3.6.1.17	E103Q	turnover-number for hydrolysis of Ap4A is 3.2% of that of the wild-type enzyme, KM-value is 66% of the wild-type value	656173	
3.6.1.17	E122Q	fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys. KM-value is 20% of the wild-type value, turnover-number is 50% of the wild-type value. 2.3fold reduction in sensitivity to fluoride	654489	
3.6.1.17	E125Q	fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser. KM-value is 0.7% of the wild-type value, turnover-number is 56% of the wild-type value. Cleavage of (2'-pdA)AppppA to produce ATP and 2'-deoxyadenylated AMP rather than 2'-deoxyadenylated ATP + AMP as with wild-type enzyme, the ratio of ATP released is increased compared to wild-type. 83fold reduction in sensitivity to fluoride	654489	
3.6.1.17	E52Q	turnover-number for hydrolysis of Ap4A is 0.02% of that of the wild-type enzyme, KM-value is 60% of the wild-type value	656173	
3.6.1.17	E55Q	fusion protein containing and N-terminal extension of Gly-Pro-Leu-Gly-Ser. KM-value is 4.8% of the wild-type value, turnover-number is 0.01% of the wild-type value. Activity with (2'-pdA)AppppA is to low to be detected. More than 330fold reduction in sensitivity to fluoride	654489	
3.6.1.17	E56Q	turnover-number for hydrolysis of Ap4A is 0.001% of that of the wild-type enzyme, KM-value is 90% of the wild-type value	656173	
3.6.1.17	E58A	crystallization data	733257	
3.6.1.17	E58D	fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys. KM-value is 38.4% of the wild-type value, turnover-number is 9% of the wild-type value. Cleavage of (2'-pdA)AppppA to produce ATP and 2'-deoxyadenylated AMP rather than 2'-deoxyadenylated ATP + AMP as with wild-type enzyme, the ratio of ATP released is increased compared to wild-type. 16.7fold reduction in sensitivity to fluoride	654489	
3.6.1.17	E58Q	fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys. KM-value is 80% of the wild-type value, turnover-number is 43.9% of the wild-type value. 6.7fold reduction in sensitivity to fluoride	654489	
3.6.1.17	E59D	fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys. KM-value is 4fold higher than the wild-type value, turnover-number is 0.02% of the wild-type value. Activity with (2'-pdA)AppppA is to low to be detected. 2fold reduction in sensitivity to fluoride	654489	
3.6.1.17	E59Q	fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys. KM-value is 2.4fold higher than the wild-type value, turnover-number is 0.00076% of the wild-type value. Activity with (2'-pdA)AppppA is to low to be detected	654489	
3.6.1.17	H31A	turnover-number for hydrolysis of Ap4A is 52% of that of the wild-type enzyme, KM-value is 8.3fold higher than the KM-value of the wild-type enzyme	656173	
3.6.1.17	H31V	turnover-number for hydrolysis of Ap4A is 61% of that of the wild-type enzyme, KM-value is 12.5fold higher than the KM-value of the wild-type enzyme	656173	
3.6.1.17	H38G	turnover-number for hydrolysis of Ap4A is 135% of that of the wild-type enzyme, KM-value is 66% of the wild-type value	656173	
3.6.1.17	H38K	turnover-number for hydrolysis of Ap4A is 135% of that of the wild-type enzyme, KM-value is 47% of the wild-type value	656173	
3.6.1.17	K36M	turnover-number for hydrolysis of Ap4A is 9% of that of the wild-type enzyme, KM-value is 1.5fold higher than the KM-value of the wild-type enzyme	656173	
3.6.1.17	K79M	turnover-number for hydrolysis of Ap4A is 0.7% of that of the wild-type enzyme, KM-value is 1.7fold higher than the KM-value of the wild-type enzyme	656173	
3.6.1.17	K81M	turnover-number for hydrolysis of Ap4A is 130% of that of the wild-type enzyme, KM-value is 2.3fold higher than the KM-value of the wild-type enzyme	656173	
3.6.1.17	K83M	turnover-number for hydrolysis of Ap4A is 2.6% of that of the wild-type enzyme, KM-value is 15.9fold higher than the KM-value of the wild-type enzyme	656173	
3.6.1.17	P133A	5fold increase in Km value	733450	
3.6.1.17	P133F	3fold decrease in kcat value	733450	
3.6.1.17	R54Q	fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys. Cleavage of (2'-pdA)AppppA to produce ATP and 2'-deoxyadenylated AMP rather than 2'-deoxyadenylated ATP + AMP as with wild-type enzyme, the ratio of ATP released is increased compared to wild-type. 330fold reduction in sensitivity to fluoride	654489	
3.6.1.17	T70A	active site mutant, has no effect on platelet aggregation and secretion	733563	
3.6.1.17	Y121A	turnover-number for hydrolysis of Ap4A is 61% of that of the wild-type enzyme, KM-value is 8.5fold higher than the KM-value of the wild-type enzyme	656173	
3.6.1.17	Y27A	turnover-number for hydrolysis of Ap4A is 113% of that of the wild-type enzyme, KM-value is 1.25fold higher than the KM-value of the wild-type enzyme	656173	
3.6.1.17	Y27D	turnover-number for hydrolysis of Ap4A is 126% of that of the wild-type enzyme, KM-value is 1.8fold higher than the KM-value of the wild-type enzyme	656173	
3.6.1.17	Y76A	turnover-number for hydrolysis of Ap4A is 8.7% of that of the wild-type enzyme, KM-value is 6.7fold higher than the KM-value of the wild-type enzyme	656173	
3.6.1.17	Y76A/Y121A	turnover-number for hydrolysis of Ap4A is 4.8% of that of the wild-type enzyme, KM-value is 3.75fold higher than the KM-value of the wild-type enzyme	656173