Cytochrome P450 BM3 E267V and Inhibition
Presentation Type
Poster
Faculty Advisor
Jaclyn Catalano
Access Type
Event
Start Date
26-4-2024 9:45 AM
End Date
26-4-2024 10:44 AM
Description
Cytochromes P450 are membrane bound heme enzymes that play a big role in detoxifying xenobiotics, cellular metabolism, and homeostasis. The particular enzyme studied is Cytochrome P450 from Bacillus Megaterium (BM-3). Two different variants of residue position 267 were tested: glutamic acid (the wild type, negatively charged) and valine (non polar and neutral). The first goal was to compare two fatty acid substrates N-palmitoylglycine (NPG) and lauric acid with both variants. The second goal was to determine the IC50 value of the inhibitor Liarizole. Our studies found that NPG was a better substrate than lauric acid for both variants. In addition, we hypothesize that Liarizole will inhibit both variants. Future studies will include testing other substrates to help determine the role of glutamic acid.
Cytochrome P450 BM3 E267V and Inhibition
Cytochromes P450 are membrane bound heme enzymes that play a big role in detoxifying xenobiotics, cellular metabolism, and homeostasis. The particular enzyme studied is Cytochrome P450 from Bacillus Megaterium (BM-3). Two different variants of residue position 267 were tested: glutamic acid (the wild type, negatively charged) and valine (non polar and neutral). The first goal was to compare two fatty acid substrates N-palmitoylglycine (NPG) and lauric acid with both variants. The second goal was to determine the IC50 value of the inhibitor Liarizole. Our studies found that NPG was a better substrate than lauric acid for both variants. In addition, we hypothesize that Liarizole will inhibit both variants. Future studies will include testing other substrates to help determine the role of glutamic acid.