Glutamine amidotransferase activity of NAD+ synthetase from Mycobacterium tuberculosis depends on an amino-terminal nitrilase domain
M Bellinzoni, S Buroni, MR Pasca, P Guglierame… - Research in …, 2005 - Elsevier
NAD+ synthetase (NadE; EC 6.3. 5.1) from Mycobacterium tuberculosis utilizes both
glutamine and ammonia to catalyze NAD+ production, in contrast to the corresponding NH3-
dependent enzymes from other prokaryotes. Here we report the site-directed mutagenesis of
amino acids located in the N-terminal domain and predicted to be essential for glutamine
hydrolysis. The residues forming the putative catalytic triad (Cys176, Glu52 and Lys121)
were replaced by alanine; the mutated enzymes were expressed in the Escherichia coli …
glutamine and ammonia to catalyze NAD+ production, in contrast to the corresponding NH3-
dependent enzymes from other prokaryotes. Here we report the site-directed mutagenesis of
amino acids located in the N-terminal domain and predicted to be essential for glutamine
hydrolysis. The residues forming the putative catalytic triad (Cys176, Glu52 and Lys121)
were replaced by alanine; the mutated enzymes were expressed in the Escherichia coli …