B.Sc. University of British Columbia
Ph.D. Oregon State University
Enzymes are large macromolecules that serve as biological catalysts for an immense number of biochemical reactions. Given that enzymes catalyze reactions with a high level of stereo- and regio-specificity under mild conditions, they can serve as valuable tools for the synthesis of new drugs and other high commodity chemicals. Knowledge of enzyme structure and function can also lead to the treatment of diseases including bacterial infections, cancer and metabolic disorders. My research group is interested in unravelling the complexities of enzymatic reactions, as this knowledge can lead to advances in biotechnology and human health.
Bioengineering of Flavin-Dependent Monooxygenases
Our research group investigates acetone monooxygenase (ACMO), which preferentially catalyzes the Baeyer-Villiger oxidation of small (a)cyclic ketones to esters or lactones using molecular oxygen and reducing equivalents from NADPH.
We are specifically interested in structural features that control substrate specificity and the stability of key catalytic intermediates in ACMO and related flavin-dependent monooxygenases.
Bifunctional Ornithine Decarboxylase/Arginase
Fusobacterium nucleatum is a Gram-negative bacterium that is ubiquitous to the oral cavity. Recent research has shown that this bacterium is an opportunistic pathogen that is implicated in preterm births, colorectal cancer and periodontal disease. The organism encodes a novel bifunctional enzyme that fuses the activities of arginase and ornithine decarboxylase. The unique properties of this enzyme make it a potential therapeutic drug target to treat F. nucleatum infections. We are currently in the early stages of characterizing this novel enzyme.
Once thought to be a rarity, free-radical chemistry is becoming a more mainstream event in enzyme catalysis. Radicals are highly reactive species that enable the enzyme to perform difficult reactions with high activation energy barriers (e.g. cleavage of C-C, C-N and C-H bonds on chemically inert substrates).
We study radical chemistry mediated by coenzyme B12- and PLP-dependent aminomutases. In particular, we investigate how the protein, in concert with the two cofactors, initiates and controls radical chemistry with high fidelity.
Last reviewed 11/2/2016 1:20:37 PM
Dr. Kirsten R. Wolthers
Associate Professor, Chemistry
University of British Columbia Okanagan
Fipke Centre for Innovative Research
3247 University Way
Kelowna, BC, Canada V1V 1V7
Office: FIP 342