3.6.1.52	C214S	inactive	-, 757172	
3.6.1.52	E66Q	no significant activity towards diphosphoinositol pentakisphosphate or bisdiphosphoinositol tetrakisphosphate, activity with diadenosine 5',5'''-P1,P6-hexaphosphate is 2% of the activity of the wild-type enzyme	393826	
3.6.1.52	E70Q	-	393824	
3.6.1.52	E70Q	greatly reduced rate of hydrolysis of diphosphoinositol pentakisphosphate or bisdiphosphoinositol tetrakisphosphate	393824	
3.6.1.52	E70Q	inactive against dATP,diphosphoinositol pentakisphosphate or bisdiphosphoinositol tetrakisphosphate	393826	
3.6.1.52	F84Y	hydrolysis of bisdiphosphoinositol tetrakisphosphate at 63% of the activity of the wild-type enzyme, hydrolysis of diadenosine 5',5'''-P1,P6-hexaphosphate is 75% of the activity of the wild-type enzyme, activity with diphosphoinositol pentakisphosphate is only slightly reduced	393826	
3.6.1.52	G50A	hydrolysis of diphosphoinositol polyphosphates is more than 85% less than that of the wild-type enzyme	393826	
3.6.1.52	G52A	hydrolysis of diphosphoinositol polyphosphates is more than 85% less than that of the wild-type enzyme	393826	
3.6.1.52	G72A	catalytic activity towards bisdiphosphoinositol tetrakisphosphate, diadenosine 5',5'''-P1,P6-hexaphosphateand diphosphoinositol pentakisphosphate is impaired by more than 95%	393826	
3.6.1.52	G75A	catalytic activity towards bisdiphosphoinositol tetrakisphosphate, diadenosine 5',5'''-P1,P6-hexaphosphateand diphosphoinositol pentakisphosphate is impaired by more than 95%	393826	
3.6.1.52	G78A	catalytic activity and CD spectrum is not significantly different from that of the wild.type enzyme	393826	
3.6.1.52	G82A	mutation promotes some unraveling of the normal secondary structure	393826	
3.6.1.52	H91L	hydrolysis of bisdiphosphoinositol tetrakisphosphate at 4% of the activity of the wild-type enzyme, hydrolysis of diadenosine 5',5'''-P1,P6-hexaphosphate is 26% of the activity of the wild-type enzyme, activity with diphosphoinositol pentakisphosphate is only slightly reduced	393826	
3.6.1.52	additional information	overexpression of yeast diphosphoinositol polyphosphate phosphohydrolase (DDP1) in Saccharomyces cerevisiae leads to significantly increased compared to the parent strain. The content of acid-soluble and acid-insoluble polyphosphates under DDP1 overexpression decreases by 9 and 28%, respectively	-, 756069	
3.6.1.52	P89R	codes for isoenzyme hDIPP3beta	659184