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3 glycogen + H2O
4 maltotriose
4-nitrophenyl alpha-D-maltoheptaoside + H2O
4-nitrophenol + alpha-D-maltoheptaose
4-nitrophenyl alpha-D-maltotrioside + H2O
4-nitrophenol + alpha-D-maltotriose
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
6-O-alpha-maltosyl cyclodextrin + H2O
glucose + cyclodextrin
6-O-alpha-maltotriosyl cyclomaltoheptaose + H2O
glucose + cyclodextrin
6-O-alpha-maltotriosyl cyclomaltohexaose + H2O
glucose + cyclodextrin
alpha-cyclodextrin + H2O
?
-
-
-
?
amylopectin + H2O
D-glucose + maltose + maltotriose
amylopectin + H2O
malto-2-4-oligosaccharide + ?
-
-
-
-
?
amylopectin + H2O
maltohexaose + maltopentaose + maltotetraose + maltotriose + maltose + D-glucose
amylopectin + H2O
maltooligosaccharides + maltose
amylopectin + H2O
maltotriose
-
-
-
?
amylopectin + H2O
maltotriose + maltose + ?
amylopectin + H2O
maltotriose + maltose + maltooligosaccharides
amylopectin + H2O
maltotriose + maltotetraose + maltopentaose + maltohexaose
amylopectin beta-limit dextrin + H2O
maltotriose + maltose
amylose + H2O
malto-2-4-oligosaccharide + ?
-
-
-
-
?
amylose + H2O
maltooligosaccharides + maltose
amylose + H2O
maltose + maltotriose
amylose + H2O
maltotriose + maltose
beta-cyclodextrin + H2O
?
beta-limit dextrin + H2O
?
beta-limited dextrin + H2O
maltotriose + maltose + maltooligosaccharides
cyclomaltooctaose + H2O
6,6-di-O-alpha-maltosyl-cG8
-
gamma-cyclodextrin
-
-
?
dextran + H2O
?
-
-
-
-
?
dextrin + H2O
maltooligosaccharides + maltose
gamma-cyclodextrin + H2O
?
glycogen + H2O
malto-2-4-oligosaccharide + ?
-
-
-
-
?
glycogen + H2O
maltooligosaccharides + maltose
glycogen + H2O
maltotriose + maltose
-
-
-
?
glycogen + H2O
maltotriose + maltose + maltooligosaccharides
glycogen beta-limit dextrin + H2O
maltotriose + maltose + maltosetetraose
guar galactomannan + H2O
?
-
-
-
-
?
maltoheptaose + H2O
maltotriose + maltose + D-glucose
maltohexaose + H2O
maltotriose + maltose + D-glucose + maltotetraose
maltopentaose + H2O
maltotriose + maltose
maltose + cG8
6-O-alpha-maltosyl-cG8
-
through the reversed action
-
-
r
maltotetraose + H2O
maltose + glucose + maltotriose
phytoglycogen + H2O
?
9% of activity compared to pullulan
-
-
?
potato starch + H2O
?
14% of the activity with pullulan
-
-
?
pullulan + H2O
malto-2-4-oligosaccharide + ?
-
best substrate
-
-
?
pullulan + H2O
maltotriose + ?
pullulan + H2O
maltotriose + maltose
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
-
-
?
rice flour + H2O
?
15% of the activity with pullulan
-
-
?
soluble starch
maltotriose + maltose
soluble starch + H2O
malto-2-4-oligosaccharide + ?
-
-
-
-
?
soluble starch + H2O
maltotriose + maltose
soluble starch + H2O
maltotriose + maltose + maltooligosaccharides
12.8% of the activity with pullulan
-
-
?
starch + H2O
D-glucose + maltose + maltotriose
starch + H2O
maltohexaose + maltopentaose + maltotetraose + maltotriose + maltose + D-glucose
starch + H2O
maltose + maltotriose
starch + H2O
maltotriose + ?
starch + H2O
maltotriose + oligosaccharides
metroxylon sagu + H2O
debranched starch
3 glycogen + H2O
4 maltotriose
-
-
-
?
3 glycogen + H2O
4 maltotriose
-
-
-
-
?
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
?
the enzyme specifically attacks alpha-1,6-linkages of branched oligosaccharides
-
-
?
amylopectin + H2O
?
12% of the activity compared to pullulan
-
-
?
amylopectin + H2O
?
-
-
-
?
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
?
-
-
-
?
amylopectin + H2O
?
-
hydrolyzed at 60% compared to pullulan
-
-
?
amylopectin + H2O
?
20% of activity compared to pullulan
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
-
34.1% of the rate with pullulan
-
?
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
-
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
-
branched polysaccharides
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
Thermoanaerobium sp.
-
-
-
-
?
amylopectin + H2O
maltooligosaccharides + maltose
Thermoanaerobium sp.
-
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
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
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 beta-limit dextrin + H2O
maltotriose + maltose
-
-
-
-
?
amylopectin beta-limit dextrin + H2O
maltotriose + maltose
-
-
-
-
?
amylose + H2O
?
-
-
-
?
amylose + H2O
?
77% of activity compared to pullulan
-
-
?
amylose + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylose + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylose + H2O
maltooligosaccharides + maltose
-
weakly
-
-
?
amylose + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylose + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylose + H2O
maltooligosaccharides + maltose
-
-
-
-
?
amylose + H2O
maltooligosaccharides + maltose
Thermoanaerobium sp.
-
-
-
-
?
amylose + H2O
maltose + maltotriose
-
-
-
-
?
amylose + H2O
maltose + maltotriose
-
-
-
-
?
amylose + H2O
maltotriose + 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-limit dextrin + H2O
?
-
-
19.5% of the rate with pullulan
-
?
beta-limit dextrin + H2O
?
-
-
-
?
beta-limit dextrin + H2O
?
135% of activity compared to pullulan
-
-
?
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
-
-
?
dextrin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
dextrin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
dextrin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
dextrin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
dextrin + H2O
maltooligosaccharides + maltose
-
-
-
-
?
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
?
-
-
-
?
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
?
-
hydrolyzed at 30% compared to pullulan
-
-
?
glycogen + H2O
maltooligosaccharides + maltose
-
-
-
-
?
glycogen + H2O
maltooligosaccharides + maltose
-
-
-
-
?
glycogen + H2O
maltooligosaccharides + maltose
-
-
-
-
?
glycogen + H2O
maltooligosaccharides + maltose
-
-
-
-
?
glycogen + H2O
maltooligosaccharides + maltose
-
-
-
-
?
glycogen + H2O
maltooligosaccharides + maltose
-
-
-
-
?
glycogen + H2O
maltooligosaccharides + maltose
-
-
6.3% of the rate with pullulan
-
?
glycogen + H2O
maltooligosaccharides + maltose
-
-
-
-
?
glycogen + H2O
maltooligosaccharides + maltose
-
-
-
-
?
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
-
-
-
-
?
maltopentaose + H2O
maltotriose + maltose
-
-
-
-
?
maltopentaose + H2O
maltotriose + maltose
-
-
-
-
?
maltopentaose + H2O
maltotriose + maltose
-
-
-
-
?
maltotetraose + H2O
maltose + glucose + maltotriose
-
-
-
-
?
maltotetraose + H2O
maltose + glucose + maltotriose
-
-
-
-
?
maltotetraose + H2O
maltose + glucose + maltotriose
-
-
-
-
?
maltotetraose + H2O
maltose + glucose + maltotriose
Thermoanaerobium sp.
-
slowly
-
-
?
pullulan + H2O
?
-
-
-
?
pullulan + H2O
?
-
-
-
-
?
pullulan + H2O
?
Ax203843.1
-
-
-
?
pullulan + H2O
?
-
substrate from Aureobasidium pullulans strain FB-1
-
-
?
pullulan + H2O
?
-
-
-
-
?
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
?
-
-
-
-
?
pullulan + H2O
?
-
-
-
-
?
pullulan + H2O
?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
final product
-
?
pullulan + H2O
maltotriose + ?
EPZ37738
soluble enzyme is highly reactive towards pullulan but was unable to degrade short branches in starch
-
-
?
pullulan + H2O
maltotriose + ?
EPZ37738
soluble enzyme is highly reactive towards pullulan but was unable to degrade short branches in starch
-
-
?
pullulan + H2O
maltotriose + ?
EPZ37738
-
-
-
?
pullulan + H2O
maltotriose + ?
EPZ37738
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
preparation of maltotriose by hydrolyzing of pullulan with pullulanase, overview
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
complete conversion to maltotriose
-
?
pullulan + H2O
maltotriose + ?
-
complete conversion to maltotriose
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
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 + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
preferred substrate
-
-
?
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 + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
the enzyme hydrolyzes pullulan to yield mainly maltotriose, more than 95%
-
-
?
pullulan + H2O
maltotriose + ?
the enzyme hydrolyzes pullulan to yield mainly maltotriose, more than 95%
-
-
?
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 + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
Thermoanaerobium sp.
-
-
-
-
?
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 + ?
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
-
?
pullulan + H2O
maltotriose + ?
-
-
-
?
pullulan + H2O
maltotriose + maltose
-
-
-
-
?
pullulan + H2O
maltotriose + maltose
-
-
-
-
?
pullulan + H2O
maltotriose + maltose
-
-
-
-
?
pullulan + H2O
maltotriose + maltose
-
-
-
-
?
pullulan + H2O
maltotriose + maltose
-
-
-
-
?
pullulan + H2O
maltotriose + maltose
-
-
-
-
?
pullulan + H2O
maltotriose + maltose
-
-
-
?
pullulan + H2O
maltotriose + maltose
-
-
-
?
soluble starch
maltotriose + maltose
-
-
-
-
?
soluble starch
maltotriose + maltose
-
-
-
-
?
soluble starch
maltotriose + maltose
-
-
-
-
?
soluble starch
maltotriose + maltose
-
-
-
-
?
soluble starch
maltotriose + maltose
-
-
-
-
?
soluble starch
maltotriose + maltose
-
-
-
-
?
soluble starch
maltotriose + maltose
-
-
-
-
?
soluble starch
maltotriose + maltose
-
-
-
-
?
soluble starch
maltotriose + maltose
-
-
15.8% of the rate with pullulan
-
?
soluble starch
maltotriose + maltose
-
-
-
-
?
soluble starch
maltotriose + maltose
-
-
-
-
?
soluble starch
maltotriose + maltose
Thermoanaerobium sp.
-
-
-
-
?
soluble starch
maltotriose + maltose
-
-
-
-
?
soluble starch + H2O
?
-
-
-
-
?
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
?
the enzyme specifically attacks alpha-1,6-linkages of branched oligosaccharides
-
-
?
soluble starch + H2O
?
-
-
-
-
?
soluble starch + H2O
?
-
hydrolyzed at 80% compared to pullulan
-
-
?
soluble starch + H2O
maltotriose + maltose
-
-
-
-
?
soluble starch + H2O
maltotriose + maltose
-
-
-
?
soluble starch + H2O
maltotriose + maltose
-
-
-
?
starch + H2O
?
-
together with amylase, both enzymes immobilized on calcium alginate beads
-
-
?
starch + H2O
?
62% of activity compared to pullulan
-
-
?
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
maltose + maltotriose
-
-
-
-
?
starch + H2O
maltose + maltotriose
-
-
-
-
?
starch + H2O
maltotriose + ?
-
-
-
?
starch + H2O
maltotriose + ?
-
-
-
-
?
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
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
-
-
?
metroxylon sagu + H2O
debranched starch
additional information
-
native sago starch
-
-
?
additional information
?
-
no substrate: amylose
-
-
?
additional information
?
-
-
no substrate: amylose
-
-
?
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
?
-
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
?
-
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
-
-
?
additional information
?
-
no substrate: phytogen
-
-
?
pullulan + H2O
maltotriose + maltose
additional information
-
-
-
-
?
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2-mercaptoethanol
5 mM, 51% residual activity
ammonium sulfate
0.5 mM, 36% residual activity
CaCl2
1 mM, 1.8fold activation. 5 mM, 66% loss of activity. 10 mM, 97% loss of activity
CoCl2
1 mM, 97% inhibition
EGTA
-
1-10 mM, 65-70% inhibition
gamma-cyclodextrin
-
10 mM, 20% loss of activity
iodoacetate
-
1 M, 10% loss of activity
NH4+
EPZ37738
2 mM, 49% of initial activtiy
phenylmethylsulfonyl fluoride
-
partially
pullulan
-
substrate inhibition above 0.1%
sodium dodecylsulfate
1 mM, no residual activity
Sodium fluoride
-
1 M, 10% loss of activity
ZnCl2
5 mM, 51% residual activity
ZnSO4
1 mM, complete inhibition
1,10-phenanthroline
-
-
Ag+
-
-
Ag+
1 mM, 84% loss of activity
Ag+
-
0.1 M, 50% loss of activity
alpha-cyclodextrin
-
10 mM, 10% loss of activity
alpha-cyclodextrin
1%, 99% inhibition
alpha-cyclodextrin
-
1-10 mM, about 85% inhibition
Ba2+
EPZ37738
2 mM, 54% of initial activtiy
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
beta-cyclodextrin
-
1-10 mM, 80-85% inhibition
Ca2+
-
-
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
Co2+
EPZ37738
2 mM, 15% of initial activtiy
Co2+
-
5 mM, at least 60% inhibition
Co2+
1 mM, 18% residual activity
Cr3+
-
-
Cr3+
5 mM, 34% inhibition, pH 6.5, 70°C
Cu2+
EPZ37738
2 mM, 8% of initial activtiy
Cu2+
5 mM, 67% residual activity
Cu2+
2 mM, 79% residual activity
Cu2+
-
5 mM, at least 60% inhibition
Cu2+
1 mM, 82% loss of activity
Cu2+
1 mM, complete inactivation
Cu2+
5 mM, complete inhibition, pH 6.5, 70°C
CuCl2
5 mM, no residual activity
CuCl2
1 mM, complete inhibition
cyclodextrin
-
-
Cyclodextrins
-
-
-
Cyclodextrins
-
Schardinger dextrins
-
EDTA
EPZ37738
2 mM, 68% of initial activtiy
EDTA
5 mM, 63% residual activity
EDTA
5 mM, 72% residual activity
EDTA
5 mM, complete inhibition
EDTA
-
1-10 mM, about 70% inhibition
Fe2+
EPZ37738
2 mM, 6% of initial activtiy
Fe3+
-
-
Guanidine HCl
-
unfolding of the enzyme
Guanidine HCl
2.0 mM, about 55% inhibition
Guanidine HCl
-
at 0.25 M
Hg2+
-
-
Hg2+
-
complete inactivation
Hg2+
-
5 mM, at least 60% inhibition
Hg2+
1 mM, 99% loss of activity
Hg2+
1 mM, complete inactivation
Hg2+
5 mM, complete inhibition, pH 6.5, 70°C
Hg2+
-
0.1 M, 70% loss of activity
iodoacetamide
-
-
Mg2+
5 mM, 90% residual activity
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
Mn2+
EPZ37738
2 mM, 40% of initial activtiy
Mn2+
1 mM, 15% residual activity
N-bromosuccinimide
-
inhibitory at 10mM
N-bromosuccinimide
0.01%, no residual activity
N-bromosuccinimide
-
at 5 mM
N-bromosuccinimide
complete inactivation
Ni2+
EPZ37738
2 mM, 47% of initial activtiy
Ni2+
1 mM, 18% residual activity
Ni2+
5 mM, 31% inhibition, pH 6.5, 70°C
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
Pb2+
-
-
Pb2+
5 mM, 75% inhibition, pH 6.5, 70°C
SDS
5 mM, 46% residual activity
SDS
5-50 mM, 25-85% inhibition
SDS
1%, complete inactivation
SDS
10 mM, 96% inhibition, pH 6.5, 70°C
Sn2+
-
-
Sn2+
1 mM, 87% loss of activity
Sodium dodecyl sulfate
-
-
Sodium dodecyl sulfate
-
-
Sodium dodecyl sulfate
-
-
Sodium dodecyl sulfate
-
-
Sodium dodecyl sulfate
-
-
Sr2+
EPZ37738
2 mM, 73% of initial activtiy
Triton X-100
EPZ37738
1% v/v, 72% of initial activtiy
Urea
EPZ37738
2 mM, 57% of initial activtiy
Urea
4 M, 81% residual activity
Urea
2 M, complete inhibition
Zn2+
EPZ37738
2 mM, 22% of initial activtiy
Zn2+
2 mM, 48% residual activity
Zn2+
-
5 mM, at least 60% inhibition
Zn2+
1 mM, 53% residual activity
Zn2+
5 mM, 58% inhibition, pH 6.5, 70°C
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
-
additional information
-
EDTA has no effect
-
additional information
not inhibitory: EDTA
-
additional information
-
not inhibitory: EDTA
-
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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
Leukocyte debranching enzyme in glycogen storage disease.
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
[Genetic heterogeneity and the diagnosis of hepatic glycogenoses]
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
Diet therapy in severe clinical expression of debrancher deficiency.
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
The molecular background of glycogen metabolism disorders.
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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0.037 - 0.664
4-nitrophenyl alpha-D-maltotrioside
0.25
alpha-cyclodextrin
pH 3.5, 95°C
5.16
beta-cyclodextrin
pH 3.5, 95°C
4.1
beta-limit dextrin
pH 6.0, 37°C
0.71
gamma-cyclodextrin
pH 3.5, 95°C
additional information
amylopectin
0.037
4-nitrophenyl alpha-D-maltotrioside
-
pH 5.6, 98°C, 5 mM Ca2+
0.067
4-nitrophenyl alpha-D-maltotrioside
-
pH 5.6, 98°C, no metal added
0.077
4-nitrophenyl alpha-D-maltotrioside
-
pH 5.6, 98°C, 5 mM Ca2+
0.664
4-nitrophenyl alpha-D-maltotrioside
-
pH 5.6, 98°C, no metal added
0.021 - 0.078
pullulan
-
glucose equivalents
0.27
pullulan
-
pH 6, 40°C
0.37
pullulan
pH 6.0, 37°C
2.5
pullulan
-
glucose equivalents
additional information
amylopectin
Km-value: 3.95 mg/ml, pH 3.5, 95°C
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
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
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
pH 6.5, 70°C
additional information
pullulan
-
pH 6.5, 70°C
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: 4 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: 0.0031 mg/ml
additional information
pullulan
Km-value: 0.08 mg/ml, pH 3.5, 95°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
Km-value: 16.5 mg/ml, pH 5.5, 60°C, mutant enzyme H5A/R6A/T7A
additional information
pullulan
Km-value: 20.1 mg/ml, pH 5.5, 60°C, mutant enzyme R93T
additional information
pullulan
Km-value: 22.3 mg/ml, pH 5.5, 60°C, mutant enzyme R93A
additional information
pullulan
Km-value: 22.5 mg/ml, pH 5.5, 60°C, wild-type enzyme
additional information
pullulan
Km-value: 24.4 mg/ml, pH 5.5, 60°C, mutant enzyme A90G
additional information
pullulan
Km-value: 24.6 mg/ml, pH 5.5, 60°C, mutant enzyme A90D
additional information
pullulan
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
-
Km-value: 3.3 mg/ml, pH 6.5, 55°C
additional information
pullulan
Km-value: 31.2 mg/ml, pH 5.5, 60°C, mutant enzyme Q87A/L173D
additional information
pullulan
Km-value: 4.7 mg/ml, pH 5.5, 60°C, mutant enzyme R93K
additional information
pullulan
Km-value: 45.0 mg/ml, pH 5.5, 60°C, mutant enzyme A90S
additional information
pullulan
Km-value: 5.6 mg/ml, pH 5.5, 60°C, mutant enzyme R93E
additional information
pullulan
Km-value: 5.8 mg/ml, pH 5.5, 60°C, mutant enzyme L173D
additional information
pullulan
Km-value: 6.0 mg/ml, pH 5.5, 60°C, mutant enzyme DELTA(N)
additional information
pullulan
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
-
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: 1.8 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
-
additional information
starch
Km-value: 7.29 mg/ml, pH 3.5, 95°C
additional information
starch
-
Km-value: 7.29 mg/ml, pH 3.5, 95°C
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A90D
mutant enzyme shows increase in thermostability as compared to wild-type enzyme, increase in kcat/Km for pullulan
A90G
mutant enzyme shows increase in thermostability as compared to wild-type enzyme, increase in kcat/Km for pullulan
A90P
mutant enzyme shows increase in thermostability as compared to wild-type enzyme, increase in kcat/Km for pullulan
A90S
mutant enzyme shows increase in thermostability as compared to wild-type enzyme, increase in kcat/Km for pullulan
H5A
mutant enzyme shows the same thermostability as wild-type enzyme. No activity with pullulan
H5A/R6A/T7A
mutant enzyme shows increase in thermostability as compared to wild-type enzyme, decrease in kcat/Km for pullulan
L173D
mutant enzyme shows increase in thermostability as compared to wild-type enzyme, increase in kcat/Km for pullulan
M88D
mutant enzyme shows increase in thermostability as compared to wild-type enzyme. No activity with pullulan
Q87A
mutant enzyme shows increase in thermostability as compared to wild-type enzyme, decrease in kcat/Km for pullulan
Q87A/L173D
mutant enzyme shows increase in thermostability as compared to wild-type enzyme, decrease in kcat/Km for pullulan
Q87G
mutant enzyme shows slight decrease in thermostability as compared to wild-type enzyme. No activity with pullulan
R6A
mutant enzyme shows the same thermostability as wild-type enzyme. No activity with pullulan
R93A
mutant enzyme shows slight decrease in thermostability as compared to wild-type enzyme, slight decrease in kcat/Km for pullulan
R93E
mutant enzyme shows slight decrease in thermostability as compared to wild-type enzyme, decrease in kcat/Km for pullulan
R93K
mutant enzyme shows slight increase in thermostability as compared to wild-type enzyme, decrease in kcat/Km for pullulan
R93T
mutant enzyme shows slight increase in thermostability as compared to wild-type enzyme, slight decrease in kcat/Km for pullulan
T7A
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
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
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
-
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
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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
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construction of GUS expressing transgenic rice lines by Agrobacterium tumefaciens transfection, overview
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construction of GUS expressing transgenic rice lines by Agrobacterium tumefaciens transfection, overview
additional information
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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
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the active hydrogen bond network is applied for engineering of pullulanase and improvement of thermal stability and pH-sensitivity of the enzyme
additional information
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the active hydrogen bond network is applied for engineering of pullulanase and improvement of thermal stability and pH-sensitivity of the enzyme
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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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null mutation of enzyme, plants are impaired in transient and storage starch degradation, developing mutant endosperm accumulates branched maltooligosaccharides not found in wild type and is deficient in linear maltooligosaccharides
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