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.
| Identifer | oai:union.ndltd.org:GEORGIA/oai:scholarworks.gsu.edu:chemistry_theses-1083 |
| Date | 16 December 2015 |
| Creators | Ouedraogo, Daniel, Gadda, Gioavanni |
| Publisher | ScholarWorks @ Georgia State University |
| Source Sets | Georgia State University |
| Detected Language | English |
| Type | text |
| Format | application/pdf |
| Source | Chemistry Theses |
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