3.2.1.135	A416I	t1/2 of mutant enzyme at 70°C is 17 min, compared to 15 min for wild-type enzyme. Mutation does not compromise the catalytic activity	752088	
3.2.1.135	A566L	t1/2 of mutant enzyme at 70°C is 27 min, compared to 15 min for wild-type enzyme. Mutation does not compromise the catalytic activity	752088	
3.2.1.135	D328H	site-directed mutagenesis, inactive mutant	664673	
3.2.1.135	D328N	site-directed mutagenesis, inactive mutant	664673	
3.2.1.135	D424H	site-directed mutagenesis, inactive mutant	664673	
3.2.1.135	D424N	site-directed mutagenesis, inactive mutant	664673	
3.2.1.135	D46E	t1/2 of mutant enzyme at 70°C is 100 min, compared to 15 min for wild-type enzyme. Mutation does not compromise the catalytic activity	752088	
3.2.1.135	E357H	site-directed mutagenesis, inactive mutant	664673	
3.2.1.135	E357Q	site-directed mutagenesis, inactive mutant	664673	
3.2.1.135	I358V	mutation decreases the preference for alpha(1-6)-branched oligosaccharides and pullulan as substrates	-, 646815	
3.2.1.135	I358V	site-directed mutagenesis, the mutant shows increased activity hydrolyzing alpha-1,6-glucosidic bonds, producing maltotriose, compared to the wild-type enzyme	-, 664673	
3.2.1.135	I358W	mutation reduces the acceptability of alpha(1-6)-branched oligo- and polysaccharides	-, 646815	
3.2.1.135	I358W	site-directed mutagenesis, the mutant shows decreased activity hydrolyzing alpha-1,6-glucosidic bonds, producing maltotriose, compared to the wild-type enzyme	-, 664673	
3.2.1.135	M375L	mutation increases transglycosylation activity in comparison to wild-type enzyme	-, 646815	
3.2.1.135	additional information	C-terminal truncated ApuA produced with Escherichia coli plasmid, and transformed into Lactobacillus plantarum	-, 699051	
3.2.1.135	additional information	diverse mutants are constructed and specific activities, sugar compositions of pullulan hydrolysate and hydrolysis activities toward alpha-(1-4) and alpha-(1-6)-glucosidic linkages analyzed	-, 393353	
3.2.1.135	additional information	knockout variant through insertion in gene apuB that is encoding for amylopullulanase: no growth on starch, amylopectin, glycogen, or pullulan	-, 695738	
3.2.1.135	additional information	mutation of residues A357, Q359, and Y360X also leads to increased activity hydrolyzing alpha-1,6-glucosidic bonds, producing maltotriose	-, 664673	
3.2.1.135	additional information	R855 C-terminal truncated (100 amino acids) mutant R855 of full length TetApuM955, produced with trypsin-like proteolytic cleavage reaction	-, 697834	
3.2.1.135	N413Q	t1/2 of mutant enzyme at 70°C is 32 min, compared to 15 min for wild-type enzyme. Mutation does not compromise the catalytic activity	752088	
3.2.1.135	S407T	t1/2 of mutant enzyme at 70°C is 66 min, compared to 15 min for wild-type enzyme. Mutation does not compromise the catalytic activity	752088	
3.2.1.135	S422V	mutation increases transglycosylation activity in comparison to wild-type enzyme	-, 646815	
3.2.1.135	V239L	t1/2 of mutant enzyme at 70°C is 103 min, compared to 15 min for wild-type enzyme. Mutation does not compromise the catalytic activity	752088	
3.2.1.135	V374I	t1/2 of mutant enzyme at 70°C is 14 min, compared to 15 min for wild-type enzyme. Mutation does not compromise the catalytic activity	752088	
3.2.1.135	V404L	t1/2 of mutant enzyme at 70°C is 191 min, compared to 15 min for wild-type enzyme. Mutation does not compromise the catalytic activity	752088	
3.2.1.135	V533L	t1/2 of mutant enzyme at 70°C is 8 min, compared to 15 min for wild-type enzyme. Mutation does not compromise the catalytic activity	752088	
3.2.1.135	Y377D	mutation decreases transglycosylation activity in comparison to wild-type enzyme	646815	
3.2.1.135	Y377F	mutation increases transglycosylation activity in comparison to wild-type enzyme	-, 646815	
3.2.1.135	Y377S	mutation decreases transglycosylation activity in comparison to wild-type enzyme	646815