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Information on EC 3.2.1.41 - pullulanase
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EC Tree
3.2.1.41 pullulanaseIUBMB Comments
Different from EC 3.2.1.142 (limit dextrinase) in its action on glycogen, and its rate of hydrolysis of limit dextrins. Its action on amylopectin is complete. Maltose is the smallest sugar that it can release from an alpha-(1->6)-linkage.
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Word Map
- 3.2.1.41
- starch
- pullulans
- glycogen
- klebsiella
- amylose
- maltotriose
- alpha-amylase
- isoamylase
-
lariat
- glucoamylase
-
amylolytic
- beta-amylase
- oxytoca
- cyclodextrins
-
dextrinase
- amyloglucosidase
-
alpha-1,6
-
saccharification
- beta-cyclodextrins
-
waxy
- maltodextrins
- aureobasidium
-
glucanotransferase
- phytoglycogen
- maltotetraose
-
aerobacter
- synthesis
- pilins
-
thermoanaerobacterium
-
branchpoints
-
starch-based
- alpha-glucans
- malto-oligosaccharides
-
starch-degrading
- maltohexaose
- anoxybacillus
- industry
- food industry
- degradation
- biotechnology
- thermoleovorans
- amylo-1,6-glucosidase
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
pullulanase, debranching enzyme, amylopullulanase, pulask, r-enzyme, pullulanase type i, pbpula, bapul13a, type ii pullulanase, pulwb42, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,4-alpha-D-glucan glucanohydrolase
-
-
-
-
Alpha-dextrin endo-1,6-alpha-glucosidase
-
-
-
-
amylase-pullulanase
amylopectin 6-glucanohydrolase
-
-
-
-
amylopullulanase
AmyX
Apu
ApuK885
ApuM957
Ask
BmPul
BNPulA324
debranching enzyme
EC 3.2.1.69
-
-
formerly
-
glucanohydrolase, amylopectin 6-
-
-
-
-
limit dextrinase
-
-
-
-
Pcal-1616
PelBsp-PulA
-
a nonacylated variant of PulA made by replacing the lipoprotein signal peptide with the signal peptide of pectate lyase PelB from Erwinia chrysanthemi
PUL US105
Pul3YH5
PulASK
pulGT
Pullulan 6-glucanohydrolase
pullulan-6-glucanohydrolase
pullulanase
pullulanase type 1
pullulanase type I
pullulanase type II
R-enzyme
-
-
-
-
Saci_1162
TPApu
type II pullulanase
additional information
Pullulan 6-glucanohydrolase
-
-
-
-
pullulanase type I
-
hydrolyzes (1-6)-alpha-D-glucosidic linkages in pullulan
pullulanase type I
-
hydrolyzes (1-6)-alpha-D-glucosidic linkages in pullulan
pullulanase type I
-
hydrolyzes (1-6)-alpha-D-glucosidic linkages in pullulan
pullulanase type I
-
hydrolyzes (1-6)-alpha-D-glucosidic linkages in pullulan
-
pullulanase type I
-
hydrolyzes (1-6)-alpha-D-glucosidic linkages in pullulan
pullulanase type I
-
hydrolyzes (1-6)-alpha-D-glucosidic linkages in pullulan
-
pullulanase type I
-
hydrolyzes (1-6)-alpha-D-glucosidic linkages in pullulan
pullulanase type I
-
hydrolyzes (1-6)-alpha-D-glucosidic linkages in pullulan
pullulanase type I
-
hydrolyzes (1-6)-alpha-D-glucosidic linkages in pullulan
pullulanase type II
-
hydrolyzes (1-6)-alpha-D-glucosidic linkages in pullulan and (1-4)-alpha-linkages in other polysaccharides
pullulanase type II
-
hydrolyzes (1-6)-alpha-D-glucosidic linkages in pullulan and (1-4)-alpha-linkages in other polysaccharides
pullulanase type II
-
hydrolyzes (1-6)-alpha-D-glucosidic linkages in pullulan and (1-4)-alpha-linkages in other polysaccharides
pullulanase type II
-
hydrolyzes (1-6)-alpha-D-glucosidic linkages in pullulan and (1-4)-alpha-linkages in other polysaccharides
pullulanase type II
-
hydrolyzes (1-6)-alpha-D-glucosidic linkages in pullulan and (1-4)-alpha-linkages in other polysaccharides
pullulanase type II
-
hydrolyzes (1-6)-alpha-D-glucosidic linkages in pullulan and (1-4)-alpha-linkages in other polysaccharides
pullulanase type II
-
hydrolyzes (1-6)-alpha-D-glucosidic linkages in pullulan and (1-4)-alpha-linkages in other polysaccharides
pullulanase type II
-
hydrolyzes (1-6)-alpha-D-glucosidic linkages in pullulan and (1-4)-alpha-linkages in other polysaccharides
pullulanase type II
-
hydrolyzes (1-6)-alpha-D-glucosidic linkages in pullulan and (1-4)-alpha-linkages in other polysaccharides
pullulanase type II
-
hydrolyzes (1-6)-alpha-D-glucosidic linkages in pullulan and (1-4)-alpha-linkages in other polysaccharides
pullulanase type II
-
hydrolyzes (1-6)-alpha-D-glucosidic linkages in pullulan and (1-4)-alpha-linkages in other polysaccharides
pullulanase type II
-
hydrolyzes (1-6)-alpha-D-glucosidic linkages in pullulan and (1-4)-alpha-linkages in other polysaccharides
pullulanase type II
-
hydrolyzes (1-6)-alpha-D-glucosidic linkages in pullulan and (1-4)-alpha-linkages in other polysaccharides
pullulanase type II
-
hydrolyzes (1-6)-alpha-D-glucosidic linkages in pullulan and (1-4)-alpha-linkages in other polysaccharides
pullulanase type II
-
hydrolyzes (1-6)-alpha-D-glucosidic linkages in pullulan and (1-4)-alpha-linkages in other polysaccharides
pullulanase type II
-
hydrolyzes (1-6)-alpha-D-glucosidic linkages in pullulan and (1-4)-alpha-linkages in other polysaccharides
-
pullulanase type II
-
hydrolyzes (1-6)-alpha-D-glucosidic linkages in pullulan and (1-4)-alpha-linkages in other polysaccharides
pullulanase type II
Thermoanaerobium sp.
-
hydrolyzes (1-6)-alpha-D-glucosidic linkages in pullulan and (1-4)-alpha-linkages in other polysaccharides
additional information
-
the enzyme belongs to a family of 13 glycosyl hydrolases, also called the alpha-amylase family
additional information
-
the enzyme belongs to the glycosidase family GH13
additional information
-
the enzyme belongs to the glycosyl hydrolase 13 family, GH13
Promozyme 200 L
additional information
-
a heat-stable pullulanase, pullulan 6-glucanohydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(Glcalpha(1-4)Glcalpha(1-4)Glcalpha(1-6))n + H2O = alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranose + (Glcalpha(1-4)Glcalpha(1-4)Glcalpha(1-6))n-1
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
hydrolysis of O-glycosyl bond
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
pullulan 6-alpha-glucanohydrolase
Different from EC 3.2.1.142 (limit dextrinase) in its action on glycogen, and its rate of hydrolysis of limit dextrins. Its action on amylopectin is complete. Maltose is the smallest sugar that it can release from an alpha-(1->6)-linkage.
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CAS REGISTRY NUMBER
COMMENTARY
9075-68-7
-
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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
42-O-beta-D-galactosyl-maltose + beta-cyclodextrin
(Gal-G2)-beta-cyclodextrin + (Gal-G2)2-beta-cyclodextrin
-
analysis of reaction conditions and structural identification of products
-
-
r
amylopectin + H2O
maltohexaose + maltopentaose + maltotetraose + maltotriose + maltose + D-glucose
cyclomaltooctaose + H2O
6,6-di-O-alpha-maltosyl-cG8
-
gamma-cyclodextrin
-
-
?
maltose + cG8
6-O-alpha-maltosyl-cG8
-
through the reversed action
-
-
r
pullulan + H2O
malto-2-4-oligosaccharide + ?
-
best substrate
-
-
?
pullulan + H2O
maltotriose + maltose + D-glucose
this enzyme can attack alpha-1,6- and alpha-1,4-glycosidic linkages in pullulan, and produce a mixture of maltotriose, maltose and glucose
-
-
?
soluble starch + H2O
maltotriose + maltose + maltooligosaccharides
12.8% of the activity with pullulan
-
-
?
starch + H2O
maltohexaose + maltopentaose + maltotetraose + maltotriose + maltose + D-glucose
4-nitrophenyl alpha-D-maltoheptaoside + H2O
4-nitrophenol + alpha-D-maltoheptaose
-
hydrolyzed in an exo-fashion
-
-
?
4-nitrophenyl alpha-D-maltoheptaoside + H2O
4-nitrophenol + alpha-D-maltoheptaose
-
hydrolyzed in an exo-fashion
-
-
?
4-nitrophenyl alpha-D-maltoheptaoside + H2O
4-nitrophenol + alpha-D-maltoheptaose
-
hydrolyzed in an exo-fashion
-
-
?
4-nitrophenyl alpha-D-maltotrioside + H2O
4-nitrophenol + alpha-D-maltotriose
-
hydrolyzed in an exo-fashion
-
-
?
4-nitrophenyl alpha-D-maltotrioside + H2O
4-nitrophenol + alpha-D-maltotriose
-
hydrolyzed in an exo-fashion
-
-
?
6-O-alpha-maltosyl cyclodextrin + H2O
glucose + cyclodextrin
-
similar enzyme
-
-
?
6-O-alpha-maltosyl cyclodextrin + H2O
glucose + cyclodextrin
-
similar enzyme
-
-
?
6-O-alpha-maltotriosyl cyclomaltoheptaose + H2O
glucose + cyclodextrin
-
-
-
-
?
6-O-alpha-maltotriosyl cyclomaltoheptaose + H2O
glucose + cyclodextrin
-
similar enzyme
-
-
?
6-O-alpha-maltotriosyl cyclomaltohexaose + H2O
glucose + cyclodextrin
-
similar enzyme
-
-
?
6-O-alpha-maltotriosyl cyclomaltohexaose + H2O
glucose + cyclodextrin
-
similar enzyme
-
-
?
amylopectin + H2O
?
35% of activity compared to pullulan
-
-
?
amylopectin + H2O
?
the enzyme specifically attacks alpha-1,6-linkages of branched oligosaccharides
-
-
?
amylopectin + H2O
?
Geobacillus thermocatenulatus DSMZ730
the enzyme specifically attacks alpha-1,6-linkages of branched oligosaccharides
-
-
?
amylopectin + H2O
?
12% of the activity compared to pullulan
-
-
?
amylopectin + H2O
?
the enzyme prefers to debranch the DP6-12 side chains of amylopectin at pH 4.5 and 100°C
-
-
?
amylopectin + H2O
?
the enzyme prefers to debranch the DP6-12 side chains of amylopectin at pH 4.5 and 100°C
-
-
?
amylopectin + H2O
D-glucose + maltose + maltotriose
the enzyme can degrade both the alpha-1,4 and alpha-1,6-linkages of alpha-glucans
-
-
?
amylopectin + H2O
D-glucose + maltose + maltotriose
the enzyme can degrade both the alpha-1,4 and alpha-1,6-linkages of alpha-glucans
-
-
?
amylopectin + H2O
maltohexaose + maltopentaose + maltotetraose + maltotriose + maltose + D-glucose
-
-
-
?
amylopectin + H2O
maltohexaose + maltopentaose + maltotetraose + maltotriose + maltose + D-glucose
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
-
34.1% of the rate with pullulan
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
Thermoanaerobium sp.
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltotriose + maltose + ?
-
-
-
?
amylopectin + H2O
maltotriose + maltose + ?
-
-
-
?
amylopectin + H2O
maltotriose + maltose + maltooligosaccharides
6.0% of the activity with pullulan
-
-
?
amylopectin + H2O
maltotriose + maltose + maltooligosaccharides
6.0% of the activity with pullulan
-
-
?
amylopectin + H2O
maltotriose + maltotetraose + maltopentaose + maltohexaose
28% of the activity compared to pullulan, the enzyme hydrolyzes amylopectin to release mainly maltotriose, maltotetraose, maltopentaose and maltohexaose, and their contents reach to 0.0044, 0.0068, 0.0073, 0.025 and 0.035 mg/ml, respectively, after 2 h incubation
-
-
?
amylopectin + H2O
maltotriose + maltotetraose + maltopentaose + maltohexaose
Priestia megaterium WW1210
28% of the activity compared to pullulan, the enzyme hydrolyzes amylopectin to release mainly maltotriose, maltotetraose, maltopentaose and maltohexaose, and their contents reach to 0.0044, 0.0068, 0.0073, 0.025 and 0.035 mg/ml, respectively, after 2 h incubation
-
-
?
amylose + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylose + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylose + H2O
maltotriose + maltose
-
-
-
?
beta-cyclodextrin + H2O
?
21% of activity compared to pullulan
-
-
?
beta-cyclodextrin + H2O
?
in the initial stages, the ring-opening reactions of 6-O-glucosyl-beta-cyclodextrin, 6-O-maltosyl-beta-cyclodextrin and the debranching reactions of 6-O-maltooctaosyl-beta-cyclodextrin are firstly catalyzed. In the subsequent reactions, a serial of maltooligosaccharides are produced
-
-
?
beta-cyclodextrin + H2O
?
in the initial stages, the ring-opening reactions of 6-O-glucosyl-beta-cyclodextrin, 6-O-maltosyl-beta-cyclodextrin and the debranching reactions of 6-O-maltooctaosyl-beta-cyclodextrin are firstly catalyzed. In the subsequent reactions, a serial of maltooligosaccharides are produced
-
-
?
beta-limited dextrin + H2O
maltotriose + maltose + maltooligosaccharides
19.7% of the activity with pullulan
-
-
?
beta-limited dextrin + H2O
maltotriose + maltose + maltooligosaccharides
19.7% of the activity with pullulan
-
-
?
gamma-cyclodextrin + H2O
?
71% of activity compared to pullulan
-
-
?
gamma-cyclodextrin + H2O
?
in the initial stages, the ring-opening reactions of gamma-cyclodextrin is firstly catalyzed. In the subsequent reactions, a serial of maltooligosaccharides are produced
-
-
?
glycogen + H2O
?
-
hydrolyzed slowly. Hydrolyzed in an endo fashion to form a series of oligosaccharides as small as glucose, with the majority of product in the DP4 to DP6 range
-
-
?
glycogen + H2O
?
the enzyme can degrade both alpha-1,4 and alpha-1,6-linkages of alpha-glucan
-
-
?
glycogen + H2O
?
the enzyme can degrade both alpha-1,4 and alpha-1,6-linkages of alpha-glucan
-
-
?
glycogen + H2O
?
-
hydrolyzed slowly. Hydrolyzed in an endo fashion to form a series of oligosaccharides as small as glucose, with the majority of product in the DP4 to DP6 range
-
-
?
glycogen + H2O
?
-
hydrolyzed slowly. Hydrolyzed in an endo fashion to form a series of oligosaccharides as small as glucose, with the majority of product in the DP4 to DP6 range
-
-
?
glycogen + H2O
maltooligosaccharides + maltose
-
-
6.3% of the rate with pullulan
-
?
glycogen + H2O
maltooligosaccharides + maltose
-
-
-
-
?
glycogen + H2O
maltotriose + maltose + maltooligosaccharides
6.1% of the activity with pullulan
-
-
?
glycogen + H2O
maltotriose + maltose + maltooligosaccharides
6.1% of the activity with pullulan
-
-
?
glycogen beta-limit dextrin + H2O
maltotriose + maltose + maltosetetraose
-
-
-
-
?
glycogen beta-limit dextrin + H2O
maltotriose + maltose + maltosetetraose
-
-
-
-
?
glycogen beta-limit dextrin + H2O
maltotriose + maltose + maltosetetraose
-
-
-
-
?
glycogen beta-limit dextrin + H2O
maltotriose + maltose + maltosetetraose
-
-
-
-
?
glycogen beta-limit dextrin + H2O
maltotriose + maltose + maltosetetraose
-
-
-
-
?
glycogen beta-limit dextrin + H2O
maltotriose + maltose + maltosetetraose
-
-
-
-
?
glycogen beta-limit dextrin + H2O
maltotriose + maltose + maltosetetraose
-
-
-
-
?
glycogen beta-limit dextrin + H2O
maltotriose + maltose + maltosetetraose
-
-
-
-
?
glycogen beta-limit dextrin + H2O
maltotriose + maltose + maltosetetraose
-
-
-
-
?
maltoheptaose + H2O
maltotriose + maltose + D-glucose
-
-
-
-
?
maltoheptaose + H2O
maltotriose + maltose + D-glucose
-
-
-
-
?
maltohexaose + H2O
maltotriose + maltose + D-glucose + maltotetraose
-
-
-
-
?
maltohexaose + H2O
maltotriose + maltose + D-glucose + maltotetraose
-
-
-
-
?
maltohexaose + H2O
maltotriose + maltose + D-glucose + maltotetraose
-
-
-
-
?
maltotetraose + H2O
maltose + glucose + maltotriose
-
-
-
-
?
pullulan + H2O
?
-
substrate from Aureobasidium pullulans strain FB-1
-
-
?
pullulan + H2O
?
-
pullalan synthesized by Aureobasidium pullulans strain AP329 as exopolysaccharide and purified, development of a colorimetric assay method for pullalan quantification, overview
-
-
?
pullulan + H2O
maltotriose + ?
EPZ37738
soluble enzyme is highly reactive towards pullulan but was unable to degrade short branches in starch
-
-
?
pullulan + H2O
maltotriose + ?
Anoxybacillus ayderensis DSM 28779
EPZ37738
soluble enzyme is highly reactive towards pullulan but was unable to degrade short branches in starch
-
-
?
pullulan + H2O
maltotriose + ?
-
preparation of maltotriose by hydrolyzing of pullulan with pullulanase, overview
-
-
?
pullulan + H2O
maltotriose + ?
-
complete conversion to maltotriose
-
?
pullulan + H2O
maltotriose + ?
-
complete conversion to maltotriose
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
specific for pullulan 1,6-glycosidic linkages
-
-
?
pullulan + H2O
maltotriose + ?
-
specific for pullulan 1,6-glycosidic linkages
-
-
?
pullulan + H2O
maltotriose + ?
the enzyme exhibits strict substrate specificity towards pullulan, but shows relatively low activity towards amylopectin and no activity towards other tested polysaccharides
-
-
?
pullulan + H2O
maltotriose + ?
the enzyme hydrolyzes pullulan to yield mainly maltotriose, more than 95%
-
-
?
pullulan + H2O
maltotriose + ?
Priestia megaterium WW1210
the enzyme hydrolyzes pullulan to yield mainly maltotriose, more than 95%
-
-
?
pullulan + H2O
maltotriose + ?
-
higher specific activity against pullulan than against starch. Enzyme attacks only the alpha-1,6 linkages in pullulan
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
higher specific activity against pullulan than against starch. Enzyme attacks only the alpha-1,6 linkages in pullulan
-
-
?
pullulan + H2O
maltotriose + ?
-
higher specific activity against pullulan than against starch. Enzyme attacks only the alpha-1,6 linkages in pullulan
-
-
?
soluble starch
maltotriose + maltose
-
-
-
-
?
soluble starch + H2O
?
17% of the activity with pullulan
-
-
?
soluble starch + H2O
?
the enzyme specifically attacks alpha-1,6-linkages of branched oligosaccharides
-
-
?
soluble starch + H2O
?
Geobacillus thermocatenulatus DSMZ730
the enzyme specifically attacks alpha-1,6-linkages of branched oligosaccharides
-
-
?
soluble starch + H2O
maltotriose + maltose
-
-
-
?
soluble starch + H2O
maltotriose + maltose
-
-
-
?
starch + H2O
?
-
together with amylase, both enzymes immobilized on calcium alginate beads
-
-
?
starch + H2O
?
-
higher specific activity against pullulan than against starch. Hydrolyzed in an endo fashion to form a series of oligosaccharides as small as glucose, with the majority of product in the DP4 to DP6 range
-
-
?
starch + H2O
?
-
higher specific activity against pullulan than against starch. Hydrolyzed in an endo fashion to form a series of oligosaccharides as small as glucose, with the majority of product in the DP4 to DP6 range
-
-
?
starch + H2O
?
-
higher specific activity against pullulan than against starch. Hydrolyzed in an endo fashion to form a series of oligosaccharides as small as glucose, with the majority of product in the DP4 to DP6 range
-
-
?
starch + H2O
D-glucose + maltose + maltotriose
the enzyme can degrade both the alpha-1,4 and alpha-1,6-linkages of alpha-glucans
-
-
?
starch + H2O
D-glucose + maltose + maltotriose
the enzyme can degrade both the alpha-1,4 and alpha-1,6-linkages of alpha-glucans
-
-
?
starch + H2O
maltohexaose + maltopentaose + maltotetraose + maltotriose + maltose + D-glucose
-
-
-
?
starch + H2O
maltohexaose + maltopentaose + maltotetraose + maltotriose + maltose + D-glucose
-
-
-
?
starch + H2O
maltotriose + oligosaccharides
EPZ37738
following immobilization through covalent attachment to three epoxides (ReliZyme EP403/M, ImmobeadIB-150P, and Immobead IB-150A) and an amino-epoxide (ReliZyme HFA403/M), all PulASK derivatives are active on both short and long branches in starch producing reducing sugars (predominantly maltotriose) and oligosaccharides (chain lenght G8 and higher), respectively, a feature that is absent in the free enzyme. Individual or coimmobilization causes changes in the product specificity, presumably due to changes in the enzyme binding pocket caused by the influence of carrier surface properties (hydrophobicor hydrophilic) and the lengths of the spacer arms
-
-
?
starch + H2O
maltotriose + oligosaccharides
Anoxybacillus ayderensis DSM 28779
EPZ37738
following immobilization through covalent attachment to three epoxides (ReliZyme EP403/M, ImmobeadIB-150P, and Immobead IB-150A) and an amino-epoxide (ReliZyme HFA403/M), all PulASK derivatives are active on both short and long branches in starch producing reducing sugars (predominantly maltotriose) and oligosaccharides (chain lenght G8 and higher), respectively, a feature that is absent in the free enzyme. Individual or coimmobilization causes changes in the product specificity, presumably due to changes in the enzyme binding pocket caused by the influence of carrier surface properties (hydrophobicor hydrophilic) and the lengths of the spacer arms
-
-
?
additional information
?
-
EPZ37738
the enzyme preferably debranches long branches at alpha-1,6 glycosidic bonds of starch, producing amylose, linear or branched oligosaccharides, but is nonreactive against short branches. In addition, the enzyme acts as limit dextrinase, reaction of EC 3.2.1.142, releasing maltotriose, maltotetraose and maltopentaose from limit dextrin
-
-
?
additional information
?
-
EPZ37738
the enzyme preferably debranches long branches at alpha-1,6 glycosidic bonds of starch, producing amylose, linear or branched oligosaccharides, but is nonreactive against short branches. In addition, the enzyme acts as limit dextrinase, reaction of EC 3.2.1.142, releasing maltotriose, maltotetraose and maltopentaose from limit dextrin
-
-
?
additional information
?
-
-
pullulanase is a debranching enzyme which hydrolyses the alpha-1,6-glucosidic linkages in pullulan and other amylaceous polysaccharides
-
-
?
additional information
?
-
-
pullulanase effectively hydrolyzes pullulan, soluble starch and dextran
-
-
?
additional information
?
-
-
the BaPul13A active centre in which hydrolysis of alpha-1,6 linkages occurs with net retention of anomeric configuration, via a covalent glycosyl-enzyme intermediate. Complete starch hydrolysis requires a consortium of enzymes including endo-amylases, glucoamylases and alpha-glucosidases as well as diverse alpha-1,6 cleaving enzymes including pullulanases
-
-
?
additional information
?
-
-
the enzyme hydrolyzes alpha-1,6-glucosidic linkages in polysacchrides
-
-
?
additional information
?
-
-
with glycogen and branched beta-cyclodextrins as substrates, pullulanase shows high-level specificity for the hydrolysis of the outer side chains of glycogen with three to five glucosyl residues. Debranching of the outer side chain of glycogen by pullulanase AmyX
-
-
?
additional information
?
-
-
with glycogen and branched beta-cyclodextrins as substrates, pullulanase shows high-level specificity for the hydrolysis of the outer side chains of glycogen with three to five glucosyl residues. Debranching of the outer side chain of glycogen by pullulanase AmyX
-
-
?
additional information
?
-
no substrates: maltotriose, maltose
-
-
?
additional information
?
-
-
no substrates: maltotriose, maltose
-
-
?
additional information
?
-
no substrates: maltotriose, maltose
-
-
?
additional information
?
-
-
no substrates: maltotriose, maltose
-
-
?
additional information
?
-
negligible activity on wheat flour and maltodextrin, no activity on amylose
-
-
?
additional information
?
-
the enzyme has no activity toward alpha-1,4-glycosidic linkages
-
-
?
additional information
?
-
-
the enzyme has no activity toward alpha-1,4-glycosidic linkages
-
-
?
additional information
?
-
Geobacillus thermocatenulatus DSMZ730
the enzyme has no activity toward alpha-1,4-glycosidic linkages
-
-
?
additional information
?
-
-
NPDE exhibits a unique catalytic preference for longer malto-oligosaccharides with more than 8 monomers, performing hydrolysis without the transgylcosylation or CD-hydrolyzing activities of other GH-13 enzymes
-
-
?
additional information
?
-
-
NPDE hydrolyzes both alpha-1,4- and alpha-1,6-glucosidic linkages with a substrate specificity in descending order of pullulan, amylopectin, starch, amylose. NPDE has no specificity for alpha-, beta-, and gamma-cyclodextris, and hydrolyzes alpha-1,6-glucosidic linkages more rapidly than alpha-1,4-glucosidic linkages. NPDE hydrolyzes the alpha-1,6 glycosidic linkages of malto-oligosaccharides, molecular basis for the substrate specificity and the catalytic properties, overview
-
-
?
additional information
?
-
-
enzyme exhibits alpha-glucosyltransfer activity and produces an alpha-(1-6) linked compound of two maltotriose molecules from pullulan
-
-
?
additional information
?
-
the enzyme does not show activity towards amylose, maltoheptaose, maltohexaose, maltopentaose and maltotetraose
-
-
?
additional information
?
-
-
the enzyme does not show activity towards amylose, maltoheptaose, maltohexaose, maltopentaose and maltotetraose
-
-
?
additional information
?
-
Priestia megaterium WW1210
the enzyme does not show activity towards amylose, maltoheptaose, maltohexaose, maltopentaose and maltotetraose
-
-
?
additional information
?
-
-
hydrolyzes the alpha-1,6 linkage in pullulan, alpha-1,4 linkages in amylose and soluble starch. No activity against maltohexaose or other smaller alpha-1,4-linked oligosaccharides
-
-
?
additional information
?
-
the enzyme also hydrolyzes oligosaccharides but much slower. The longer the oligosaccharide chain, the higher the hydrolysis rate
-
-
?
additional information
?
-
-
the enzyme also hydrolyzes oligosaccharides but much slower. The longer the oligosaccharide chain, the higher the hydrolysis rate
-
-
?
additional information
?
-
-
hydrolysis of freeze-dried waxy maize starch nanocrystals by pullulanase isoamylase as debranching enzymes and by beta-amylase, cleavage profile, overview
-
-
?
additional information
?
-
-
PulA knock-out strains display decreased binding to epithelial cells
-
-
?
additional information
?
-
the enzyme can degrade both alpha-1,4 and alpha-1,6-linkages of alpha-glucan
-
-
?
additional information
?
-
the enzyme can degrade both alpha-1,4 and alpha-1,6-linkages of alpha-glucan
-
-
?
additional information
?
-
the enzyme cleaves both alpha-1,4- and alpha-1,6-glycosidic linkages in starch, pullulan, amylopectin, and other related oligosaccharides
-
-
?
additional information
?
-
the enzyme cleaves both alpha-1,4- and alpha-1,6-glycosidic linkages in starch, pullulan, amylopectin, and other related oligosaccharides
-
-
?
additional information
?
-
-
the enzyme cleaves both alpha-1,4- and alpha-1,6-glycosidic linkages in starch, pullulan, amylopectin, and other related oligosaccharides
-
-
?
additional information
?
-
-
hydrolyzes the alpha-1,6 linkage in pullulan, alpha-1,4 linkages in amylose and soluble starch. No activity against maltohexaose or other smaller alpha-1,4-linked oligosaccharides
-
-
?
additional information
?
-
-
hydrolyzes the alpha-1,6 linkage in pullulan, alpha-1,4 linkages in amylose and soluble starch. No activity against maltohexaose or other smaller alpha-1,4-linked oligosaccharides
-
-
?
additional information
?
-
amylopullulanases (type II pullulanases) are able to degrade both the alpha-1,6 and alpha-1,4 glucosidic bonds of starch
-
-
?
additional information
?
-
-
amylopullulanases (type II pullulanases) are able to degrade both the alpha-1,6 and alpha-1,4 glucosidic bonds of starch
-
-
?
additional information
?
-
amylopullulanases (type II pullulanases) are able to degrade both the alpha-1,6 and alpha-1,4 glucosidic bonds of starch
-
-
?
additional information
?
-
no substrate: amylose. Enzyme displays transglycosylation activity, transferring the maltotriosyl residue of pullulan to aesculin by forming alpha-1,6-glucosidic linkages
-
-
?
additional information
?
-
-
no substrate: amylose. Enzyme displays transglycosylation activity, transferring the maltotriosyl residue of pullulan to aesculin by forming alpha-1,6-glucosidic linkages
-
-
?
additional information
?
-
enzyme requires at least two glucose units in linear chain to be released by cleavage of an alpha-1,6-linkage
-
-
?
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NATURAL SUBSTRATE
NATURAL 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
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
Thermoanaerobium sp.
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
additional information
?
-
-
pullulanase is a debranching enzyme which hydrolyses the alpha-1,6-glucosidic linkages in pullulan and other amylaceous polysaccharides
-
-
?
additional information
?
-
-
NPDE exhibits a unique catalytic preference for longer malto-oligosaccharides with more than 8 monomers, performing hydrolysis without the transgylcosylation or CD-hydrolyzing activities of other GH-13 enzymes
-
-
?
additional information
?
-
-
PulA knock-out strains display decreased binding to epithelial cells
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
Ca2+
CaCl2
1 mM, 1.8fold activation. 5 mM, 66% loss of activity. 10 mM, 97% loss of activity
Co2+
Cu2+
Fe2+
K+
Mg2+
MgCl2
1 mM, 1.5fold activation. 5 mM, 1.8fold activation. 10 mM, 1.1fold activation
Mn2+
Na+
NaCl
Halorubrum sp. Ha25
-
the enzyme is active over a wide range of concentrations (04.5 M) of NaCl
Ni2+
Sr2+
additional information
Ca2+
-
thermoactivity and thermostability of the enzyme is enhanced in the presence of 5 mM Ca2+, and under these conditions, enzyme activity can be measured at temperatures of up to 130 to 140°C
Ca2+
-
thermoactivity and thermostability of the enzyme is enhanced in the presence of 5 mM Ca2+, and under these conditions, enzyme activity can be measured at temperatures of up to 130 to 140°C
additional information
-
Fe2+, Mg2+, Ba2+, K+, Na+ or Zn2+ have no effect
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CaCl2
1 mM, 1.8fold activation. 5 mM, 66% loss of activity. 10 mM, 97% loss of activity
beta-cyclodextrin
-
10 mM, 90% loss of activity. Activity of pullulanase remains at more than 40% when mixtures containing beta-cyclodextrin and sodium benzoate are added. Side chain groups lead to decrease the interaction between hydrophobic cavities of beta-cyclodextrin and pullulanase molecules
Ca2+
-
5 mM, starch-hydrolyzing activity is inhibited by about 30%, hydrolytic activity against glycogen is slightly inhibited
Ca2+
-
5 mM, starch-hydrolyzing activity is inhibited by about 14%, hydrolytic activity against glycogen is slightly inhibited
Mg2+
-
reduces the thermoactivity of the enzymes below the level seen in the absence of added metal
Mg2+
-
reduces the thermoactivity of the enzymes below the level seen in the absence of added metal
additional information
-
the interaction between cyclodextrins and pullulanase is closely related to the sizes of hydrophobic cavities within cyclodextrins
-
additional information
-
EDTA has no effect, phenylmethanesulfonyl fluoride has no effect
-
additional information
-
EDTA has no effect, phenylmethanesulfonyl fluoride and diisopropylflurophosphate have almost no effect
-
additional information
not inhibitory: iodoacetamide, Triton X-100, Mn2+, Mg2+, Ca2+
-
additional information
-
not inhibitory: iodoacetamide, Triton X-100, Mn2+, Mg2+, Ca2+
-
additional information
enzyme retains 99, 89, and 54% of its activity at 10% concentration of Triton-X100, Tween 20, and SDS, respectively. The enzyme retains 80.4 and 93.7% activity in the presence of commercial detergents Rika (7.5% v/v) and Fadisheh (2.5% w/v), respectively
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
maltodextrin
-
activation is caused by an endotransglycosylation reaction catalyzed by EC 3.2.1.41
thioredoxin
upon preincubation with both dithiothreitol and thioredoxin, the initial reaction velocity increases by a factor of two
Ca2+
-
5 mM, the pullulan hydrolyzing activity is stimulated by about 25%, slight enhancing effect on hydrolysis of 4-nitrophenyl-alpha-D-maltotrioside
Ca2+
-
5 mM, the pullulan hydrolyzing activity is stimulated by about 25%, slight enhancing effect on hydrolysis of 4-nitrophenyl-alpha-D-maltotrioside
dithiothreitol
upon preincubation with both dithiothreitol and thioredoxin, the initial reaction velocity increases by a factor of two
Triton X-100
0.1%, 1.2fold activation. 1%, 1.3fold activation
Triton X-100
0.1-5.0%, activity on pullulan doubles after preincubation
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Blister
Immunocytochemical Identification and Localization of Active and Inactive alpha-Amylase and Pullulanase in Cells of Clostridium thermosulfurogenes EM1.
Carcinogenesis
Human DBR1 modulates the recycling of snRNPs to affect alternative RNA splicing and contributes to the suppression of cancer development.
Cardiomyopathies
Glycogen storage disease type III (glycogen debranching enzyme deficiency): correlation of biochemical defects with myopathy and cardiomyopathy.
Cardiomyopathies
Successful treatment of severe cardiomyopathy in glycogen storage disease type III with D,L-3-hydroxybutyrate, ketogenic and high protein diet.
Cardiomyopathy, Hypertrophic
A case of glycogen storage disease type III (glycogen debranching enzyme deficiency) with liver cirrhosis and hypertrophic cardiomyopathy.
Genetic Diseases, Inborn
[Biological and physiopathological aspects of hepatic glycogenoses]
Glycogen Storage Disease
A case of glycogen storage disease type III (glycogen debranching enzyme deficiency) with liver cirrhosis and hypertrophic cardiomyopathy.
Glycogen Storage Disease
Debranching enzyme in fibroblasts, amniotic fluid cells and chorionic villi: pre- and postnatal diagnosis of glycogenosis type III.
Glycogen Storage Disease
Definitive prenatal diagnosis for type III glycogen storage disease.
Glycogen Storage Disease
Effects of acute nutritional ketosis during exercise in adults with glycogen storage disease type IIIa are phenotype-specific: An investigator-initiated, randomized, crossover study.
Glycogen Storage Disease
Glycogen debranching enzyme deficiency: long-term study of serum enzyme activities and clinical features.
Glycogen Storage Disease
Glycogen debranching enzyme: purification, antibody characterization, and immunoblot analyses of type III glycogen storage disease.
Glycogen Storage Disease
Glycogen storage disease type III (glycogen debranching enzyme deficiency): correlation of biochemical defects with myopathy and cardiomyopathy.
Glycogen Storage Disease
Heart Failure Due to Severe Hypertrophic Cardiomyopathy Reversed by Low Calorie, High Protein Dietary Adjustments in a Glycogen Storage Disease Type IIIa Patient.
Glycogen Storage Disease
Hexose and protein tolerance tests in children with liver glycogenosis caused by a deficiency of the debranching enzyme system.
Glycogen Storage Disease
Identification of a 5' splice junction mutation in the debranching enzyme gene in a Japanese patient with glycogen storage disease type IIIa.
Glycogen Storage Disease
Phenylketonuria and glycogen storage disease type III in sibs of one family.
Glycogen Storage Disease
Reversal of glycogen storage disease type IIIa-related cardiomyopathy with modification of diet.
Glycogen Storage Disease
Some properties of fibroblasts from a patient with debrancher deficiency.
Glycogen Storage Disease
Successful treatment of severe cardiomyopathy in glycogen storage disease type III with D,L-3-hydroxybutyrate, ketogenic and high protein diet.
Glycogen Storage Disease
Type IIIb glycogen storage disease associated with end-stage cirrhosis and hepatocellular carcinoma. The Liver Transplant Group.
Glycogen Storage Disease
Uniparental isodisomy of chromosome 1 results in glycogen storage disease type III with profound growth retardation.
Glycogen Storage Disease
[Biological and physiopathological aspects of hepatic glycogenoses]
Glycogen Storage Disease
[Debranching enzyme activity in leukocytes and glycogen content of erythrocytes in patients with type III glycogenosis]
Glycogen Storage Disease Type III
A case of glycogen storage disease type III (glycogen debranching enzyme deficiency) with liver cirrhosis and hypertrophic cardiomyopathy.
Glycogen Storage Disease Type III
Glycogen debranching enzyme deficiency: long-term study of serum enzyme activities and clinical features.
Glycogen Storage Disease Type III
Glycogen storage disease type III (glycogen debranching enzyme deficiency): correlation of biochemical defects with myopathy and cardiomyopathy.
Glycogen Storage Disease Type III
Heart Failure Due to Severe Hypertrophic Cardiomyopathy Reversed by Low Calorie, High Protein Dietary Adjustments in a Glycogen Storage Disease Type IIIa Patient.
Glycogen Storage Disease Type III
Reversal of glycogen storage disease type IIIa-related cardiomyopathy with modification of diet.
Glycogen Storage Disease Type III
Successful treatment of severe cardiomyopathy in glycogen storage disease type III with D,L-3-hydroxybutyrate, ketogenic and high protein diet.
Glycogen Storage Disease Type III
Uniparental isodisomy of chromosome 1 results in glycogen storage disease type III with profound growth retardation.
Glycogen Storage Disease Type V
Glycogen debrancher deficiency is reproduced in muscle culture.
Hepatomegaly
Successful treatment of severe cardiomyopathy in glycogen storage disease type III with D,L-3-hydroxybutyrate, ketogenic and high protein diet.
Hypoglycemia
Successful treatment of severe cardiomyopathy in glycogen storage disease type III with D,L-3-hydroxybutyrate, ketogenic and high protein diet.
Infections
Conformational Changes in the 5' End of the HIV-1 Genome Dependent on the Debranching Enzyme DBR1 During Early Stages of Infection.
Infections
Fluorescent Branched RNAs for High-Throughput Analysis of Dbr1 Enzyme Kinetics and Inhibition.
Liver Cirrhosis
A case of glycogen storage disease type III (glycogen debranching enzyme deficiency) with liver cirrhosis and hypertrophic cardiomyopathy.
Meningoencephalitis
New immunodeficiency syndromes that help us understand the IFN-mediated antiviral immune response.
Muscular Diseases
Deep morphological analysis of muscle biopsies from type III glycogenesis (GSDIII), debranching enzyme deficiency, revealed stereotyped vacuolar myopathy and autophagy impairment.
Muscular Diseases
Glycogen storage disease type III (glycogen debranching enzyme deficiency): correlation of biochemical defects with myopathy and cardiomyopathy.
Muscular Diseases
Investigating glycogenosis type III patients with multi-parametric functional NMR imaging and spectroscopy.
Myopathies, Nemaline
[A 22-year-old man with long-standing weakness and atrophy predominantly in the lower extremities]
Neurodegenerative Diseases
Design, Synthesis, and Properties of Phosphoramidate 2',5'-Linked Branched RNA: Toward the Rational Design of Inhibitors of the RNA Lariat Debranching Enzyme.
Neurodegenerative Diseases
Fluorescent Branched RNAs for High-Throughput Analysis of Dbr1 Enzyme Kinetics and Inhibition.
Pemphigoid, Bullous
Differential display and cloning of the hippocampal gene mRNas in senescence accelerated mouse.
phosphorylase kinase deficiency
Myopathy due to glycogen storage disease: pathological and biochemical studies in relation to glycogenosome formation.
Pneumococcal Infections
Immune response to capsular polysaccharide and surface proteins of Streptococcus pneumoniae in patients with invasive pneumococcal disease.
Pneumonia
Characterization and expression of the structural gene for pullulanase, a maltose-inducible secreted protein of Klebsiella pneumoniae.
pullulanase deficiency
A Debranching Enzyme Deficiency in Endosperms of the Sugary-1 Mutants of Maize.
pullulanase deficiency
Debranching enzyme in fibroblasts, amniotic fluid cells and chorionic villi: pre- and postnatal diagnosis of glycogenosis type III.
pullulanase deficiency
Deep morphological analysis of muscle biopsies from type III glycogenesis (GSDIII), debranching enzyme deficiency, revealed stereotyped vacuolar myopathy and autophagy impairment.
pullulanase deficiency
Effects of acute nutritional ketosis during exercise in adults with glycogen storage disease type IIIa are phenotype-specific: An investigator-initiated, randomized, crossover study.
pullulanase deficiency
Glycogen storage disease type III (glycogen debranching enzyme deficiency): correlation of biochemical defects with myopathy and cardiomyopathy.
pullulanase deficiency
Investigating glycogenosis type III patients with multi-parametric functional NMR imaging and spectroscopy.
pullulanase deficiency
Phenylketonuria and glycogen storage disease type III in sibs of one family.
pullulanase deficiency
Successful treatment of severe cardiomyopathy in glycogen storage disease type III with D,L-3-hydroxybutyrate, ketogenic and high protein diet.
pullulanase deficiency
Uniparental isodisomy of chromosome 1 results in glycogen storage disease type III with profound growth retardation.
pullulanase deficiency
[A 22-year-old man with long-standing weakness and atrophy predominantly in the lower extremities]
Spondylitis, Ankylosing
Molecular mimicry and ankylosing spondylitis: possible role of a novel sequence in pullulanase of Klebsiella pneumoniae.
Starvation
Differential proteome and cellular adhesion analyses of the probiotic bacterium Lactobacillus acidophilus NCFM grown on raffinose - an emerging prebiotic.
Starvation
Mucin- and carbohydrate-stimulated adhesion and subproteome changes of the probiotic bacterium Lactobacillus acidophilus NCFM.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.067
4-nitrophenyl alpha-D-maltotrioside
-
pH 5.6, 98°C, no metal added
additional information
amylopectin
Km-value: 3.95 mg/ml, pH 3.5, 95°C
additional information
amylopectin
Km-value: 3.6 mg/ml, pH 6.5, 55°C
additional information
additional information
-
Km-value for pullulan is 1.284 mg/ml
-
additional information
additional information
-
kinetics and thermodynamics, overview
-
additional information
additional information
-
Ca2+ causes a 10fold decrease in Km
-
additional information
additional information
-
Ca2+ causes a 10fold decrease in Km
-
additional information
pullulan
Km-value for pullulan at pH 5.6, 98°C, no metal ion added: 1.6 mg/ml. Km-value for pullulan, at pH 5.6, 98°C, 0.5 mM Ca2+: 0.13 mg/ml
additional information
pullulan
-
Km-value for pullulan at pH 5.6, 98°C, no metal ion added: 1.6 mg/ml. Km-value for pullulan, at pH 5.6, 98°C, 0.5 mM Ca2+: 0.13 mg/ml
additional information
pullulan
Km value is 2.8 mg/ml, pH 8.5, 45°C
additional information
pullulan
Km value 0.12 mg/ml, pH 6.0, 50°C
additional information
pullulan
-
Km value 0.12 mg/ml, pH 6.0, 50°C
additional information
pullulan
Km-value: 0.08 mg/ml, pH 3.5, 95°C
additional information
pullulan
Ax203843.1
Km-value: 0.61 mg/ml, pH 5.0, 60°C, mutant enzyme L627R
additional information
pullulan
-
Km-value: 0.61 mg/ml, pH 5.0, 60°C, mutant enzyme L627R
additional information
pullulan
Ax203843.1
Km-value: 0.93 mg/ml, pH 5.0, 60°C, wild-type enzyme
additional information
pullulan
-
Km-value: 0.93 mg/ml, pH 5.0, 60°C, wild-type enzyme
additional information
pullulan
Anoxybacillus sp. WB42
Km-value: 16.5 mg/ml, pH 5.5, 60°C, mutant enzyme H5A/R6A/T7A
additional information
pullulan
Anoxybacillus sp. WB42
Km-value: 20.1 mg/ml, pH 5.5, 60°C, mutant enzyme R93T
additional information
pullulan
Anoxybacillus sp. WB42
Km-value: 22.3 mg/ml, pH 5.5, 60°C, mutant enzyme R93A
additional information
pullulan
Anoxybacillus sp. WB42
Km-value: 22.5 mg/ml, pH 5.5, 60°C, wild-type enzyme
additional information
pullulan
Anoxybacillus sp. WB42
Km-value: 24.4 mg/ml, pH 5.5, 60°C, mutant enzyme A90G
additional information
pullulan
Anoxybacillus sp. WB42
Km-value: 24.6 mg/ml, pH 5.5, 60°C, mutant enzyme A90D
additional information
pullulan
Anoxybacillus sp. WB42
Km-value: 29.7 mg/ml, pH 5.5, 60°C, mutant enzyme A90P
additional information
pullulan
Km-value: 3.3 mg/ml, pH 6.5, 55°C
additional information
pullulan
Anoxybacillus sp. WB42
Km-value: 31.2 mg/ml, pH 5.5, 60°C, mutant enzyme Q87A/L173D
additional information
pullulan
Anoxybacillus sp. WB42
Km-value: 4.7 mg/ml, pH 5.5, 60°C, mutant enzyme R93K
additional information
pullulan
Anoxybacillus sp. WB42
Km-value: 45.0 mg/ml, pH 5.5, 60°C, mutant enzyme A90S
additional information
pullulan
Anoxybacillus sp. WB42
Km-value: 5.6 mg/ml, pH 5.5, 60°C, mutant enzyme R93E
additional information
pullulan
Anoxybacillus sp. WB42
Km-value: 5.8 mg/ml, pH 5.5, 60°C, mutant enzyme L173D
additional information
pullulan
Anoxybacillus sp. WB42
Km-value: 6.0 mg/ml, pH 5.5, 60°C, mutant enzyme DELTA(N)
additional information
pullulan
Anoxybacillus sp. WB42
Km-value: 6.8 mg/ml, pH 5.5, 60°C, mutant enzyme Q87A
additional information
pullulan
-
Km: 1.01 mg/ml, pH 4.5, 60°C, 60 mM Mg2+
additional information
pullulan
-
Km: 1.06 mg/ml, pH 4.5, 60°C, without Mg2+
additional information
pullulan
Fontibacillus sp. DSHK 107
-
pH 5.0, 30°C, the apparent kcat/Km-values are 1.49, 1.54, and 0.59 mg/ml pullunan, respectively, for the soluble enzyme and pullulanase immobilized on Florisil and nano-silica
additional information
soluble starch
Km-value for soluble starch at pH 5.6, 98°C, no metal ion added: 2.48 mg/ml. Km-value for soluble starch at pH 5.6, 98°C, 0.5 mM Ca2+: 1.17 mg/ml
-
additional information
soluble starch
-
Km-value for soluble starch at pH 5.6, 98°C, no metal ion added: 2.48 mg/ml. Km-value for soluble starch at pH 5.6, 98°C, 0.5 mM Ca2+: 1.17 mg/ml
-
additional information
soluble starch
Km value 0.69 mg/ml,pH 6.0, 50°C
-
additional information
soluble starch
-
Km value 0.69 mg/ml,pH 6.0, 50°C
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1751
pullulan
truncated enzyme form ApuM957, at pH 5.0 and 70°C
1828
pullulan
truncated enzyme form ApuK855, at pH 5.0 and 70°C
574.7
soluble starch
truncated enzyme form ApuK855, at pH 6.0 and 70°C
-
877.9
soluble starch
truncated enzyme form ApuM957, at pH 6.0 and 70°C
-
additional information
pullulan
Km-value: 2.94 mg/ml, pH 5.5, 50°C
additional information
pullulan
-
Km-value: 2.94 mg/ml, pH 5.5, 50°C
additional information
pullulan
pH 4.5, 60°C, kcat of wild-type enzyme and mutant enzyme
additional information
pullulan
-
pH 4.5, 60°C, kcat of wild-type enzyme and mutant enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
pullulan
pH 4.5, 60°C, kcat/Km of wild-type enzyme and mutant enzyme
additional information
pullulan
-
pH 4.5, 60°C, kcat/Km of wild-type enzyme and mutant enzyme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1178.5
Ax203843.1
substrate: pullulan, pH 5.0, 60°C, mutant enzyme L627R
1352 - 1790
16.5 - 29.8
192.56
Km-value: 22.4 mg/ml, 70 °C, pH 6.5, recombinant wild-type enzyme
984.2
Ax203843.1
substrate: pullulan, pH 5.0, 60°C, wild-type enzyme
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
5 - 6
5.5
5.6
6.5
5
Fontibacillus sp. DSHK 107
-
immobilized pullulanases on Florisil and nano-silica through glutaraldehyde spacer arm
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 5
pH 2.0: about 60% of maximal activity, pH 5.0: about 60% of maximal activity, , amylolytic activity toward starch
4 - 7.5
4.3 - 7.2
pH 4.3: about 80% of maximal activity, pH 7.2: about 75% of maximal activity
4.5 - 6.5
-
over 89% of maximal activity between pH 5.0 and pH 6.5, over 75% at pH 4.5
4.5 - 7.8
5 - 7
5 - 8
5 - 8.5
pH 5.0: about 65% of maximal activity, pH 8.5: about 65% of maximal activity
5 - 9
pH 5.0: about 80% of maximal activity, pH 9.0: about 35% of maximal activity, wild-type enzyme
5.5 - 8.5
Halorubrum sp. Ha25
-
pH 5.5: about 45% of maximal activity, pH 8.5: about 45% of maximal activity
6 - 9
pH 6.0: about 45% of maximal activity, pH 9.0: about 25% of maximal activity
5 - 8
-
pH 5.0: about 30% of maximal activity, pH 8.0: about 30% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
115
35
Fontibacillus sp. DSHK 107
-
soluble enzyme and immobilized pullulanases on Florisil and nano-silica through glutaraldehyde spacer arm
40
45
50
55
60
60 - 65
65
70
80
85
90
95
95
temperature optimum for both amylase and pullulanase activities
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100 - 135
-
100°C: about 40% of maximal activity, 135°C: about 60% of maximal activity, substrate: starch, 5 mM Ca2+
30 - 70
-
30°C: about 60% of maximal activity, 70°C: about 40% of maximal activity
40 - 55
40 - 60
40°C: about 35% of maximal activity, 60°C: about 25% of maximal activity
40 - 65
Halorubrum sp. Ha25
-
40°C: about 45% of maximal activity, 65°C: about 55% of maximal activity
45 - 95
45°C: about 60% of maximal activity, 95°C: about 55% of maximal activity
50 - 60
50 - 80
50°C: about 60% of maximal activity, 80°C: about 30% of maximal activity, wild-type enzyme
60
60 - 110
60°C: about 60% of maximal activity, 110°C: about 90% of maximal activity
80 - 110
80°C: about 55% of maximal activity, 110°C: about 50% of maximal activity, amylolytic activity toward starch
80 - 115
80°C: about 40% of maximal activity, 115°C: about 50% of maximal activity, with or wothout 0.5 mM Ca2+
90 - 108
-
90°C: about 60% of maximal activity, 102-108: maximal activity
90 - 115
90 - 125
90 - 135
-
90°C: about 60% of maximal activity, 135°C: about 55% of maximal activity, substrate: pullulan, 5 mM Ca2+
95 - 125
-
100°C: about 65% of maximal activity, 135°C: about 80% of maximal activity, substrate: starch, 5 mM Ca2+
additional information
40 - 55
40°C: about 45% of maximal activity, 55°C: about 30% of maximal activity
90 - 115
-
90°C: about 60% of maximal activity, 125°C: about 70% of maximal activity, substrate: pullulan, no metal added
90 - 115
-
90°C: about 60% of maximal activity, 125°C: about 75% of maximal activity, substrate: starch, no metal added
90 - 125
-
90°C: about 50% of maximal activity, 125°C: about 50% of maximal activity, substrate: starch, no metal added
90 - 125
-
90°C: about 75% of maximal activity, 125°C: about 45% of maximal activity, substrate: pullulan, no metal added
90 - 125
-
90°C: about 50% of maximal activity, 135°C: about 50% of maximal activity, substrate: pullulan, 5 mM Ca2+
additional information
-
the presence of Ca2+ has a significant positive effect on enzyme activity at temperatures above 120°C, extending the range at which activity can be measured up to 130 to 140°C
additional information
-
the presence of Ca2+ has a significant positive effect on enzyme activity at temperatures above 120°C, extending the range at which activity can be measured up to 130 to 140°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme has seven isomeric forms to be distinguished by their isoelectric points
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
optimized growth conditions: medium with 1.5 g per l maltose and 8.3 g per l yeast extract
-
-
brenda
coding region of the OsPUL gene; ssp. indica cv. 9311, and ssp. japonica cv.Wuxiangjing 9, gene OsPUL
UniProt
brenda
single copy gene on rice chromosome 4; ssp. indica cv. 9311, and ssp. japonica cv.Wuxiangjing 9, gene OsPUL
UniProt
brenda
39E, bifunctional enzyme with activities of both alpha-amylase and pullulanase
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
PelBsp-PulA is efficiently secreted into the medium. At least three regions of PulA contain information that influence its secretion, depending on their context
brenda
additional information
-
recombinant enzyme expressed in Bacillus licheniformis
brenda
-
recombinant from expression in Bacillus licheniformis
brenda
-
pullulanase from germinating and nongerminating seed are the same protein
brenda
developing endosperm, expression of the OsPUL gene encoding a pullulanase-type debranching enzyme during seed development and germination in rice, the OsPUL promoter actively functions in the late stage of seed germination, overview
brenda
additional information
quantitative real-time PCR analysis of the expression pattern of the OsPUL gene in different tissues as well as in seeds at different developmental stages, overview
brenda
additional information
quantitative real-time PCR analysis of the expression pattern of the OsPUL gene in different tissues as well as in seeds at different developmental stages, overview
brenda
additional information
-
quantitative real-time PCR analysis of the expression pattern of the OsPUL gene in different tissues as well as in seeds at different developmental stages, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
remains cell surface anchored via its fatty acylated N terminus, the subcomplex of the pullulanase secreton is composed of PulM, PulE, PulC, PulD and PulL, green fluorescent protein tagged PulM and PulL reveals that secretion of pullulanase is distributed over the cell surface
-
brenda
-
enzyme exits as an cell-surface-bound intermediate prior release into the medium
-
brenda
-
enzyme exits as an cell-surface-bound intermediate prior release into the medium
-
-
brenda
the Klebsiella lipoprotein pullulanase (PulA) is exported to the periplasm, triacylated, and anchored via lipids in the inner membrane prior to its transport to the bacterial surface through a type II secretion system
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
additional information
Fontibacillus sp. DSHK 107
-
pullulanase partially purified from Fontibacillus sp. is covalently immobilized on Florisil and nano-silica through both glutaraldehyde and (3-glycidyloxypropyl)trimethoxysilane spacer arms. The pullulanase immobilized on Florisil and nano-silica through glutaraldehyde spacer arm show 85% and 190% activity of its free form, respectively, whereas no activity is observed when it is immobilized on the same supports through (3-glycidyloxypropyl)trimethoxysilane spacer arm
metabolism
-
the debranching enzyme pullulanase is involved in the carbohydrate metabolism of Bacillus subtilis
metabolism
-
the debranching enzyme pullulanase is involved in the carbohydrate metabolism of Bacillus subtilis
-
physiological function
-
role of pullulanase in glycogen utilization and the sequential process of glycogen breakdown, overview
physiological function
-
role of pullulanase in glycogen utilization and the sequential process of glycogen breakdown, overview
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
110000
112000
115000 - 116000
120000
218000 - 220000
-
gel filtration, gel electrophoresis, amino acid analysis
50000
x * 50000, recombinant enzyme after heat treatment in denaturing buffer at 70°C or below, SDS-PAGE
80000
90000
90000
x * 90000, recombinant enzyme after heat treatment in denaturing buffer at 100°C and 110°C, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
tetramer
trimer
additional information
?
x * 50000, recombinant enzyme after heat treatment in denaturing buffer at 70°C or below, SDS-PAGE
?
x * 90000, recombinant enzyme after heat treatment in denaturing buffer at 100°C and 110°C, SDS-PAGE
additional information
-
enzyme modular architecture and domain structure, it contains CBM48 and CBM41 domains, and X25 and X45 domains, overview
additional information
-
recombinant enzyme binds to human cervical epithelial cells
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
lipoprotein
proteolytic modification
proteolytic modification
sequence contains a 19-residue signal peptide
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
X-ray diffraction structure determination and analysis at 1.7 A resolution
-
hanging dop method, crystals belong to the orthorhombic space group P2(1)2(1)2(1) with unit-cell parameters a = 70.568, b = 127.68, c = 189.25 A. The crystal contains two molecules of pullulanase in the asymmetric unit, with a solvent content of 53.15%
-
hanging-drop vapor diffusion method. Characterization of the Ins subdomain by X-ray crystallography
hanging-drop vapour-diffusion method, crystal structure of pullulanase and its complex with glucose, maltose, isomaltose, maltotriose and maltotetraose, 1.7-1.9 A resolution
-
purified recombinant enzyme, mixing of 0.0012 ml of 14 mg/ml protein in 50 mM Na-phosphate buffer, pH 7.5, with 0.0012 ml reservoir solution containing 20% w/v PEG 8000, 200 mM Tris-HCl buffer, pH 8.5, and 100 mM MgCl2, X-ray diffraction structure determination and analysis at 2.37 A resolution, molecular structure modelling
-
N-terminal truncated form lacking the carbohydrate binding module, but containing the catalytic domain, in its apo form and in complex with maltotetraose, at resolutions of 2.1 and 2.4 A, respectively
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A90D
Anoxybacillus sp. WB42
mutant enzyme shows increase in thermostability as compared to wild-type enzyme, increase in kcat/Km for pullulan
A90G
Anoxybacillus sp. WB42
mutant enzyme shows increase in thermostability as compared to wild-type enzyme, increase in kcat/Km for pullulan
A90P
Anoxybacillus sp. WB42
mutant enzyme shows increase in thermostability as compared to wild-type enzyme, increase in kcat/Km for pullulan
A90S
Anoxybacillus sp. WB42
mutant enzyme shows increase in thermostability as compared to wild-type enzyme, increase in kcat/Km for pullulan
H5A
Anoxybacillus sp. WB42
mutant enzyme shows the same thermostability as wild-type enzyme. No activity with pullulan
H5A/R6A/T7A
Anoxybacillus sp. WB42
mutant enzyme shows increase in thermostability as compared to wild-type enzyme, decrease in kcat/Km for pullulan
L173D
Anoxybacillus sp. WB42
mutant enzyme shows increase in thermostability as compared to wild-type enzyme, increase in kcat/Km for pullulan
M88D
Anoxybacillus sp. WB42
mutant enzyme shows increase in thermostability as compared to wild-type enzyme. No activity with pullulan
Q87A
Anoxybacillus sp. WB42
mutant enzyme shows increase in thermostability as compared to wild-type enzyme, decrease in kcat/Km for pullulan
Q87A/L173D
Anoxybacillus sp. WB42
mutant enzyme shows increase in thermostability as compared to wild-type enzyme, decrease in kcat/Km for pullulan
Q87G
Anoxybacillus sp. WB42
mutant enzyme shows slight decrease in thermostability as compared to wild-type enzyme. No activity with pullulan
R6A
Anoxybacillus sp. WB42
mutant enzyme shows the same thermostability as wild-type enzyme. No activity with pullulan
R93A
Anoxybacillus sp. WB42
mutant enzyme shows slight decrease in thermostability as compared to wild-type enzyme, slight decrease in kcat/Km for pullulan
R93E
Anoxybacillus sp. WB42
mutant enzyme shows slight decrease in thermostability as compared to wild-type enzyme, decrease in kcat/Km for pullulan
R93K
Anoxybacillus sp. WB42
mutant enzyme shows slight increase in thermostability as compared to wild-type enzyme, decrease in kcat/Km for pullulan
R93T
Anoxybacillus sp. WB42
mutant enzyme shows slight increase in thermostability as compared to wild-type enzyme, slight decrease in kcat/Km for pullulan
T7A
Anoxybacillus sp. WB42
mutant enzyme shows the same thermostability as wild-type enzyme. No activity with pullulan
L627R
Ax203843.1
the pH optimum of the mutant enzyme shifts from 5.0 to 4.0, and its relative activity at pH 4.0 is 117% that of the wide-type enzyme. The L627R mutant exhibits increased tolerance against acid-mediated denaturation, and its maximum D-glucose content (97.4%) is obtained after 40 h incubation, which is shorter by 10 h compared with the time required by the wild-type enzyme to produce a comparable amount of the monosaccharide. The L627R mutant may be suitable for industrial application because its shortened reaction time translates to reduced energy consumption
D332H/D398Y
-
mutant enzyme shows remarkable improvement of thermal stability in higher temperature range (above 55 °C). The best temperature of the relative activity moves to 60°C. The activity performance in the middle temperature range (40 to 55°C) is worse than that of the wild type pullulanase
D332H/D398Y/V390N
-
the activity performance of mutations D332H/D398Y/V390N is better than that of mutations D332H/D398Y/V390S in all temperature range from 40°C to 65°C
D332H/D398Y/V390S
-
the activity performance of the mutant enzyme is better than the wild pullulanase-BDPulA in all temperature range from 40°C to 65°C. In the temperature range lower than 55°C the activity is worse than mutation V390S alone, and in the temperature range higher than 55°C the activity of the mutant enzyme is worse than the mutation D332H/D398Y, but better than the wild type enzyme and V390S-mutated BDPulA
D787C
D787F
higher enzymatic activity than that of wild-type enzyme
D787N
higher enzymatic activity than that of wild-type enzyme
N680D
mutation shows positive effects for the hydrolysis reaction of pullulanase
N680D/T477N
mutation improves thermal stability, pH-sensitivity, and catalysis activity of pullulanase
T477N
mutation shows positive effects for the hydrolysis reaction of pullulanase
N680D
-
mutation shows positive effects for the hydrolysis reaction of pullulanase
-
N680D/T477N
-
mutation improves thermal stability, pH-sensitivity, and catalysis activity of pullulanase
-
T477N
-
mutation shows positive effects for the hydrolysis reaction of pullulanase
-
D394N
-
kcat/KM is 24.2fold lower than wild-type value, specific activity on starch decreases 11.7times
E291Q
-
kcat/KM is 123fold lower than wild-type value, specific activity on starch decreases 91times
E396Q
-
activity of the mutant enzyme on pullulan is to low to allow reliable determination of catalytic efficiency, specific activity on starch decreases 37.2times
additional information
D787C
higher enzymatic activity than that of wild-type enzyme
D787C
the enzymatic activity and specific activity of D787C are 1.5fold higher than those of the wild-type. The enzyme shows a 1.8fold increase in kcat and a 1.7-fold increase in kcat/Km. It maintains higher activity compared with that of wild-type enzyme at temperatures over 60°C. Higher acid resistance than wild-type enzyme, maintaining 90% residual activity at pH 4.0
additional information
truncated form of enzyme, lacking first 252 amino acids, physicochemical properties almost identical to wild type enzyme
additional information
-
truncated form of enzyme, lacking first 252 amino acids, physicochemical properties almost identical to wild type enzyme
additional information
EPZ37738
amino acids 362-370 of Ask are replaced with the corresponding sequence of type I pullulanase Pul-LM14-2 from Anoxybacillus sp. LM14-2. Unlike wild-type, the mutant enzyme forms reducing sugars on digesting starch
additional information
-
amino acids 362-370 of Ask are replaced with the corresponding sequence of type I pullulanase Pul-LM14-2 from Anoxybacillus sp. LM14-2. Unlike wild-type, the mutant enzyme forms reducing sugars on digesting starch
-
additional information
-
construction of an amyX knockout strain and a glycogen overproducing glg strain with or without knockdown of amyX. The amyX glg strain accumulates significantly larger amounts of glycogen than the glg mutant, molecular masses of theglycogens, overview. Glycogen samples from the amyX glg strain exhibits average molecular masses two and three times larger, respectively, than that of glycogen from the glg mutant
additional information
-
construction of an amyX knockout strain and a glycogen overproducing glg strain with or without knockdown of amyX. The amyX glg strain accumulates significantly larger amounts of glycogen than the glg mutant, molecular masses of theglycogens, overview. Glycogen samples from the amyX glg strain exhibits average molecular masses two and three times larger, respectively, than that of glycogen from the glg mutant
-
additional information
different N-terminally domain truncated (730T) or spliced (730T-U1 and 730T-U2) mutants are constructed. Truncating the N-terminal 85 amino acids decreases the Km value and does not change its optimum pH. Wild-type enzyme can exhibit almost entirely soluble expression, but inclusion bodies are formed after truncating 85 amino acids from its N-terminus. This indicates that the N-terminal 85 amino acids of PulGT are responsible for ensuring secretory protein folding and maintaining its stability
additional information
-
different N-terminally domain truncated (730T) or spliced (730T-U1 and 730T-U2) mutants are constructed. Truncating the N-terminal 85 amino acids decreases the Km value and does not change its optimum pH. Wild-type enzyme can exhibit almost entirely soluble expression, but inclusion bodies are formed after truncating 85 amino acids from its N-terminus. This indicates that the N-terminal 85 amino acids of PulGT are responsible for ensuring secretory protein folding and maintaining its stability
additional information
Geobacillus thermocatenulatus DSMZ730
-
different N-terminally domain truncated (730T) or spliced (730T-U1 and 730T-U2) mutants are constructed. Truncating the N-terminal 85 amino acids decreases the Km value and does not change its optimum pH. Wild-type enzyme can exhibit almost entirely soluble expression, but inclusion bodies are formed after truncating 85 amino acids from its N-terminus. This indicates that the N-terminal 85 amino acids of PulGT are responsible for ensuring secretory protein folding and maintaining its stability
-
additional information
-
investigation of the function of pullulanase in starch biosynthesis using the mutant lines e10-/- and i16-/- containing the Tos17 insertion at exon 10 and intron 16 of the OsPUL gene, respectively, and EM1003, a product of N-methyl-N-nitrosourea mutagenesis, which mutated from C to T at 1266 bp before the start codon. Reduction of pullulanase activity has no effects on the other enzymes involved in starch biosynthesis. Short chains with a degree of polymerizytion below 14 are increased in the mutants compared with wild-type. The alpha-glucan composition and the structure of the starch components of the mutants is essentially the same, although the average chain length of the B2,3 chains of amylopectin in the mutants is about 3 residues longer than that of wild-type. Pullulanase fucntion may partially overlap with that of isoamylase 1
additional information
construction of GUS expressing transgenic rice lines by Agrobacterium tumefaciens transfection, overview
additional information
construction of GUS expressing transgenic rice lines by Agrobacterium tumefaciens transfection, overview
additional information
-
construction of GUS expressing transgenic rice lines by Agrobacterium tumefaciens transfection, overview
additional information
the active hydrogen bond network is applied for engineering of pullulanase and improvement of thermal stability and pH-sensitivity of the enzyme
additional information
-
the active hydrogen bond network is applied for engineering of pullulanase and improvement of thermal stability and pH-sensitivity of the enzyme
additional information
-
the active hydrogen bond network is applied for engineering of pullulanase and improvement of thermal stability and pH-sensitivity of the enzyme
-
additional information
parallel N- and C-terminal truncations facilitate purification. Catalytic properties of truncation construct Pul13A-N1/C1 are not impaired
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 11
5
4°C, 60 min, 75% residual activity, wild-type enzyme
750894
5 - 6.5
after incubation at 95°C for 4 h in a pH range from 5.0 to 6.5, the residual pullulanase and amylase activities of the enzyme are above 90% of the maximum activity
714788
5.5 - 10.5
30 min, enzyme retains more than 80% of its activity
752096
6.5 - 8.5
30 min, enzyme retains more than 85% of its original activity
750159
7
4°C, 60 min, 85% residual activity, wild-type enzyme
750894
8
4°C, 60 min, 70% residual activity, wild-type enzyme
750894
9
4°C, 60 min, 55% residual activity, wild-type enzyme
750894
6
4°C, 60 min, 90% residual activity, wild-type enzyme
750894
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
35
40
50
50 - 70
-
irreversible inactivation of free pullulanase, 92.51% and 82.52% of maximal activity at 55°C and 60°C, respectively, rapid decrease at 70°C
55
60
69
Anoxybacillus sp. WB42
T50, mutant enzyme Q87A, T50, mutant enzyme L173D, mutant enzyme Q87A/L173D
70
75
80
80 - 110
the pullulanase shows 96%, 91%, 70%, and 50% of the maximum activity at 80, 90, 100 and 110°C, respectively. The residual total activities of the amylopullulanase-MalE fusion protein and the hydrolytic domain of the amylopullulanase are both 89% after incubation at 100°C for 1 h
85
90
additional information
100
denaturating temperatures of above 100°C are required for complete unfolding. The enzyme remains active even after denaturation at 100 and 110°C,suggesting that unfolding isnot complete
35
Fontibacillus sp. DSHK 107
-
t1/2 of soluble enzyme: 8.9 min. Thermal stability of pullulanase immobilized on Florisil and nano-silica is enhanced 6.5- and 15.6fold
50
Fontibacillus sp. DSHK 107
-
t1/2 of soluble enzyme: 6.2 min. Thermal stability of pullulanase immobilized on Florisil and nano-silica is enhanced 6.6- and 16.0fold
55
-
120 min, no residual activity of free enzyme, 50% residual activity of enzyme immobilized on calcium alginate beads
60
3 h, about 45% loss of activity. 1 h, about 20% loss of activity, wild-type enzyme
70
3 h, about 75% loss of activity. 1 h, about 20% loss of activity, wild-type enzyme
70
the recombinant enzyme remains folded after denaturation at temperatures of below 70°C
70
1 h, residual activity is more than 90%. More than 70% of the activity is retained after 1 h at pH 6-8 with the absence of the substrate
90
half-life: 11 h for EDTA-treated enzyme, 44 h in presence of 5 mM Ca2+
additional information
-
thermostability of the enzyme is enhanced in the presence of 5 mM Ca2+
additional information
-
thermostability of the enzyme is enhanced in the presence of 5 mM Ca2+
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the pullulanases immobilized on Florisil and nano-silica protected 71% and 90% of their initial activities after 10 reuses
Fontibacillus sp. DSHK 107
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acetone
Halorubrum sp. Ha25
-
20%, half-life of pullulytic activity: 155 h, half-life of amylolytic activity: 255 h
chloroform
Halorubrum sp. Ha25
-
20%, half-life of pullulytic activity: 150 h, half-life of amylolytic activity: 230 h
dimethyl sulfoxide
Halorubrum sp. Ha25
-
20%, half-life of pullulytic activity: 46 h, half-life of amylolytic activity: 41 h
DMSO
Ethanol
N,N-dimethylformamide
Halorubrum sp. Ha25
-
20%, half-life of pullulytic activity: 65 h, half-life of amylolytic activity: 101 h
n-Butanol
Halorubrum sp. Ha25
-
20%, half-life of pullulytic activity: 125 h, half-life of amylolytic activity: 215 h
propanol
Halorubrum sp. Ha25
-
20%, half-life of pullulytic activity: 33 h, half-life of amylolytic activity: 53 h
additional information
Halorubrum sp. Ha25
-
the enzyme is more stable in the presence of non-polar organic solvents than polar solvents (20%)
Ethanol
Halorubrum sp. Ha25
-
20%, half-life of pullulytic activity: 57 h, half-life of amylolytic activity: 99 h
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, anion exchange and gel filtration chromatography
-
ammonium sulfate precipitation, DEAE-52 column chromatography, TSK G2000 SWXL column chromatography, and Sephadex G-100 gel filtration
BD TALON spin column chromatography, gel filtration
of the recombinant protein
of the recombinant protein using heat treatment, size exclusion, and anion-exchange chromatography
-
parallel N- and C-terminal truncations facilitate purification
recombinant His-tagged NPDE from Escherichia coli strain MC1061 by nickel affinity chromatography to homogeneity and over 96% purity
-
recombinant protein expressed in Escherichia coli
to homogeneity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Rosetta (DE3) pLysS cells
expressed in Escherichia coli using pHsh and pET28a vectors. The pHsh expression system produces a 3.6fold higher recombinant pullulanase than pET28a
expression in Bacillus subtilis
expression in Escherichia coli
expression in Escherichia coli BL21(DE3)
expression in Escherichia coli, connection to the lipase A signal peptide of Bacillus subtilis strain leads to an efficient secretion of an active form enzyme on the periplasmic fraction, fusion to the amylase signal sequence of the Bacillus stearothermophilus US100 strain leads to an efficient secretion of this natively cytoplasmic enzyme as an active form in the supernatant
-
expression of wild-type and mutant enzymes in Escherichia coli BL21 (DE3) cells
heterologously expressed in Escherichia coli
heterologously expressed in Escherichia coli as an intracellular soluble protein
quantitative real-time PCR analysis of the expression pattern of the OsPUL gene from Oryza sativa ssp. indica cv. 9311 encoding a pullulanase-type debranching enzyme in different tissues as well as in seeds at different developmental stages, the OsPUL promoter actively functions in the late stage of seed germination, overview. Transcriptional profiling and regulatory elements of endogenous OsPUL gene in rice
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
magnesium ion addition represses transcription of cell wall protein (HWP). Because the pullulanase gene and HWP have identical promoters, pullulanase gene transcription is also inhibited. When cultured in medium without added magnesium ions, Brevibacillus choshinensis mainly produced a thermolabile, inactive form of pullulanase. The addition of magnesium ions leads to the production of a thermostable, active form of pullulanase. When pullulanase is expressed slowly, it tends to fold into an active form
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
use of enzyme entrapped in calcium alginate beads for hydrolysis of starch
degradation
-
pullulanase is useful in the fermentation of high-gravity maize, together with other proteolytic and polysaccharide-degrading enzyme. Adding pullulanase resultes in the acceleration of the starch hydrolysis degree, which leads to lower amounts of unhydrolyzed dextrins and higher ethanol yield
food industry
industry
synthesis
industry
additional information
-
resistant starch in food is beneficial for human health, a commercial preparation of pullulanase is used to debranch amylopectin of sago starch at subgelatinization temperature and to evaluate the formation of resistant starch
food industry
-
debranching of guar galactomannan by pullulanase as an alternative and inexpensive route to produce modified guar galactomannan with enhanced functional properties
food industry
-
maltotriose syrup preparation from pullulan using pullulanase, overview. In a batch system, pullulanase hydrolyzes 94.25% of purified pullulan and the resultant syrup contains 3.8 mg/ml of maltotriose
food industry
Ax203843.1
break down of starch for the production of high-glucose syrup. The L627R mutant enzyme may be suitable for industrial application because its shortened reaction time translates to reduced energy consumption
food industry
the enzyme can be used directly for maize starch saccharification without adjusting the pH, which reduces cost and improves efficiency
food industry
useful in starch industries. The addition of the enzyme in gelatinized rice and maize starches significantly increases the resistant starch type 3 yields (RS3). RS3 is of great importance for nutritionists and food industry, due to its reduced levels of plasma glucose and insulin, increased faecal bulk, and short-chain fatty acid production through fermentation in the large intestine
food industry
Geobacillus thermocatenulatus DSMZ730
-
the enzyme can be used directly for maize starch saccharification without adjusting the pH, which reduces cost and improves efficiency
-
industry
-
in starch processing industry for the production of sugar syrups, a very effective medium for remarkably improved pullulanase production is designed, a new mutant Bacillus cereus FDTA 13/NTG04-B4 with 2fold increase in pullulanase activity
industry
-
in the starch processing industry for the production of sugar syrups
industry
the acidic thermoactive amylopullulanase-MalE fusion protein and the hydrolytic domain of the amylopullulanase can be employed for industrial saccharification of starch
industry
the enzyme can be employed for industrial saccharification of starch
industry
truncation construct with parallel N- and C-terminal truncations facilitate purification and analysis. Thus the truncation construct may be superior for industrial applications over the full-length pullulanase
industry
-
in the starch processing industry for the production of sugar syrups
-
industry
-
the acidic thermoactive amylopullulanase-MalE fusion protein and the hydrolytic domain of the amylopullulanase can be employed for industrial saccharification of starch
-
industry
-
in starch processing industry for the production of sugar syrups, a very effective medium for remarkably improved pullulanase production is designed, a new mutant Bacillus cereus FDTA 13/NTG04-B4 with 2fold increase in pullulanase activity
-
synthesis
-
use of enzyme for synthesis of novel heterobranche beta-cyclodextrins
synthesis
-
preparation of maltotriose by hydrolyzing of pullulan with pullulanase, optimum conditions are: time 6 h, pH 5.0, temperature 45°C, amount of pullulanase 10 ASPU/g, concentration of pullulan 3% w/v, method, overview
synthesis
recombinant expression of PulB in Bacillus subtilis is increased by stronger constitutive promoter P43 and use of strain WB600 instread of WB800. Extracellular pullulanase activity reaches up to 24.5 U/ml
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Release 2023.1 (January 2023)
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