3.1.3.56	D232A	traces of activity	646400	
3.1.3.56	H184A	traces of activity	646400	
3.1.3.56	P387A	traces of activity	646400	
3.1.3.56	V388A	traces of activity	646400	
3.1.3.56	additional information	T-DNA insertional mutants for 5PTase1 (5ptase1-1 and 5ptase1-2, containing a T-DNA insertion within the fifth and fourth introns) and 5PTase2 (5ptase2-1 which contains a T-DNA insertion in the seventh intron) are identified and characterized and a At5PTase1-1/At5PTase2-1 double mutant is produced: grown in dark, seeds from mutants germinate faster than wildtype seeds and the mutant seedlings have longer hypocotyls than wild-type seedlings. Seeds from these mutant lines demonstrate an increase in sensitivity to abscisic acid. These changes in early seedling growth are accompanied by mass increases in Ins(1,4,5)P3, but not by changes in endogenous ABA content. By labeling the endogenous myoinositol pool in 5ptase1 and 5ptase2 mutants, an increases in Ins(1,4,5)P3 and a decrease in PtdIns, PtdIns(4)P, and phosphatidylinositol (4,5)bisphosphate is detected	682411	
3.1.3.56	additional information	T-DNA insertional mutants for 5PTase1 (5ptase1-1 and 5ptase1-2, containing a T-DNA insertion within the fifth and fourth introns) and 5PTase2 (5ptase2-1 which contains a T-DNA insertion in the seventh intron) are identified and characterized and a At5PTase1-1/At5PTase2-1 double mutant is produced: grown in dark, seeds from mutants germinate faster than wild-type seeds and the mutant seedlings have longer hypocotyls than wild-type seedlings. Seeds from these mutant lines demonstrate an increase in sensitivity to abscisic acid. These changes in early seedling growth are accompanied by mass increases in Ins(1,4,5)P3, but not by changes in endogenous ABA content. By labeling the endogenous myoinositol pool in 5ptase1 and 5ptase2 mutants, an increases in Ins(1,4,5)P3 and a decrease in PtdIns, PtdIns(4)P, and phosphatidylinositol (4,5)bisphosphate is detected	682411	
3.1.3.56	E597Q	site-directed mutagenesis, the mutant enzyme shows an over 140fold increased catalytic efficiency and a 2.4fold reduced affinity for Mg2+ compared to the wild-type enzyme	665575	
3.1.3.56	R220A	site-directed mutagenesis, mutation in the P-loop/alpha4-helix, the mutant shows altered substrate specificities and activities compared to the wild-type enzyme, overview	751120	
3.1.3.56	H219A	site-directed mutagenesis, mutation in the P-loop/alpha-helix4, the mutant shows altered substrate specificities and activities compared to the wild-type enzyme, overview	751120	
3.1.3.56	C214S	site-directed mutagenesis, mutation in the P-loop, the mutant shows altered substrate specificities and activities compared to the wild-type enzyme, overview	-, 751120