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Information on EC 3.2.1.135 - neopullulanase
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EC Tree
3.2.1.135 neopullulanaseIUBMB Comments
cf. EC 3.2.1.41 (pullulanase ) and EC 3.2.1.57 (isopullulanase).
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Word Map
- 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
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
neopullulanase, tetapum955, env npu193a, tetapur855, apuadelta, type iii pullulan hydrolase, bsnpl, pullulanase ii, neopullulanase-like enzyme, pullulan hydrolase type i, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
amylopullalanase
amylopullulanase
ApuA
ApuADELTA
neopullulanase-alpha-amylase
pullulan 4-D-glucanohydrolase (6-alpha-D-glucosylmaltose)
pullulan hydrolase type I
pullulanase
pullulanase II
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-
-
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pullulanase, neo-
-
-
-
-
Rbamy5
TetApuM955
TetApuR855
type III pullulan hydrolase
additional information
amylopullulanase
-
type II bifunctional amylopullulanase: N-terminal alpha-amylase-containing domain to cleave alpha-1,4-glucosidic linkages such in starch, amylopectin, and glycogen to produce maltooligosaccharides, and a separate C-terminal pullulanase-containing domain to cleave alpha-1,6-glucosidic linkages in pullulan to produce maltotriose and polymers of maltotriose
amylopullulanase
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type II bifunctional amylopullulanase: N-terminal alpha-amylase-containing domain to cleave alpha-1,4-glucosidic linkages such in starch, amylopectin, and glycogen to produce maltooligosaccharides, and a separate C-terminal pullulanase-containing domain to cleave alpha-1,6-glucosidic linkages in pullulan to produce maltotriose and polymers of maltotriose
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pullulan 4-D-glucanohydrolase (6-alpha-D-glucosylmaltose)
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-
additional information
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bifunctional enzyme, cf. EC 3.2.1.1, alpha-amylase
additional information
-
bifunctional enzyme, cf. EC 3.2.1.1, alpha-amylase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
pullulan + H2O = panose
acidic residues determine the substrate specificity, residues A357, Q359, and Y360, located in region II, are involved in action pattern formation
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pullulan + H2O = panose
residues E357, D424, and D328 are involved in the catalytic reaction at the active site, residues H423, E332, and N331 are involved in substrate recognition
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pullulan + H2O = panose
acidic residues determine the substrate specificity, residues A357, Q359, and Y360, located in region II, are involved in action pattern formation
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-
pullulan + H2O = panose
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis
hydrolysis of O-glycosyl bond
-
-
-
-
hydrolysis
only enzymatic activity on alpha-1,6-glusocidic linkages of pullulan, not on alpha-1,4-glucosidic bonds
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SYSTEMATIC NAME
IUBMB Comments
pullulan 4-D-glucanohydrolase (panose-forming)
cf. EC 3.2.1.41 (pullulanase ) and EC 3.2.1.57 (isopullulanase).
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CAS REGISTRY NUMBER
COMMENTARY
119632-58-5
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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
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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
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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
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50 mM sodium acetate buffer, pH 6.0, 5 mM CaCl2, 80°C
-
-
?
glycogen + H2O
maltooligosaccharides
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50 mM sodium acetate buffer, pH 6.0, 5 mM CaCl2, 80°C
-
-
?
maltotriose + H2O
maltose + D-glucose
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in presence of D-glucose
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-
?
pullulan + H2O
6-alpha-D-glucosylmaltose + ?
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-
i.e. panose
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?
pullulan + H2O
6-alpha-D-glucosylmaltose + ?
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-
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
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50 mM sodium acetate buffer, pH 6.0, 5 mM CaCl2, 75°C
-
-
?
pullulan + H2O
maltooligosaccharides
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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
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-
?
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 + ?
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the enzyme may have a role to provide branched maltooligosaccharides to stimulate the growth of beneficial microorganisms in the human intestine
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-
?
pullulan + H2O
panose + ?
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the enzyme is an alpha-amylase with neopullulanase-like activity
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-
?
soluble and raw starch + H2O
maltose + maltotriose + maltotetraose + maltopentaose + maltohexaose + maltoheptaose + ?
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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
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-
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
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-
?
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
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-
?
additional information
?
-
-
enzyme is able to cleave beta-cyclodextrin
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-
?
additional information
?
-
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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
?
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-
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
-
-
?