Date of Award
6-4-2021
Document Type
Thesis
Degree Name
Master of Science (MS)
Department
Chemistry
First Advisor
Shanzhi Wang
Abstract
Staphylococcus aureus 5’-methylthioadenosine/S-adenosylhomocysteine nucleosidase (SaMTAN), a multiple substrate-specific enzyme that catalyzes the irreversible hydrolytic reaction by cleaving the glycosidic bond in different adenosine based metabolites and plays a key role in biofilm production regulated by bacterial quorum sensing (Mishra & Ronning, 2012). The reaction mechanism of SaMTAN has been suggested to be acid-base catalyzed hydrolysis. The active site of SaMTAN has five amino acid residues that are candidates for the general acid residues or the general base residues. It has been suggested that Glutamic acid 11, 171 and 173 (E11,E171 and E173) may play as the general base while Aspartic acid 196 (D196) or Serine 195 (S195) acts as the general acid. The role of active site residues was investigated by site-directed mutagenesis and steady-state kinetic analysis. The enzymatic assays performed on each mutant showed reduced catalytic activity of 2-3 orders of magnitudes, which suggests that the selected residues play a strong role in the reaction of the enzyme.
Recommended Citation
Karn, Kumari Vaijayanti, "Assessment of the Chemical Mechanism of Staphylococcus aureus 5’-Methylthioadenosine/S-Adenosylhomocysteine Nucleosidase, a Novel Target for Drug Design" (2021). Theses and Dissertations. 1011.
https://research.ualr.edu/etd/1011
