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• W2002154346 date "2006-04-01" @default.
• W2002154346 modified "2023-09-26" @default.
• W2002154346 title "Mutagenesis of putative serine–threonine phosphorylation sites proximal to Arg255 of human cytochrome P450c17 does not selectively promote its 17,20-lyase activity" @default.
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• W2002154346 doi "https://doi.org/10.1016/j.fertnstert.2005.12.011" @default.
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