Article
Structural and biochemical studies on the role of active site Thr166 and Asp236 in the catalytic function of D-Serine deaminase from Salmonella typhimurium.
Biochemical and biophysical research communications - 26 Sept 2018
Deka Geeta, Bharath Sakshibeedu R, Savithri Handanhal Subbarao, Murthy Mathur Ramabhadrashastry Narasimha
Abstract excerpt
D-Serine deaminase (DSD) degrades D-Ser to pyruvate and ammonia. Uropathogenic bacteria survive in the toxic D-Ser containing mammalian urine because of DSD activity. The crystal structure of the apo form of Salmonella typhimurium DSD (StDSD) has been reported earlier. In the present work, we have investigated the role of two active site residues, Thr166 and Asp236 by site directed mutagenesis (T166A and D236L)....
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