3.2.2.6	D147A	site-directed mutagenesis, the mutant shows a decrease in activity compared to the wild-type enzyme	731357	
3.2.2.6	E138A	site-directed mutagenesis, the mutation causes a modest increase in the rate of NAD+ transformation which is proportional to its concentration. At 4.0 M, the rate increase is about 1.2fold and the formation of beta-1'-O-methyl ADP-ribose amounts to about 80% of the total reaction products. The observed selectivity in favor of methanolysis is similar to that of wild-type enzyme. The ADP-ribosyl cyclase activity of E138A mutant is more affected by the competing nucleophile, i.e. formation of ADP-ribose and cADPR are reduced by 75% and 90% respectively at 4.0 M methanol, the mutant shows an increase in ADP cyclization and higly reduced overall activity compared to the wild-type enzyme	731357	
3.2.2.6	E138Q	site-directed mutagenesis, in the presence of methanol, mutant E138Q efficiently catalyzes the formation of beta-1'-O-methyl ADP-ribose. But in contrast with mutant E138A, and like the wild-type enzyme, solvolysis does not affect the overall turnover rate of NAD+ indicating that the formation of the E.ADP-ribosyl intermediate is still rate limiting	731357	
3.2.2.6	E218A	site-directed mutagenesis, the mutant shows a decrease in activity compared to the wild-type enzyme	731357	
3.2.2.6	E218Q	site-directed mutagenesis, catalytic site mutant, crystal structure analysis, almost inactive mutant	732691	
3.2.2.6	E218Q	site-directed mutagenesis, the mutant shows a decrease in activity compared to the wild-type enzyme	731357	
3.2.2.6	E226D	site-directed mutagenesis, catalytic mutant	731119	
3.2.2.6	E226D	site-directed mutagenesis, inactive catalytic site mutant	731987	
3.2.2.6	E226Q	site-directed mutagenesis, catalytic mutant	731119	
3.2.2.6	E226Q	site-directed mutagenesis, inactive catalytic site mutant	731987	
3.2.2.6	E226Q	the mutation cripples enzymatic activity	714921	
3.2.2.6	K120A	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	732691	
3.2.2.6	additional information	construction of CD38/NAD+ glycohydrolase truncated for the first 31 amino acids that encompass the transmembrane and short intracellular domains	732691	
3.2.2.6	N100D	site-directed mutagenesis, N-glycoylation at the site is abolished	731119	
3.2.2.6	N164D	site-directed mutagenesis, N-glycoylation at the site is abolished	731119	
3.2.2.6	N209D	site-directed mutagenesis, N-glycoylation at the site is abolished	731119	
3.2.2.6	N219D	site-directed mutagenesis, N-glycoylation at the site is abolished	731119	
3.2.2.6	R216A	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	732691	
3.2.2.6	S185A	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	732691	
3.2.2.6	W118A	site-directed mutagenesis, the mutant shows a decrease of the catalytic rate compared to the wild-type enzyme	731357	
3.2.2.6	W118A/W181A	site-directed mutagenesis, the mutant shows a decrease of the catalytic rate which is 16fold lower than the product of the effects of the two single mutations	731357	
3.2.2.6	W118F	site-directed mutagenesis, the mutant shows a decrease in activity compared to the wild-type enzyme	731357	
3.2.2.6	W118H	site-directed mutagenesis, the mutant shows a decrease in activity compared to the wild-type enzyme	731357	
3.2.2.6	W168A	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	732691	
3.2.2.6	W181A	site-directed mutagenesis, the mutant shows a decrease of the catalytic rate and a reduced sensitivity to nicotinamide inhibition compared to the wild-type enzyme	731357	
3.2.2.6	W181F	site-directed mutagenesis, the mutant shows a decrease in activity and an increase in ADP cyclization compared to the wild-type enzyme	731357