Describe your undergraduate research or creative project:
The prenyltransferase CdpNPT, a member of the DMATS superfamily, was investigated as a tool for chemoenzymatic synthesis of prenylated secondary metabolites. Site-directed mutagenesis was performed to generate mutant enzymes that had expansions of the enzyme’s hydrophobic binding site. Pseudo-first order kinetic studies were then performed with all the mutant enzymes and a variety of non-native synthetic alkyl donors in order to determine the effects of the mutations on the enzyme’s promiscuity towards alkyl donors. From these results, three major criteria were found to determine CdpNPT’s affinity for an alkyl donor: carbocation stability, steric hindrance, and hydrophobic interaction within the active site. The mutations performed here not only expanded the promiscuity of CdpNPT, but also altered its regiochemistry, creating a wider range of prenylated products than the wild-type enzyme was able to.
Awards and/or presentations:
Schene, Miranda. "Rational Design and Substrate Specificity Study of Prenyltransferase CdpNPT." Curiosity to Creativity Spring Symposium, 25 April 2018, Oklahoma Memorial Union, Norman, OK