Date of Award:
5-2017
Document Type:
Thesis
Degree Name:
Master of Science (MS)
Department:
Chemistry and Biochemistry
Department name when degree awarded
Chemistry
Committee Chair(s)
Alvan C. Hengge
Committee
Alvan C. Hengge
Committee
Sean Johnson
Committee
Cheng-Wei Tom Chang
Abstract
Protein-tyrosine phosphatases (PTPs) catalyze the hydrolysis of phosphorylated tyrosines by a 2-step mechanism involving nucleophilic attack by cysteine and general acid catalysis by aspartic acid. In most PTPs the aspartic acid resides on a flexible protein loop, consisting of about a dozen residues, called the WPD loop. PTP catalysis rates span several orders of magnitude, and differences in WPD loop dynamics have recently been show to correlate with the rate of enzymatic catalysis. The rate of WPD loop motion could possibly be related to a widely conserved tryptophan residue on the WPD loop. Therefore, point mutants were made in PTP1B (a human PTP) to the conserved tryptophan residue and their effects on catalytic rate and chemical reaction were studied. The results of these studies are presented in this thesis.
Checksum
f43fecbff553e4065e06c1751ea028a0
Recommended Citation
Richan, Teisha, "Conservative Tryptophan Mutations in Protein Tyrosine Phosphatase PTP1B and its Effect on Catalytic Rate and Chemical Reaction" (2017). All Graduate Theses and Dissertations, Spring 1920 to Summer 2023. 5584.
https://digitalcommons.usu.edu/etd/5584
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