Date of Award
12-16-2015
Degree Type
Thesis
Degree Name
Master of Science (MS)
Department
Chemistry
First Advisor
Giovanni Gadda
Second Advisor
Donald Hamelberg
Third Advisor
Jun Yin
Abstract
Pseudomonas aeruginosa ᴅ-arginine dehydrogenase (PaDADH) is a flavin-dependent enzyme. The enzyme catalyzes the oxidative deamination of a broad range of ᴅ-amino acids to their corresponding imino-acids, which are non-enzymatically hydrolyzed to α-keto-acids and ammonia. A46, S45 and I335 residues are located in flexible loops, which form a flask-like substrate-binding pocket. In this study, I335, A46, and S45 were mutated to histidine, glycine, and alanine, respectively and individually, through site-directed mutagenesis, to investigate their role in binding and catalysis in PaDADH. The results showed that A46 and S45 residues participate in the optimal orientation of the substrate α-amino group and I335 modulate the active site flexibility.
DOI
https://doi.org/10.57709/7918686
Recommended Citation
Ouedraogo, Daniel and Gadda, Gioavanni, "Mechanistic Investigation of the Flavin-Neighboring Residues S45, A46 and I335 in Pseudomonas aeruginosa D-arginine Dehydrogenase." Thesis, Georgia State University, 2015.
doi: https://doi.org/10.57709/7918686