Cytochromes P450s are essential enzymes in all living things that catalyze the oxidation of substrates related to steroid synthesis and detoxification of xenobiotics. Recently, P450s have been investigated as drug targets for anticancer prodrugs (to be activated by P450 only in cancer cells). Cytochrome P450 2S1 (CYP2S1) has been shown to be overexpressed in certain cancer cells and has been investigated as a prodrug target. CYP2S1, unlike most known cytochrome P450s, has only been shown to catalyze the reduction of substrates. It is not known why the chemistry of CYP2S1 is different from the rest of P450s. Our hypothesis is that specific amino acids near the heme may contribute to the unique chemistry of this enzyme. Current investigation involves mutants of the well-studied P450 BM-3 to mimic the chemistry of CYP2S1. We tested different structured substrates to observe enzymatic activity when glutamic acid is replaced with a methionine at position 270 in the oxygen binding pocket. The mutation did not alter the binding of the substrate but the catalysis was inhibited. This result supports our hypothesis that the glutamic acid is important for oxidation of the substrate.

Comparing CYP2S1 and CYP102A1: Factors that influence the chemistry of CYP2S1

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.