Transglutaminase is a highly versatile enzyme that allows the formation of amide bonds between amino compounds and glutamine on the surface of a protein. Although the exact mechanism that explains the selectivity of this enzyme for specific glutamines is still poorly understood, this enzyme is already used in several industries, such as the food industry.  Subsequent studies on transglutaminase-reactive mutants may provide important information on the selectivity of this enzyme.

•    B.Sc. 2019, (Biochemistry, Molecular Medicine), Department of Biochemistry, University of Montreal

•    09/2018 -- 12/2018: Study of protein evolution using TEM-1 β-lactamase and variants as models.

•    01/2019 -- 05/2019:  Kinetics characterization of Cytochrome P450 and variants of interest for      industrial purposes in flow biocatalysis.

•   Part of the Advanced Protein Engineering Training, Internships, Courses, and Exhibition (APRENTICE) program, a Collaborative Research and Training Experience (CREATE) supported by the Natural Science and Engineering Research Council of Canada (NSERC).

• Deweid, L.*, H.-Parisien, A.*, Lafontaine, K., Rochet, L.N.C., Kolmar, H. and Pelletier, J.N. (2020) Glutamine-walking: creating reactive substrates for transglutaminase-mediated protein labelling. Met. Enzymol., 644:121-148. (*equal contribution)

• Rousseau, O., Ebert, M.C., Quaglia, D., Fendri, A., H.-Parisien, A., Besna, J. N., Iyathurai, S. and Pelletier, J.N. (2019) Indigo Formation and Rapid NADPH Consumption Provide Robust Prediction of Raspberry Ketone Synthesis by Engineered Cytochrome P450 BM3. ChemCatChem, 12(3): 837-845.