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acarbose + H2O
pseudotrisaccharide + D-glucose
alpha-cyclomaltodextrin + H2O
maltose + D-glucose
-
-
-
-
?
amylose + H2O
maltose + D-glucose
amylose + H2O
maltotriose + maltotetraose + maltopentaose
beta-cyclomaltodextrin + H2O
maltose + D-glucose
gamma-cyclodextrin + H2O
maltose + ?
not alpha or beta-cyclodextrins
no glucose
-
?
gamma-cyclomaltodextrin + H2O
maltose + D-glucose
-
-
-
-
?
glycogen + H2O
maltooligosaccharides
linear maltooligosaccharides + H2O
maltose + ?
-
no glucose
-
?
maltodextrin 10 + H2O
?
-
-
-
?
maltoheptaose + H2O
D-glucose + maltose + ?
maltohexaose + H2O
D-glucose + maltose + ?
maltopentaose + H2O
D-glucose + maltose + ?
maltotetraose + H2O
2 D-glucose + maltose
maltotriose + H2O
?
-
-
-
-
?
maltotriose + H2O
maltose + D-glucose
pullulan + H2O
6-alpha-D-glucosylmaltose + ?
pullulan + H2O
D-glucose + ?
-
-
-
-
?
pullulan + H2O
D-glucose + maltose + maltotriose
-
the enzyme attacks both alpha-D-(1->4) and alpha-D-(1->6) glycosidic linkages
-
-
?
pullulan + H2O
isomaltose + ?
-
-
-
-
?
pullulan + H2O
maltohexaose + ?
-
strains CCUG43878 and CCUG34405
-
-
?
pullulan + H2O
maltooligosaccharides
pullulan + H2O
maltotriose + ?
pullulan + H2O
maltotriose + maltopentaose + maltohexaose + maltoheptaose
pullulan + H2O
panose + ?
soluble and raw starch + H2O
maltose + maltotriose + maltotetraose + maltopentaose + maltohexaose + maltoheptaose + ?
soluble starch + H2O
D-glucose + maltose
-
-
-
-
?
soluble starch + H2O
maltotriose + maltotetraose
additional information
?
-
acarbose + H2O
pseudotrisaccharide + D-glucose
-
and transglycosylation of D-glucose to isoacarbose
?
acarbose + H2O
pseudotrisaccharide + D-glucose
-
and transglycosylation of D-glucose to isoacarbose
?
amylopectin + H2O
?
-
-
-
?
amylopectin + H2O
?
-
-
-
?
amylose + H2O
maltose + D-glucose
-
-
small amount D-glucose
?
amylose + H2O
maltose + D-glucose
-
-
-
?
amylose + H2O
maltotriose + maltotetraose + maltopentaose
-
61% larger oligosaccharides than maltoocataose after 60 min of C-terminal truncated enzyme ApuADELTA activity compared to 92.6% of full length enzyme activity
no glucose, nor maltose
-
?
amylose + H2O
maltotriose + maltotetraose + maltopentaose
-
61% larger oligosaccharides than maltoocataose after 60 min of C-terminal truncated enzyme ApuADELTA activity compared to 92.6% of full length enzyme activity
no glucose, nor maltose
-
?
beta-cyclomaltodextrin + H2O
maltose + D-glucose
-
-
-
-
?
beta-cyclomaltodextrin + H2O
maltose + D-glucose
-
-
-
?
beta-cyclomaltodextrin + H2O
maltose + D-glucose
-
-
-
?
glycogen + H2O
?
-
-
-
?
glycogen + H2O
maltooligosaccharides
-
50 mM sodium acetate buffer, pH 6.0, 5 mM CaCl2, 80°C
-
-
?
glycogen + H2O
maltooligosaccharides
-
50 mM sodium acetate buffer, pH 6.0, 5 mM CaCl2, 80°C
-
-
?
maltoheptaose + H2O
?
-
-
-
-
?
maltoheptaose + H2O
?
-
-
-
-
?
maltoheptaose + H2O
D-glucose + maltose + ?
-
-
-
?
maltoheptaose + H2O
D-glucose + maltose + ?
-
-
-
-
?
maltoheptaose + H2O
D-glucose + maltose + ?
-
-
-
-
?
maltohexaose + H2O
?
-
-
-
-
?
maltohexaose + H2O
?
-
-
-
-
?
maltohexaose + H2O
D-glucose + maltose + ?
-
-
-
?
maltohexaose + H2O
D-glucose + maltose + ?
-
-
-
-
?
maltohexaose + H2O
D-glucose + maltose + ?
-
-
-
-
?
maltopentaose + H2O
?
-
-
-
-
?
maltopentaose + H2O
?
-
-
-
-
?
maltopentaose + H2O
D-glucose + maltose + ?
-
-
-
?
maltopentaose + H2O
D-glucose + maltose + ?
-
-
-
-
?
maltotetraose + H2O
2 D-glucose + maltose
-
-
-
?
maltotetraose + H2O
2 D-glucose + maltose
-
-
-
-
?
maltotetraose + H2O
?
-
-
-
-
?
maltotetraose + H2O
?
-
-
-
-
?
maltotriose + H2O
maltose + D-glucose
-
in presence of D-glucose
-
-
?
maltotriose + H2O
maltose + D-glucose
-
in presence of D-glucose
-
-
?
maltotriose + H2O
maltose + D-glucose
-
-
-
?
maltotriose + H2O
maltose + D-glucose
-
-
-
?
maltotriose + H2O
maltose + D-glucose
-
-
-
-
?
maltotriose + H2O
maltose + D-glucose
-
-
-
?
maltotriose + H2O
maltose + D-glucose
-
-
-
-
?
pullulan + H2O
6-alpha-D-glucosylmaltose + ?
-
-
i.e. panose
-
?
pullulan + H2O
6-alpha-D-glucosylmaltose + ?
-
-
i.e. panose
-
?
pullulan + H2O
6-alpha-D-glucosylmaltose + ?
-
-
i.e. panose
-
?
pullulan + H2O
6-alpha-D-glucosylmaltose + ?
-
-
i.e. panose
-
?
pullulan + H2O
6-alpha-D-glucosylmaltose + ?
-
-
i.e. panose
-
?
pullulan + H2O
6-alpha-D-glucosylmaltose + ?
-
-
i.e. panose
-
?
pullulan + H2O
6-alpha-D-glucosylmaltose + ?
-
hydrolysis of alpha-1,4-glucosidic linkages
i.e. panose
-
?
pullulan + H2O
6-alpha-D-glucosylmaltose + ?
-
-
i.e. panose
-
?
pullulan + H2O
6-alpha-D-glucosylmaltose + ?
-
hydrolysis of alpha-1,4-glucosidic linkages
i.e. panose
-
?
pullulan + H2O
maltooligosaccharides
-
50 mM sodium acetate buffer, pH 6.0, 5 mM CaCl2, 75°C
-
-
?
pullulan + H2O
maltooligosaccharides
-
50 mM sodium acetate buffer, pH 6.0, 5 mM CaCl2, 75°C
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
no panose
-
?
pullulan + H2O
maltotriose + maltopentaose + maltohexaose + maltoheptaose
-
no larger oligosaccharides than maltoocataose after 5 min of C-terminal truncated enzyme ApuADELTA activity compared to 95.5% of ApuA activity
no glucose, nor maltose
-
?
pullulan + H2O
maltotriose + maltopentaose + maltohexaose + maltoheptaose
-
no larger oligosaccharides than maltoocataose after 5 min of C-terminal truncated enzyme ApuADELTA activity compared to 95.5% of ApuA activity
no glucose, nor maltose
-
?
pullulan + H2O
panose + ?
-
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
-
?
pullulan + H2O
panose + ?
-
N-terminal alpha-amylase-containing domain and C-terminal pullulanase-containing domain
-
-
?
pullulan + H2O
panose + ?
-
N-terminal alpha-amylase-containing domain and C-terminal pullulanase-containing domain
-
-
?
pullulan + H2O
panose + ?
-
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
?
pullulan + H2O
panose + ?
-
-
?
pullulan + H2O
panose + ?
-
-
in the first step, the enzyme hydrolyzes only alpha-1,4-glucosidic linkages on the nonreducing side of alpha-1,6-linkages of pullulan and produces panose and several intermediate products composed of some panose units. In the second step, taking 62-O-alpha-(63-O-alpha-glucosyl-maltotriosyl)-maltose as an example of one of the intermediate products, the enzyme hydrolyzes either alpha-1,4-, or alpha-1,6-linkages and produces panose or 63-O-alpha-glucosyl-maltotriose plus maltose, respectively. In the third step, the alpha-1,4-linkage of the 63-O-alpha-glucosyl-maltotriose is hydrolyzed by the enzyme, and D-glucose and another panose are produced, + maltose + D-glucose, in a molar ratio of 3:1:1, small amount
?
pullulan + H2O
panose + ?
-
-
+ maltose + D-glucose, in a molar ratio of 3:1:1, small amount
?
pullulan + H2O
panose + ?
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
?
pullulan + H2O
panose + ?
-
-
?
pullulan + H2O
panose + ?
-
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
?
pullulan + H2O
panose + ?
-
the enzyme may have a role to provide branched maltooligosaccharides to stimulate the growth of beneficial microorganisms in the human intestine
-
-
?
pullulan + H2O
panose + ?
-
the enzyme is an alpha-amylase with neopullulanase-like activity
-
-
?
pullulan + H2O
panose + ?
-
-
-
?
pullulan + H2O
panose + ?
-
-
-
?
soluble and raw starch + H2O
maltose + maltotriose + maltotetraose + maltopentaose + maltohexaose + maltoheptaose + ?
-
50 mM sodium acetate buffer, pH 6.0, 5 mM CaCl2, 80°C
-
-
?
soluble and raw starch + H2O
maltose + maltotriose + maltotetraose + maltopentaose + maltohexaose + maltoheptaose + ?
-
50 mM sodium acetate buffer, pH 6.0, 5 mM CaCl2, 80°C
-
-
?
soluble starch + H2O
maltotriose + maltotetraose
-
-
no glucose, nor maltose
-
?
soluble starch + H2O
maltotriose + maltotetraose
-
-
no glucose, nor maltose
-
?
starch + H2O
maltose + ?
-
-
-
-
?
starch + H2O
maltose + ?
-
-
-
-
?
starch + H2O
maltose + ?
not alpha or beta-cyclodextrins
no glucose
-
?
additional information
?
-
-
4 reactions are catalyzed by the enzyme: 1. hydrolysis of alpha-1,4-glucosidic linkage, 2. hydrolysis of alpha-1,6-glucosidic linkage, 3. transglycosylation to form alpha-1,4-glucosidic linkage, 4. transglycosylation to form alpha-1,6-glucosidic linkage
-
-
?
additional information
?
-
-
4 reactions are catalyzed by the enzyme: 1. hydrolysis of alpha-1,4-glucosidic linkage, 2. hydrolysis of alpha-1,6-glucosidic linkage, 3. transglycosylation to form alpha-1,4-glucosidic linkage, 4. transglycosylation to form alpha-1,6-glucosidic linkage
-
-
?
additional information
?
-
-
enzyme is able to cleave beta-cyclodextrin
-
-
?
additional information
?
-
-
enzyme also cleaves alpha-1,4-bonds in amylose and in oligosaccharides of maltotriose through maltoheptaose in chain length
-
-
?
additional information
?
-
-
4 reactions are catalyzed by the enzyme: 1. hydrolysis of alpha-1,4-glucosidic linkage, 2. hydrolysis of alpha-1,6-glucosidic linkage, 3. transglycosylation to form alpha-1,4-glucosidic linkage, 4. transglycosylation to form alpha-1,6-glucosidic linkage
-
-
?
additional information
?
-
-
enzyme hydrolyzes starch
-
-
?
additional information
?
-
-
4 reactions are catalyzed by the enzyme: 1. hydrolysis of alpha-1,4-glucosidic linkage, 2. hydrolysis of alpha-1,6-glucosidic linkage, 3. transglycosylation to form alpha-1,4-glucosidic linkage, 4. transglycosylation to form alpha-1,6-glucosidic linkage
-
-
?
additional information
?
-
-
enzyme hydrolyzes starch
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
the enzyme catalyses condensation between two maltose molecules and subsequent hydrolysis of the resulting 6-O-alpha-maltosylmaltose to D-glucose and panose, when maltose concentration is inceased to 20%
-
-
?
additional information
?
-
-
the enzyme catalyses condensation between two maltose molecules and subsequent hydrolysis of the resulting 6-O-alpha-maltosylmaltose to D-glucose and panose, when maltose concentration is inceased to 20%
-
-
?
additional information
?
-
-
analysis of the active centre, one active centre participates in the dual activity toward alpha-1,4-, and alpha-1,6-glucosidic linkages
-
-
?
additional information
?
-
-
4 reactions are catalyzed by the enzyme: 1. hydrolysis of alpha-1,4-glucosidic linkage, 2. hydrolysis of alpha-1,6-glucosidic linkage, 3. transglycosylation to form alpha-1,4-glucosidic linkage, 4. transglycosylation to form alpha-1,6-glucosidic linkage
-
-
?
additional information
?
-
-
4 reactions are catalyzed by the enzyme: 1. hydrolysis of alpha-1,4-glucosidic linkage, 2. hydrolysis of alpha-1,6-glucosidic linkage, 3. transglycosylation to form alpha-1,4-glucosidic linkage, 4. transglycosylation to form alpha-1,6-glucosidic linkage
-
-
?
additional information
?
-
4 reactions are catalyzed by the enzyme: 1. hydrolysis of alpha-1,4-glucosidic linkage, 2. hydrolysis of alpha-1,6-glucosidic linkage, 3. transglycosylation to form alpha-1,4-glucosidic linkage, 4. transglycosylation to form alpha-1,6-glucosidic linkage
-
-
?
additional information
?
-
-
4 reactions are catalyzed by the enzyme: 1. hydrolysis of alpha-1,4-glucosidic linkage, 2. hydrolysis of alpha-1,6-glucosidic linkage, 3. transglycosylation to form alpha-1,4-glucosidic linkage, 4. transglycosylation to form alpha-1,6-glucosidic linkage
-
-
?
additional information
?
-
-
enzyme hydrolyzes starch
-
-
?
additional information
?
-
-
enzyme hydrolyzes starch
-
-
?
additional information
?
-
-
enzyme hydrolyzes starch
-
-
?
additional information
?
-
-
enzyme hydrolyzes starch
-
-
?
additional information
?
-
enzyme hydrolyzes starch
-
-
?
additional information
?
-
-
enzyme hydrolyzes starch
-
-
?
additional information
?
-
-
enzyme hydrolyzes not only alpha-1,4-glucosidic linkages but also specific alpha-1,6-glucosidic linkages of several branched oligosaccharides
-
-
?
additional information
?
-
the dual specificity of the enzyme toward alpha-1,4-, and alpha-1,6-glucosidic linkages based on structural analyses of the complexes with the enzyme and substrates is demonstrated
-
-
?
additional information
?
-
-
the dual specificity of the enzyme toward alpha-1,4-, and alpha-1,6-glucosidic linkages based on structural analyses of the complexes with the enzyme and substrates is demonstrated
-
-
?
additional information
?
-
-
the enzyme is unable to degrade alpha-cyclodextrin and panose
-
-
?
additional information
?
-
the enzyme catalyzes the hydrolysis of alpha-1,4- and alpha-1,6-glucosidic linkages (of pullulan) of transglycosylations to form both alpha-1,4- and alpha-1,6-glucosidic bonds
-
-
?
additional information
?
-
the enzyme catalyses condensation between two maltose molecules and subsequent hydrolysis of the resulting 6-O-alpha-maltosylmaltose to D-glucose and panose, when maltose concentration is inceased to 20%
-
-
?
additional information
?
-
enzyme hydrolyzes starch
-
-
?
additional information
?
-
-
the enzyme is unable to degrade alpha-cyclodextrin and panose
-
-
?
additional information
?
-
-
4 reactions are catalyzed by the enzyme: 1. hydrolysis of alpha-1,4-glucosidic linkage, 2. hydrolysis of alpha-1,6-glucosidic linkage, 3. transglycosylation to form alpha-1,4-glucosidic linkage, 4. transglycosylation to form alpha-1,6-glucosidic linkage
-
-
?
additional information
?
-
-
enzyme hydrolyzes starch
-
-
?
additional information
?
-
-
enzyme hydrolyzes starch
-
-
?
additional information
?
-
4 reactions are catalyzed by the enzyme: 1. hydrolysis of alpha-1,4-glucosidic linkage, 2. hydrolysis of alpha-1,6-glucosidic linkage, 3. transglycosylation to form alpha-1,4-glucosidic linkage, 4. transglycosylation to form alpha-1,6-glucosidic linkage
-
-
?
additional information
?
-
the dual specificity of the enzyme toward alpha-1,4-, and alpha-1,6-glucosidic linkages based on structural analyses of the complexes with the enzyme and substrates is demonstrated
-
-
?
additional information
?
-
-
enzyme hydrolyzes starch
-
-
?
additional information
?
-
-
enzyme hydrolyzes not only alpha-1,4-glucosidic linkages but also specific alpha-1,6-glucosidic linkages of several branched oligosaccharides
-
-
?
additional information
?
-
-
enzyme hydrolyzes starch
-
-
?
additional information
?
-
-
enzyme hydrolyzes not only alpha-1,4-glucosidic linkages but also specific alpha-1,6-glucosidic linkages of several branched oligosaccharides
-
-
?
additional information
?
-
comparison of substrate specificity of wild-type and recombinant enzymes
-
-
?
additional information
?
-
-
comparison of substrate specificity of wild-type and recombinant enzymes
-
-
?
additional information
?
-
-
4 reactions are catalyzed by the enzyme: 1. hydrolysis of alpha-1,4-glucosidic linkage, 2. hydrolysis of alpha-1,6-glucosidic linkage, 3. transglycosylation to form alpha-1,4-glucosidic linkage, 4. transglycosylation to form alpha-1,6-glucosidic linkage
-
-
?
additional information
?
-
-
enzyme hydrolyzes starch
-
-
?
additional information
?
-
enzyme hydrolyzes starch
-
-
?
additional information
?
-
-
enzyme hydrolyzes starch
-
-
?
additional information
?
-
comparison of substrate specificity of wild-type and recombinant enzymes
-
-
?
additional information
?
-
enzyme hydrolyzes starch
-
-
?
additional information
?
-
-
the enzyme also shows alpha-amylase activity hydrolysing alpha-1,6-glucosidic bonds, enzyme substrate specificity is determined by two Asp and one Glu residues
-
-
?
additional information
?
-
-
the enzyme also shows alpha-amylase activity hydrolysing alpha-1,6-glucosidic bonds, enzyme substrate specificity is determined by two Asp and one Glu residues
-
-
?
additional information
?
-
enzyme hydrolyzes not only alpha-1,4-glucosidic linkages but also specific alpha-1,6-glucosidic linkages of several branched oligosaccharides
-
-
?
additional information
?
-
enzyme hydrolyzes not only alpha-1,4-glucosidic linkages but also specific alpha-1,6-glucosidic linkages of several branched oligosaccharides
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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
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
D328H
-
site-directed mutagenesis, inactive mutant
D328N
-
site-directed mutagenesis, inactive mutant
D424H
-
site-directed mutagenesis, inactive mutant
D424N
-
site-directed mutagenesis, inactive mutant
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
E357H
-
site-directed mutagenesis, inactive mutant
E357Q
-
site-directed mutagenesis, inactive mutant
I358V
-
mutation decreases the preference for alpha(1-6)-branched oligosaccharides and pullulan as substrates
I358W
-
mutation reduces the acceptability of alpha(1-6)-branched oligo- and polysaccharides
M375L
-
mutation increases transglycosylation activity in comparison to wild-type enzyme
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
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
S422V
-
mutation increases transglycosylation activity in comparison to wild-type enzyme
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
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
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
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
Y377D
-
mutation decreases transglycosylation activity in comparison to wild-type enzyme
Y377F
-
mutation increases transglycosylation activity in comparison to wild-type enzyme
Y377S
-
mutation decreases transglycosylation activity in comparison to wild-type enzyme
I358V
-
mutation decreases the preference for alpha(1-6)-branched oligosaccharides and pullulan as substrates
-
I358W
-
mutation reduces the acceptability of alpha(1-6)-branched oligo- and polysaccharides
-
M375L
-
mutation increases transglycosylation activity in comparison to wild-type enzyme
-
S422V
-
mutation increases transglycosylation activity in comparison to wild-type enzyme
-
Y377F
-
mutation increases transglycosylation activity in comparison to wild-type enzyme
-
I358V
-
site-directed mutagenesis, the mutant shows increased activity hydrolyzing alpha-1,6-glucosidic bonds, producing maltotriose, compared to the wild-type enzyme
I358W
-
site-directed mutagenesis, the mutant shows decreased activity hydrolyzing alpha-1,6-glucosidic bonds, producing maltotriose, compared to the wild-type enzyme
I358V
-
site-directed mutagenesis, the mutant shows increased activity hydrolyzing alpha-1,6-glucosidic bonds, producing maltotriose, compared to the wild-type enzyme
-
I358W
-
site-directed mutagenesis, the mutant shows decreased activity hydrolyzing alpha-1,6-glucosidic bonds, producing maltotriose, compared to the wild-type enzyme
-
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
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
-
additional information
-
knockout variant through insertion in gene apuB that is encoding for amylopullulanase: no growth on starch, amylopectin, glycogen, or pullulan
additional information
-
knockout variant through insertion in gene apuB that is encoding for amylopullulanase: no growth on starch, amylopectin, glycogen, or pullulan
-
additional information
-
C-terminal truncated ApuA produced with Escherichia coli plasmid, and transformed into Lactobacillus plantarum
additional information
-
C-terminal truncated ApuA produced with Escherichia coli plasmid, and transformed into Lactobacillus plantarum
-
additional information
-
mutation of residues A357, Q359, and Y360X also leads to increased activity hydrolyzing alpha-1,6-glucosidic bonds, producing maltotriose
additional information
-
mutation of residues A357, Q359, and Y360X also leads to increased activity hydrolyzing alpha-1,6-glucosidic bonds, producing maltotriose
-
additional information
-
R855 C-terminal truncated (100 amino acids) mutant R855 of full length TetApuM955, produced with trypsin-like proteolytic cleavage reaction
additional information
-
R855 C-terminal truncated (100 amino acids) mutant R855 of full length TetApuM955, produced with trypsin-like proteolytic cleavage reaction
-
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brenda
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Bacillus sp. KSM-1876, Geobacillus stearothermophilus, Paenibacillus polymyxa, Bacteroides thetaiotaomicron, Klebsiella pneumoniae, Bacteroides thetaiotaomicron 95-1
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brenda
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Cooperativity and substrate specificity of an alkaline amylase and neopullulanase complex of Micrococcus halobius OR-1
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Nesterenkonia halobia, Nesterenkonia halobia OR-1
brenda
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Characterization of novel neopullulanase from Bacillus polymyxa
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68
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Paenibacillus polymyxa, Paenibacillus polymyxa CECT 155
-
brenda
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Structural consequences of neopullulanase mutations
Biochim. Biophys. Acta
1295
195-200
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Geobacillus stearothermophilus
brenda
Erra-Pujada, M.; Debeire, P.; Duchiron, F.; O'Donohue, M.J.
The type II pullulanase of Thermococcus hydrothermalis: molecular characterization of the gene and expression of the catalytic domain
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3284-3287
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Thermococcus hydrothermalis (Q9Y8I8), Thermococcus hydrothermalis AL662 (Q9Y8I8)
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Expression and secretion of Bacillus polymyxa neopullulanase in Saccharomyces cerevisiae
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Pullulan degrading enzymes of bacterial origin
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brenda
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Screening for and identification of starch-, amylopectin-, and pullulan-degrading activities in bifidobacterial strains
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72
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Bifidobacterium breve, Bifidobacterium dentium, Bifidobacterium longum subsp. infantis, Bifidobacterium pseudolongum, Bifidobacterium thermophilum, Bifidobacterium dentium NCFB2243, Bifidobacterium thermophilum JCM 7027
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Green fluorescent chimeras indicate nonpolar localization of pullulanase secreton components PulL and PulM
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Klebsiella oxytoca
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Isolation and characterization of a novel thermostable neopullulanase-like enzyme from a hot spring in Thailand
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uncultured microorganism (A7LI67)
brenda
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Biochemical characterization of engineered amylopullulanase from Thermoanaerobacter ethanolicus 39E-implicating the non-necessity of its 100 C-terminal amino acid residues
Extremophiles
12
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Thermoanaerobacter ethanolicus, Thermoanaerobacter ethanolicus 39E
brenda
Kim, J.H.; Sunako, M.; Ono, H.; Murooka, Y.; Fukusaki, E.; Yamashita, M.
Characterization of the C-terminal truncated form of amylopullulanase from Lactobacillus plantarum L137
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107
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Lactiplantibacillus plantarum, Lactiplantibacillus plantarum ATCC BAA-793
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Zareian, S.; Khajeh, K.; Ranjbar, B.; Dabirmanesh, B.; Ghollasi, M.; Mollania, N.
Purification and characterization of a novel amylopullulanase that converts pullulan to glucose, maltose, and maltotriose and starch to glucose and maltose
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46
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Geobacillus stearothermophilus, Geobacillus stearothermophilus L14
-
brenda
Majzlova, K.; Pukajova, Z.; Jane?ek, S.
Tracing the evolution of the alpha-amylase subfamily GH13_36 covering the amylolytic enzymes intermediate between oligo-1,6-glucosidases and neopullulanases
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367
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Geobacillus stearothermophilus (P38940)
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Over-expression of recombinant proteins with N-terminal His-tag via subcellular uneven distribution in Escherichia coli
Acta Biochim. Biophys. Sin. (Shanghai)
47
488-495
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Bacillus cereus (A0A1Y6AAA3)
brenda
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Isolation and identification of a new Bacillus cereus strain and characterization of its neopullulanase
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2
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Bacillus cereus, Bacillus cereus SDK2
-
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Characterization of a novel extracellular alpha-amylase from Ruminococcus bromii ATCC 27255 with neopullulanase-like activity
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brenda
Heravi, K.M.; Watzlawick, H.; Altenbuchner, J.
Development of an anhydrotetracycline-inducible expression system for expression of a neopullulanase in B. subtilis
Plasmid
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2015
unidentified
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Improving thermal and detergent stability of Bacillus stearothermophilus neopullulanase by rational enzyme design
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