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Name: Mary Anderson, PhD
Title: Associate Professor
Department: Chemistry & Biochemistry
Phone: 940-898-2564    
Email address:
Description of research activities: Dr. Anderson's group recent studies have focused on the enzymology and structure-function relationships of the enzymes of GSH biosynthesis, g-glutamylcysteine synthetase and most especially on GSH synthetase. She and her group were the first to clone and express GSH synthetase and have optimized its expression and purification using a bacterial system. Their research was the first to show that the rat and the human enzyme display negative cooperativity with respect to the g-glutamylcysteine substrate, but not toward the other substrates, ATP or glycine. They have prepared a number of site-directed mutant enzymes, and now are studying the effects of these changes on activity and function of GSH synthetase. Other current GSH synthetase projects include studies of its ATP binding site and its catalytic mechanism (obtaining a kinetic model of reaction order and examining the molecular basis of negative cooperativity). Also, GSH synthetase has several loop structures at/near the substrate binding sites, and Dr. Anderson plans to examine the role that loop-loop and loop-substrate interactions have in enzyme function. They are also working on understanding the nature of the patient GSH synthetase deficiencies. Most recently, Dr. Anderson's group has embarked on molecular modeling studies; these modeling studies help explain their experimental findings and help guide their future studies.
Key Words: Biochemistry, enzymes, antioxidant, glutathione

page last updated 5/2/2016 9:37 AM