Date of Award
5-2022
Document Type
Thesis
Degree Name
Master of Science (MS)
College/School
College of Science and Mathematics
Department/Program
Chemistry and Biochemistry
Thesis Sponsor/Dissertation Chair/Project Chair
Nina Goodey
Committee Member
David Konas
Committee Member
Jaclyn Catalano
Abstract
Mycobacterium tuberculosis is a bacterium that affects the lungs and causes tuberculosis, infecting over 10 million people worldwide each year. Owing to the organism’s evolving drug resistance, existing antibiotics no longer combat the disease. The need to discover new drug targets has never been greater. Previous findings suggest that the protein IGPS (indole-3-glycerol phosphate synthase) in M. tuberculosis (MtIGPS) may be a target in the treatment of the disease. MtIGPS catalyzes the fourth step in the tryptophan biosynthetic process. The ability to create their own tryptophan is a major advantage that many bacteria have. The role of E168, in the active site of MtIGPS was investigated. Wildtype and E168D MtIGPS proteins were then purified and KM values were determined to be 6.9 ± 1.4 μM and 26 ± 3 μM, respectively. After this, Wildtype and E168D kcat values were determined to be 0.022 ± 0.002 s-1 and 0.011 ± 0.001 s-1, respectively. An enhanced understanding of ligand binding and catalysis in the MtIGPS active site will aid in the design of MtIGPS inhibitors.
File Format
Recommended Citation
Booter, Hedda, "Role of E168D in M. tuberculosis IGPS Catalysis" (2022). Theses, Dissertations and Culminating Projects. 1055.
https://digitalcommons.montclair.edu/etd/1055