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Information on EC 3.2.1.41 - pullulanase
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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
- glucoamylase
-
amylolytic
-
lariat
- beta-amylase
- oxytoca
- cyclodextrins
-
alpha-1,6
-
waxy
- maltodextrins
- maltotetraose
-
saccharification
-
aerobacter
-
dextrinase
- amyloglucosidase
- phytoglycogen
-
glucanotransferase
- aureobasidium
- beta-cyclodextrins
-
thermoanaerobacterium
- maltohexaose
- alpha-glucans
-
starch-based
- food industry
- anoxybacillus
-
starch-degrading
- degradation
- thermoleovorans
- synthesis
-
branchpoints
- industry
- pilins
- malto-oligosaccharides
- biotechnology
- amylo-1,6-glucosidase
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
1,4-alpha-D-glucan glucanohydrolase, Alpha-dextrin endo-1,6-alpha-glucosidase, amylase-pullulanase, amylopectin 6-glucanohydrolase, amylopullulanase, AmyX, Apu, ApuK885, ApuM957, Ask, 
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
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in pullulan, amylopectin and glycogen, and in the alpha- and beta-limit dextrins of amylopectin and glycogen
-
-
-
-
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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
-
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
-
-
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
-
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
-
-
?
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
-
-
?
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 (0â4.5 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
0.664
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
amylose
Km-value: 0.71 mg/ml, pH 3.5, 95°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