3.2.1.135: neopullulanase
This is an abbreviated version!
For detailed information about neopullulanase, go to the full flat file.
Word Map on EC 3.2.1.135
-
3.2.1.135
-
starch
-
stearothermophilus
-
amylolytic
-
alpha-amylases
-
cyclomaltodextrinase
-
maltogenic
-
amylopectin
-
transglycosylation
-
amylose
-
alpha-1,4
-
amylopullulanase
-
debranching
-
oligo-1,6-glucosidase
-
glucanotransferase
-
thermoactinomyces
-
alpha-1,6-glucosidic
-
isopanose
-
cdase
-
saccharifying
-
pullulanases
-
cyclodextrinase
-
maltooligosaccharides
-
isoamylase
-
isopullulanase
-
gamma-cyclodextrins
-
biotechnology
-
industry
-
synthesis
- 3.2.1.135
- starch
- stearothermophilus
-
amylolytic
- alpha-amylases
- cyclomaltodextrinase
-
maltogenic
- amylopectin
-
transglycosylation
- amylose
-
alpha-1,4
- amylopullulanase
-
debranching
- oligo-1,6-glucosidase
-
glucanotransferase
-
thermoactinomyces
-
alpha-1,6-glucosidic
- isopanose
-
cdase
-
saccharifying
- pullulanases
- cyclodextrinase
- maltooligosaccharides
- isoamylase
- isopullulanase
- gamma-cyclodextrins
- biotechnology
- industry
- synthesis
Reaction
Synonyms
Amo105, amylopullalanase, amylopullulanase, ApuA, ApuADELTA, bsNpl, cyclomaltodextrinase, Env Npu193A, More, neopullulanase-alpha-amylase, neopullulanase-like enzyme, Pul, pullulan 4-D-glucanohydrolase (6-alpha-D-glucosylmaltose), pullulan hydrolase type I, pullulanase, pullulanase II, pullulanase, neo-, Rbamy5, TetApuM955, TetApuR855, type II pullulanase, type III pullulan hydrolase
ECTree
3.2.1.135 neopullulanaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.2.1.135 - neopullulanase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
gamma-cyclodextrin + H2O
maltose + ?
not alpha or beta-cyclodextrins
no glucose
-
?
linear maltooligosaccharides + H2O
maltose + ?
-
no glucose
-
?
pullulan + H2O
D-glucose + maltose + maltotriose
-
the enzyme attacks both alpha-D-(1->4) and alpha-D-(1->6) glycosidic linkages
-
-
?
pullulan + H2O
maltohexaose + ?
-
strains CCUG43878 and CCUG34405
-
-
?
soluble and raw starch + H2O
maltose + maltotriose + maltotetraose + maltopentaose + maltohexaose + maltoheptaose + ?
acarbose + H2O
pseudotrisaccharide + D-glucose
-
and transglycosylation of D-glucose to isoacarbose
?
acarbose + H2O
pseudotrisaccharide + D-glucose
-
and transglycosylation of D-glucose to isoacarbose
?
amylose + H2O
maltose + D-glucose
-
-
small amount 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
Lactiplantibacillus plantarum ATCC BAA-793
-
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
-
-
-
?
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
-
-
?
maltotriose + H2O
maltose + D-glucose
-
in presence of 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 + ?
-
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 + 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
Lactiplantibacillus plantarum ATCC BAA-793
-
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 + ?
-
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 + ?
-
-
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 + ?
-
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
-
-
?
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
Lactiplantibacillus plantarum ATCC BAA-793
-
-
no glucose, nor 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
?
-
-
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
?
-
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 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 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
-
-
?
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
?
-
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
-
-
?
