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- W4377029172 abstract "<b>Abstract ID 26055</b> <b>Poster Board 580</b> Cytochrome P450 enzymes (CYPs) are responsible for a wide array of reactions in mammalian and bacterial cells, including hormone synthesis, steroidogenesis, and drug metabolism. In particular, we are focused on CYPs involved in vitamin D metabolism. Mammalian vitamin D-metabolizing CYPs like CYP2R1 and CYP27B1 display a narrow substrate specificity, hydroxylating vitamin D at one position. However, certain bacterial CYPs reportedly display a broader specificity and are capable of hydroxylating multiple vitamin D substrates at different positions. In particular, CYP107 from the soil organism <i>Sebekia benihana</i> has been reported to carry out hydroxylations at both the carbon-25 and the 1? positions of the hormone precursor cholecalciferol, thus combining CYP2R1 and CYP27B1 functions into a single enzyme. Our objective is to investigate structure and function in CYP107 as a way of understanding the conservation of vitamin D recognition in both bacterial and mammalian enzymes. We have successfully expressed and purified CYP107 in <i>E. coli</i> and have collected absorbance binding data with vitamin D compounds. Under low salt conditions, alfacalcidol (1α-OH vitamin D) exhibits tight binding to CYP107 as a type-I ligand. Interestingly, the spin state of the heme displays salt sensitivity that is independent of ligand, with slow interconversion between high-spin (390nm) at high salt and low-spin (420 nm) at low salt. Future work will combine mutagenesis guided by mammalian substrate-CYP interactions, 1D and 2D NMR to investigate structure, and functional assays to monitor function of the protein and its mutants. This work will help elucidate the structural basis of functional conservation of CYPs across bacteria and mammals, providing insight into important active site residues and active site morphology on enzyme specificity for vitamin D." @default.
- W4377029172 created "2023-05-19" @default.
- W4377029172 creator A5041251048 @default.
- W4377029172 creator A5076488776 @default.
- W4377029172 date "2023-05-18" @default.
- W4377029172 modified "2023-09-29" @default.
- W4377029172 title "Characterization of a novel bifunctional cytochrome P450 enzyme CYP107 from bacterium<i>Sebekia benihana</i>" @default.
- W4377029172 doi "https://doi.org/10.1124/jpet.122.260550" @default.
- W4377029172 hasPublicationYear "2023" @default.
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