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alpha-D-glucan + H2O
?
-
cleavage of alpha-D-glucosidic linkages of certain branched alpha-D-glucans
-
-
?
alpha-limit dextrin + H2O
linear maltooligosaccharides
amylomaize + H2O
?
-
debranching
-
-
?
amylopectin + H2O
amylose + linear maltooligosaccharides
amylopectin + H2O
linear maltooligosaccharides
amylopectin + H2O
maltose + maltooligosaccharides
amylopectin phi-dextrin + H2O
maltotetraose
-
substrate on which all 3 types of debranching enzymes act
-
?
amylose + H2O
?
-
short chain
-
-
?
amylose-extender amylopectin + H2O
maltose + maltooligosaccharides
O80403
-
-
-
?
Arabidopsis starch + H2O
?
beta limit dextrin + H2O
linear maltooligosaccharides
-
-
-
?
beta limit dextrin + H2O
maltose + maltooligosaccharides
O80403
from maize
-
-
?
beta-amylase limit dextrin + H2O
?
beta-limit dextrin + H2O
?
beta-limit dextrin + H2O
linear maltooligosaccharides
beta-limit dextrin + H2O
maltose + ?
-
-
-
-
?
branched chain oligosaccharides + H2O
maltotriose + higher maltosaccharides
-
-
no detectable maltose released, characteristic action is hydrolysis of alpha 1,6-glucosidic linkages, but alpha 1,6 glucosidic linkages attaching maltose residues to chains of alpha 1,4-linked glucose residues are not readily hydrolyzed
?
D-glucose + H2O
?
-
59% of the activity with dextrin as substrate
-
-
?
dextrin + H2O
?
-
enzyme activity 100%
-
-
?
di-O-alpha-maltosyl-beta-cyclodextrin + H2O
maltose + beta-cyclodextrin
-
-
-
-
r
ginkgo starch + H2O
ginkgo amylose
-
74.74% yield at pH 5.0 and 52°C after 170 min
-
-
?
glycogen + H2O
linear maltooligosaccharides
glycogen + H2O
maltodextrin
glycogen + H2O
maltose + maltooligosaccharides
maize amylopectin + H2O
?
-
isoamylase hydrolyses both inner and outer branching linkages of amylopectin simultaneously
-
-
?
maize beta-limit dextrin + H2O
?
-
-
-
?
maltopentaose + H2O
?
-
sugar immobilized on Sepharose 4B
-
-
?
maltotriose + H2O
?
-
activity 28%
-
-
?
oyster gylcogen + H2O
maltose + maltooligosaccharides
O80403
-
-
-
?
panose + H2O
D-glucose + maltose
-
acts very slowly, small amounts of product formed after 24 h
-
?
phosphorylase a limit dextrin + H2O
?
phytoglycogen + H2O
maltose + maltooligosaccharides
O80403
-
-
-
?
potato amylopectin + H2O
?
-
-
-
?
potato starch + H2O
?
-
-
-
-
?
potato starch, boiled + H2O
?
pullulan + H2O
linear maltooligosaccharides
-
-
-
?
saccharose + H2O
?
-
activity 67%
-
-
?
starch + H2O
amylose
-
the enzyme has the ability to attack side chains composed of 1-3 glucose residues
-
-
?
starch + H2O
linear maltooligosaccharides
-
-
-
-
?
starch + H2O
maltose + maltooligosaccharides
O80403
-
-
-
?
sticky rice starch + H2O
?
-
-
-
?
waxy corn amylopectin + H2O
?
-
-
-
-
?
waxy rice starch + H2O
?
-
-
-
-
?
additional information
?
-
alpha-limit dextrin + H2O
linear maltooligosaccharides
-
-
-
-
?
alpha-limit dextrin + H2O
linear maltooligosaccharides
-
-
-
?
alpha-limit dextrin + H2O
linear maltooligosaccharides
-
-
-
?
amylopectin + H2O
?
-
-
-
?
amylopectin + H2O
?
-
-
-
?
amylopectin + H2O
?
-
-
-
-
?
amylopectin + H2O
?
-
-
-
?
amylopectin + H2O
?
-
-
-
?
amylopectin + H2O
?
-
the enzyme can debranch almost all of component chains of amylopectin and shows 9.4% activity compared to phosphorylase a limit dextrin
-
-
?
amylopectin + H2O
?
-
-
hydrolysis of alpha-1,6-linkages
-
?
amylopectin + H2O
?
-
-
hydrolysis of alpha-1,6-linkages
-
?
amylopectin + H2O
?
-
the enzyme shows 0.8% activity compared to phosphorylase a limit dextrin
-
-
?
amylopectin + H2O
?
-
-
-
?
amylopectin + H2O
?
-
-
-
-
?
amylopectin + H2O
?
-
isoform ISA1 removes the wide range of chains with a degree of polymerization (DP) of 6-20 from amylopectin although the long chains of DP higher than 20 are debranched by the prolonged incubation. Isoform ISA1 shows 356% activity compared to phosphorylase a limit dextrin. Isoform ISA3 shows trace activity compared to phosphorylase a limit dextrin
-
-
?
amylopectin + H2O
?
-
-
-
-
?
amylopectin + H2O
?
-
the enzyme can debranch almost all of component chains of amylopectin
-
-
?
amylopectin + H2O
?
-
-
-
?
amylopectin + H2O
?
-
-
-
-
?
amylopectin + H2O
?
B6U0X5
-
-
-
?
amylopectin + H2O
?
B6U0X5
-
-
-
?
amylopectin + H2O
amylose + linear maltooligosaccharides
-
-
-
?
amylopectin + H2O
amylose + linear maltooligosaccharides
-
-
-
?
amylopectin + H2O
linear maltooligosaccharides
-
-
-
?
amylopectin + H2O
linear maltooligosaccharides
-
-
-
-
?
amylopectin + H2O
linear maltooligosaccharides
-
-
-
-
?
amylopectin + H2O
maltose + maltooligosaccharides
-
specific cleavage of alpha 1,6-glucosidic inter-chain linkages producing essentially linear chains
-
-
?
amylopectin + H2O
maltose + maltooligosaccharides
-
or the beta-limit dextrins, cleaves the branching points completely in vitro
-
-
?
amylopectin + H2O
maltose + maltooligosaccharides
-
or the beta-limit dextrins, cleaves the branching points completely in vitro
-
?
amylopectin + H2O
maltose + maltooligosaccharides
-
isoamylase is a direct debranching enzyme with the ability to cleave all the alpha-1,6 linkages of glycogen both inner and outer branching points of soluble amylopectin
-
-
?
amylopectin + H2O
maltose + maltooligosaccharides
O80403
-
-
-
?
amylopectin + H2O
maltose + maltooligosaccharides
-
-
-
-
r
amylopectin + H2O
maltose + maltooligosaccharides
-
waxy maize amylopectin, potato amylopectin, amylopectin beta-dextrin
-
?
amylopectin + H2O
maltose + maltooligosaccharides
-
or the beta-limit dextrins, cleaves the branching points completely in vitro
-
?
amylopectin + H2O
maltose + maltooligosaccharides
-
or the beta-limit dextrins, cleaves the branching points completely in vitro
-
?
amylopectin + H2O
maltose + maltooligosaccharides
-
or the beta-limit dextrins, cleaves the branching points completely in vitro
-
?
amylopectin + H2O
maltose + maltooligosaccharides
-
or the beta-limit dextrins, cleaves the branching points completely in vitro
-
?
amylopectin + H2O
maltose + maltooligosaccharides
-
or the beta-limit dextrins, cleaves the branching points completely in vitro
-
?
amylopectin + H2O
maltose + maltooligosaccharides
-
or the beta-limit dextrins, cleaves the branching points completely in vitro
-
-
?
amylopectin + H2O
maltose + maltooligosaccharides
-
or the beta-limit dextrins, cleaves the branching points completely in vitro
hydrolysis of beta-limit dextrins forming maltotriose as main reaction product
?
amylopectin + H2O
maltose + maltooligosaccharides
-
or the beta-limit dextrins, cleaves the branching points completely in vitro
hydrolysis of beta-limit dextrins forming maltotriose as main reaction product
?
amylopectin + H2O
maltose + maltooligosaccharides
isoamylase is a direct debranching enzyme with the ability to cleave all the alpha-1,6 linkages of glycogen both inner and outer branching points of soluble amylopectin
-
-
?
amylopectin + H2O
maltose + maltooligosaccharides
isoamylase is a direct debranching enzyme with the ability to cleave all the alpha-1,6 linkages of glycogen both inner and outer branching points of soluble amylopectin
-
-
?
amylopectin + H2O
maltose + maltooligosaccharides
-
or the beta-limit dextrins, cleaves the branching points completely in vitro
-
-
?
amylopectin + H2O
maltose + maltooligosaccharides
-
or the beta-limit dextrins, cleaves the branching points completely in vitro
hydrolysis of beta-limit dextrins forming maltotriose as main reaction product
?
amylopectin + H2O
maltose + maltooligosaccharides
-
or the beta-limit dextrins, cleaves the branching points completely in vitro
-
-
r
Arabidopsis starch + H2O
?
-
-
-
?
Arabidopsis starch + H2O
?
-
-
-
?
beta-amylase limit dextrin + H2O
?
-
the enzyme shows 55% activity compared to phosphorylase a limit dextrin
-
-
?
beta-amylase limit dextrin + H2O
?
-
the enzyme shows 34% activity compared to phosphorylase a limit dextrin
-
-
?
beta-amylase limit dextrin + H2O
?
-
isoform ISA1 shows 71% activity compared to phosphorylase a limit dextrin. Isoform ISA3 shows 48% activity compared to phosphorylase a limit dextrin
-
-
?
beta-limit dextrin + H2O
?
-
-
-
?
beta-limit dextrin + H2O
?
-
-
-
?
beta-limit dextrin + H2O
?
-
-
-
?
beta-limit dextrin + H2O
?
-
-
-
?
beta-limit dextrin + H2O
?
-
-
-
-
?
beta-limit dextrin + H2O
?
-
-
-
?
beta-limit dextrin + H2O
?
best substrate
-
-
?
beta-limit dextrin + H2O
?
medium activity
-
-
?
beta-limit dextrin + H2O
?
-
-
-
-
?
beta-limit dextrin + H2O
?
B6U0X5
-
-
-
?
beta-limit dextrin + H2O
linear maltooligosaccharides
-
-
-
-
?
beta-limit dextrin + H2O
linear maltooligosaccharides
-
-
-
?
beta-limit dextrin + H2O
linear maltooligosaccharides
-
-
-
?
corn amylopectin + H2O
?
-
-
-
-
?
corn amylopectin + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
-
-
?
glycogen + H2O
?
-
80% activity compared to amylopectin
-
-
?
glycogen + H2O
?
-
80% activity compared to amylopectin
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
-
-
-
?
glycogen + H2O
linear maltooligosaccharides
-
-
-
?
glycogen + H2O
linear maltooligosaccharides
-
-
-
-
?
glycogen + H2O
maltodextrin
-
-
-
-
?
glycogen + H2O
maltodextrin
-
-
-
-
?
glycogen + H2O
maltose + maltooligosaccharides
-
cleaves the branching points completely in vitro
-
-
?
glycogen + H2O
maltose + maltooligosaccharides
-
or the beta-limit dextrins
-
-
?
glycogen + H2O
maltose + maltooligosaccharides
-
cleaves the branching points completely in vitro
-
?
glycogen + H2O
maltose + maltooligosaccharides
-
or the beta-limit dextrins
-
?
glycogen + H2O
maltose + maltooligosaccharides
-
-
-
-
?
glycogen + H2O
maltose + maltooligosaccharides
-
-
-
-
?
glycogen + H2O
maltose + maltooligosaccharides
-
-
-
-
?
glycogen + H2O
maltose + maltooligosaccharides
-
-
-
-
r
glycogen + H2O
maltose + maltooligosaccharides
-
-
-
?
glycogen + H2O
maltose + maltooligosaccharides
-
cleaves the branching points completely in vitro
-
?
glycogen + H2O
maltose + maltooligosaccharides
-
cleaves the branching points completely in vitro
-
?
glycogen + H2O
maltose + maltooligosaccharides
-
cleaves the branching points completely in vitro
-
?
glycogen + H2O
maltose + maltooligosaccharides
-
cleaves the branching points completely in vitro
-
?
glycogen + H2O
maltose + maltooligosaccharides
-
cleaves the branching points completely in vitro
-
?
glycogen + H2O
maltose + maltooligosaccharides
-
cleaves the branching points completely in vitro
-
?
glycogen + H2O
maltose + maltooligosaccharides
-
cleaves the branching points completely in vitro
-
-
?
glycogen + H2O
maltose + maltooligosaccharides
-
oyster glycogen, glycogen beta-dextrin, rabbit liver glycogen
-
?
glycogen + H2O
maltose + maltooligosaccharides
-
or the beta-limit dextrins
-
?
glycogen + H2O
maltose + maltooligosaccharides
-
or the beta-limit dextrins
-
?
glycogen + H2O
maltose + maltooligosaccharides
-
or the beta-limit dextrins
-
?
glycogen + H2O
maltose + maltooligosaccharides
-
or the beta-limit dextrins
-
?
glycogen + H2O
maltose + maltooligosaccharides
-
or the beta-limit dextrins
-
?
glycogen + H2O
maltose + maltooligosaccharides
-
or the beta-limit dextrins
-
?
glycogen + H2O
maltose + maltooligosaccharides
-
or the beta-limit dextrins
-
-
?
glycogen + H2O
maltose + maltooligosaccharides
-
-
-
?
glycogen + H2O
maltose + maltooligosaccharides
-
cleaves the branching points completely in vitro
-
-
?
glycogen + H2O
maltose + maltooligosaccharides
-
or the beta-limit dextrins
-
-
?
glycogen + H2O
maltose + maltooligosaccharides
-
cleaves the branching points completely in vitro
-
?
glycogen + H2O
maltose + maltooligosaccharides
-
or the beta-limit dextrins
-
?
glycogen + H2O
maltose + maltooligosaccharides
-
-
-
?
glycogen + H2O
maltose + maltooligosaccharides
-
cleaves the branching points completely in vitro
-
-
r
glycogen + H2O
maltose + maltooligosaccharides
-
or the beta-limit dextrins
-
-
r
maize starch + H2O
?
-
-
-
?
maize starch + H2O
?
-
-
-
-
?
maize starch + H2O
?
B6U0X5
-
-
-
?
maize starch + H2O
?
B6U0X5
-
-
-
?
maltodextrin + H2O
?
-
-
-
?
maltodextrin + H2O
?
-
-
-
?
maltose + H2O
?
-
iam gene induced by maltose
-
-
?
maltose + H2O
?
-
-
-
-
?
maltose + H2O
?
-
iam gene induced by maltose
-
-
?
maltose + H2O
?
-
iam gene induced by maltose
-
-
?
maltose + H2O
?
-
iam gene induced by maltose
-
-
?
maltose + H2O
?
-
iam gene induced by maltose
-
-
?
oyster glycogen + H2O
?
-
-
-
?
oyster glycogen + H2O
?
-
the enzyme shows 14% activity compared to phosphorylase a limit dextrin
-
-
?
oyster glycogen + H2O
?
-
the enzyme shows 2% activity compared to phosphorylase a limit dextrin
-
-
?
oyster glycogen + H2O
?
O80403
-
-
-
?
oyster glycogen + H2O
?
-
isoform ISA1 shows 104% activity compared to phosphorylase a limit dextrin. Isoform ISA3 shows 1.5% activity compared to phosphorylase a limit dextrin
-
-
?
phosphorylase a limit dextrin + H2O
?
-
100% activity
-
-
?
phosphorylase a limit dextrin + H2O
?
-
100% activity
-
-
?
phosphorylase a limit dextrin + H2O
?
-
100% activity
-
-
?
phythoglycogen + H2O
?
-
-
-
-
r
phythoglycogen + H2O
?
-
highly branched polysaccharide, complete hydrolysis of the alpha-1,6-glucosidic bonds
-
-
?
phythoglycogen + H2O
?
-
-
-
-
r
phytoglycogen + H2O
?
-
the liberated chains formed two distinct peaks: the first large peak of DP3-4 and the second small peak of DP5-10
-
-
?
phytoglycogen + H2O
?
-
the enzyme removes only exclusively chains of DP3 and DP4 when incubated with phytoglycogen while DP5-7 chains are slightly liberated after the prolonged incubation
-
-
?
phytoglycogen + H2O
?
-
short chains of DP3 and DP4 are most effectively liberated by isoform ISA1 during the short period, and with the elapse of the incubation time intermediate chains with the peak of DP6 are more significantly produced. Almost only short chains of DP3 and DP4 are found after the isoform ISA3 reaction for 5-10 min, then during the course of enzymatic reaction until 60 min a small amount of the DP5-10 chains is found
-
-
?
phytoglycogen + H2O
?
-
the enzyme can debranch almost all of component chains of phytoglycogen
-
-
?
phytoglycogen + H2O
?
-
-
-
?
phytoglycogen + H2O
?
little activity
-
-
?
phytoglycogen + H2O
?
-
the liberated chains from phytoglycogen are enriched in short chains of DP3-6, but contained longer chains of DP higer than 7, decreasing in amounts with the increase in chain-length until DP about 15
-
-
?
phytoglycogen + H2O
?
-
the liberated chains from phytoglycogen are enriched in short chains of DP3-6, but contained longer chains of DP higer than 7, decreasing in amounts with the increase in chain-length until DP about 15
-
-
?
potato starch, boiled + H2O
?
best substrate
-
-
?
potato starch, boiled + H2O
?
little activity
-
-
?
pullulan + H2O
?
-
-
-
?
pullulan + H2O
?
little activity
-
-
?
soluble starch + H2O
?
-
-
-
?
soluble starch + H2O
?
-
-
-
?
soluble starch + H2O
?
-
-
-
-
?
starch + H2O
?
hydrolysis of alpha-1,6-glycosidic linkages
-
-
?
starch + H2O
?
specific hydrolysis of alpha-1,6-glucosidic linkages
detection of aminobenzamide-labeled maltooligosaccharide products, overview
-
?
starch + H2O
?
specific hydrolysis of alpha-1,6-glucosidic linkages
detection of aminobenzamide-labeled maltooligosaccharide products, overview
-
?
starch + H2O
?
-
debranching of Cassava starch in concert with pullulanase yielding resistant starch type III. Effects of starch concentration, isoamylase concentration and incubation time on hydrolysis of cassava starch, overview
-
-
?
starch + H2O
?
-
soluble starch, immobilized on Sepharose 4B
-
-
?
additional information
?
-
AtISA1 and AtISA2 are required for the production of a functional isoamylase-type of debranching enzyme named Iso1, the major isoamylase found in leaves. The absence of Iso1 leads to an 80% decrease in the starch content and to accumulation of water-soluble polysaccharides whose structure is similar to glycogen
-
-
?
additional information
?
-
AtISA1 and AtISA2 are required for the production of a functional isoamylase-type of debranching enzyme named Iso1, the major isoamylase found in leaves. The absence of Iso1 leads to an 80% decrease in the starch content and to accumulation of water-soluble polysaccharides whose structure is similar to glycogen
-
-
?
additional information
?
-
AtISA1 and AtISA2 are required for the production of a functional isoamylase-type of debranching enzyme named Iso1, the major isoamylase found in leaves. The absence of Iso1 leads to an 80% decrease in the starch content and to accumulation of water-soluble polysaccharides whose structure is similar to glycogen
-
-
?
additional information
?
-
-
AtISA1/AtISA2 isoamylase influences glucan branching pattern
-
-
?
additional information
?
-
-
glucan debranching occurs primarily at the granule surface via ISA3, but in its absence soluble branched glucans are debranched in the stroma via limit dextrinase. Isoamylase acts at the surface of the starch granule. Atisa3 mutants have more leaf starch and a slower rate of starch breakdown than wild-type plants
-
-
?
additional information
?
-
mutant lines carrying a defect in AtISA3 display a strong starch-excess phenotype at the end of both the light and the dark phases accompanied by a small modification of the amylopectin structure
-
-
?
additional information
?
-
mutant lines carrying a defect in AtISA3 display a strong starch-excess phenotype at the end of both the light and the dark phases accompanied by a small modification of the amylopectin structure
-
-
?
additional information
?
-
mutant lines carrying a defect in AtISA3 display a strong starch-excess phenotype at the end of both the light and the dark phases accompanied by a small modification of the amylopectin structure
-
-
?
additional information
?
-
synthesis of amylopectin and phytoglycogen by associated and separated ISA1 and ISA2, respectively, overview
-
-
?
additional information
?
-
synthesis of amylopectin and phytoglycogen by associated and separated ISA1 and ISA2, respectively, overview
-
-
?
additional information
?
-
-
isoamylase catalyzes the hydrolysis of alpha-1,6-glucosidic linkage specifically in amylopectin, glycogen and derived oligosaccharides
-
-
?
additional information
?
-
-
isoamylase catalyzes the hydrolysis of alpha-1,6-glucosidic linkage specifically in amylopectin, glycogen and derived oligosaccharides
-
-
?
additional information
?
-
pullulan is a poor substrate
-
-
?
additional information
?
-
-
pullulan is a poor substrate
-
-
?
additional information
?
-
pullulan is a poor substrate
-
-
?
additional information
?
-
-
no substrate: pullulan, glycogen
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-
?
additional information
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-
pullulan is a poor substrate
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?
additional information
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pullulan is a poor substrate
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-
?
additional information
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-
pullulan is a poor substrate
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-
?
additional information
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-
pullulan is a poor substrate
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-
?
additional information
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-
pullulan is a poor substrate
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-
?
additional information
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-
-
no substrate: dextran, amylose
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-
?
additional information
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-
-
no substrate: dextran, amylose
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-
?
additional information
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-
-
no activity with amylose
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-
?
additional information
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-
-
no activity with pullulan
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-
?
additional information
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-
-
no activity towards pullulan
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-
?
additional information
?
-
-
ISA1 activity plays a critical role in the stochastic process in starch synthesis in rice endosperm
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?
additional information
?
-
-
recombinant isoamylase 3 does not readily hydrolyze red pullulan and amylose
-
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?
additional information
?
-
-
isoform Psisa2 most likely does not have catalytic activity
-
-
?
additional information
?
-
-
direct debranching enzyme, attacks unmodified glycogen and/or amylopectin with hydrolysis of the 1,6-bond, smallest substrate is not known
-
-
?
additional information
?
-
-
direct debranching enzyme, attacks unmodified glycogen and/or amylopectin with hydrolysis of the 1,6-bond, smallest substrate is not known
-
-
?
additional information
?
-
-
distinguished from alpha-dextrin endo-1,6-alpha-glucosidase, EC 3.2.1.41, by the inability of isoamylase to attack pullulan, and by limited action on alpha-limit dextrins, action on glycogen however is complete in contrast to limited action by alpha-dextrin glucanohydrolase, 1,6-linkage hydrolysed only at branch point
-
-
?
additional information
?
-
-
isoamylase is one of the starch-debranching enzymes which catalyzes the hydrolysis of alpha-1,6-glucosidic linkages specific in alpha-glucans including amylopectin, branched starch, and glycogen
-
-
?
additional information
?
-
no activity towards pullulan
-
-
?
additional information
?
-
no activity towards pullulan
-
-
?
additional information
?
-
-
isoamylase is one of the starch-debranching enzymes which catalyzes the hydrolysis of alpha-1,6-glucosidic linkages specific in alpha-glucans including amylopectin, branched starch, and glycogen
-
-
?
additional information
?
-
-
TreX from Sulfolobus solfataricus shows dual activities for alpha-1,4-transferase, EC 2.4.1.25 and alpha-1,6-glucosidase, EC 3.2.1.68, bifunctional mechanism, substrate glycogen, overview. TreX exhibits two different active-site configurations depending on its oligomeric state
-
-
?
additional information
?
-
-
direct debranching enzyme, attacks unmodified glycogen and/or amylopectin with hydrolysis of the 1,6-bond, smallest substrate is not known
-
-
?
additional information
?
-
-
distinguished from alpha-dextrin endo-1,6-alpha-glucosidase, EC 3.2.1.41, by the inability of isoamylase to attack pullulan, and by limited action on alpha-limit dextrins, action on glycogen however is complete in contrast to limited action by alpha-dextrin glucanohydrolase, 1,6-linkage hydrolysed only at branch point
-
-
?
additional information
?
-
involved in starch synthesis
-
-
?
additional information
?
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involved in starch synthesis
-
-
?
additional information
?
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involved in starch synthesis
-
-
?
additional information
?
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-
involved in starch synthesis
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-
?
additional information
?
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involved in synthesis of reserve and leaf starches
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?
additional information
?
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isoamylase1 is directly involved in the synthesis of amylopectin
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?
additional information
?
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Zea mays subunit ISA 2 alone is catalytically inactive
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?
additional information
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B6U0X5
Zea mays subunit ISA 2 alone is catalytically inactive
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-
?
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evolution
subunit ISA1 is a family 13 glycoside hydrolase, which has activity for hydrolyzing alpha-1,6-glucosidic linkages corresponding to branch points of growing amylopectin molecules
evolution
subunit ISA2 is a family 13 glycoside hydrolase, but its putative catalytic residues are altered, rendering it enzymatically inactive. Despite its inactivity, ISA2 is evolutionarily conserved in plants, and has been suggested to play a role as a regulatory subunit for ISA1
evolution
B6U0X5
the enzyme belongs to the glycosyl hydrolase family 13 GH13, and harbors a carbohydrate-binding module family 48 (CBM48) domain
evolution
B6U0X5
the enzyme belongs to the glycosyl hydrolase family 13 GH13, and harbors a carbohydrate-binding module family 48 (CBM48) domain
evolution
the enzyme harbors a carbohydrate-binding module family 48 (CBM48) domain
evolution
-
subunit ISA2 is a family 13 glycoside hydrolase, but its putative catalytic residues are altered, rendering it enzymatically inactive. Despite its inactivity, ISA2 is evolutionarily conserved in plants, and has been suggested to play a role as a regulatory subunit for ISA1
-
evolution
-
subunit ISA1 is a family 13 glycoside hydrolase, which has activity for hydrolyzing alpha-1,6-glucosidic linkages corresponding to branch points of growing amylopectin molecules
-
evolution
-
the enzyme harbors a carbohydrate-binding module family 48 (CBM48) domain
-
malfunction
-
both overexpression and loss of function of isoamylase 3 in the endosperm generated pleomorphic amyloplasts and starch granules
malfunction
loss of isozyme ISA1 or ISA2 causes phytoglycogen accumulation
malfunction
mutants of the STA8 locus accumulate both phytoglycogen and a reduced amount of high amylose starch
malfunction
mutation of the STA7 locus leads to a very severe reduction of starch content and its replacement by a water-soluble polysaccharide phytoglycogen
malfunction
B6U0X5
the ISA1 homomer does not provide the full physiological function of ISA activity in maize leaves. This is in contrast to the endosperm, where loss of ISA2, and thus the ISA1/ISA2 heteromeric enzyme, can be tolerated without major defects. Mutants without ISA2 differ in leaf starch content, granule morphology, and amylopectin structure compared with nonmutants or lines lacking both ISA1 and ISA2, mutant phenotypes, overview
malfunction
B6U0X5
the ISA1 homomer does not provide the full physiological function of ISA activity in maize leaves. This is in contrast to the endosperm, where loss of ISA2, and thus the ISA1/ISA2 heteromeric enzyme, can be tolerated without major defects. Mutants without ISA2 differ in leaf starch content, granule morphology, and amylopectin structure compared with nonmutants or lines lacking both ISA1 and ISA2. Plastids from maize leaves lacking ISA2 exhibit a nearly normal appearance with the exception that starch granules appear to be slightly smaller than in wild-type, mutant phenotypes, overview
malfunction
-
seeds of the homozygous mutants, cr-isa1-1 (type 1, with an adenine insertion) and cr-isa1-2 (type 3, with a cytosine deletion) display a shrunken endosperm with significantly lower grain weight. Abnormal starch granules and amyloplasts are found in cr-isa1-1 and cr-isa1-2 endosperm cells. The contents of total starch, amylose and amylopectin in the endosperm of the cr-isa1 mutants are significantly reduced, whereas sugar content and starch gel consistency were observably increased compared to the wild type. The gelatinization temperature and starch chain length distributions of the cr-isa1 mutants are also altered. The transcript levels of most starch synthesis-related genes are significantly lower in cr-isa1 mutants
malfunction
-
mutants of the STA8 locus accumulate both phytoglycogen and a reduced amount of high amylose starch
-
malfunction
-
mutation of the STA7 locus leads to a very severe reduction of starch content and its replacement by a water-soluble polysaccharide phytoglycogen
-
physiological function
-
isoamylase 3 facilitates starch metabolism and affects morphological characteristics of plastids in rice. Both overexpression and loss of function of isoamylase 3 in the endosperm generates pleomorphic amyloplasts and starch granules
physiological function
-
the isoamylase 1 is essential for amylopectin biosynthesis and starch production in rice endosperm. Overexpression of the isoamylase 2 gene brings about a dramatic reduction in kernel size in the dry seed and the transformants contain less than 50% of the starch in the kernel, while the content of soluble sugars, including maltodextrins, malto-oligosaccharides, and simple sugars, increase by about 8fold when compared with the host cultivar Kinmaze
physiological function
the isoamylase ISA1/ISA2 heteromeric complexes II and III are not required in maize endosperm for normal starch content and structure, and the ISA1 homomeric complex is sufficient for most ISA functions. ISA1 is required for the accumulation of ISA2, which is regulated posttranscriptionally, while the absence of ISA2 in isa2-339 mutants has no effect on the accumulation of ISA1 mRNA or protein
physiological function
isoamylase catalyzes hydrolysis of alpha-D-(1,6)-glucosidic branch linkages in amylopectin and glycogen to release amylose and linear maltooligosaccharides
physiological function
starch debranching enzymes isoamylase 1 and 2, ISA1 and ISA2, are known to exist in a large complex and are involved in the biosynthesis and crystallization of starch. The function of the complex is to remove misplaced branches of growing amylopectin molecules, which would otherwise prevent the association and crystallization of adjacent linear chains
physiological function
starch debranching enzymes isoamylase 1 and 2, ISA1 and ISA2, are known to exist in a large complex and are involved in the biosynthesis and crystallization of starch. The function of the complex is to remove misplaced branches of growing amylopectin molecules, which would otherwise prevent the association and crystallization of adjacent linear chains. ISA2 plays a role as a regulatory subunit for ISA1
physiological function
the ISA1 class of DBE is the one primarily associated with amylopectin synthesis
physiological function
-
starch debranching enzymes isoamylase 1 and 2, ISA1 and ISA2, are known to exist in a large complex and are involved in the biosynthesis and crystallization of starch. The function of the complex is to remove misplaced branches of growing amylopectin molecules, which would otherwise prevent the association and crystallization of adjacent linear chains. ISA2 plays a role as a regulatory subunit for ISA1
-
physiological function
-
starch debranching enzymes isoamylase 1 and 2, ISA1 and ISA2, are known to exist in a large complex and are involved in the biosynthesis and crystallization of starch. The function of the complex is to remove misplaced branches of growing amylopectin molecules, which would otherwise prevent the association and crystallization of adjacent linear chains
-
physiological function
-
isoamylase catalyzes hydrolysis of alpha-D-(1,6)-glucosidic branch linkages in amylopectin and glycogen to release amylose and linear maltooligosaccharides
-
additional information
Arabidopsis thaliana subunit ISA1 requires subunit ISA2 as a partner for enzymatic function. Images of purified starch granules of wild-type and mutant lines, overview
additional information
Arabidopsis thaliana subunit ISA1 requires subunit ISA2 as a partner for enzymatic function. Images of purified starch granules of wild-type and mutant lines, overview
additional information
Arabidopsis thaliana subunit ISA1 requires subunit ISA2 as a partner for enzymatic function. Images of purified starch granules of wild-type and mutant lines, overview. Recombinant AtISA1 is capable of enzymatic activity if mixed with recombinant AtISA2 but does not display such function on its own
additional information
Arabidopsis thaliana subunit ISA1 requires subunit ISA2 as a partner for enzymatic function. Images of purified starch granules of wild-type and mutant lines, overview. Recombinant AtISA1 is capable of enzymatic activity if mixed with recombinant AtISA2 but does not display such function on its own
additional information
isozyme ISA1 interacts with its homologue ISA2, but no evidence for interaction with other starch biosynthetic enzymes. ISA1 and ISA2 form a heteromultimeric enzyme with ISA1 being the catalytic subunit and ISA2 subunit not catalytically active
additional information
isozyme ISA1 interacts with its homologue ISA2, but no evidence for interaction with other starch biosynthetic enzymes. ISA1 and ISA2 form a heteromultimeric enzyme with ISA1 being the catalytic subunit and ISA2 subunit not catalytically active
additional information
subunit ISA2 interacts physically with ISA1, presence of both homomeric ISA1 and heteromeric ISA1-ISA2 complexes in vivo
additional information
subunit ISA2 interacts physically with ISA1, presence of both homomeric ISA1 and heteromeric ISA1-ISA2 complexes in vivo
additional information
-
subunit ISA2 interacts physically with ISA1, presence of both homomeric ISA1 and heteromeric ISA1-ISA2 complexes in vivo
additional information
subunit ISA2 interacts physically with ISA1, presence of both homomeric ISA1 and heteromeric ISA1-ISA2 complexes in vivo. Subunit ISA1 enzyme is also partially functional without subunit ISA2
additional information
subunit ISA2 interacts physically with ISA1, presence of both homomeric ISA1 and heteromeric ISA1-ISA2 complexes in vivo. Subunit ISA1 enzyme is also partially functional without subunit ISA2
additional information
-
subunit ISA2 interacts physically with ISA1, presence of both homomeric ISA1 and heteromeric ISA1-ISA2 complexes in vivo. Subunit ISA1 enzyme is also partially functional without subunit ISA2
additional information
-
Zea mays subunit ISA1 is active by itself and does not require subunit ISA2 for activity, subunit ISA 2 alone is catalytically inactive
additional information
B6U0X5
Zea mays subunit ISA1 is active by itself and does not require subunit ISA2 for activity, subunit ISA 2 alone is catalytically inactive
additional information
-
Zea mays subunit ISA1 is active by itself, either in vitro or in transgenic Arabidopsis leaves, and does not require subunit ISA2 for activity
additional information
B6U0X5
Zea mays subunit ISA1 is active by itself, either in vitro or in transgenic Arabidopsis leaves, and does not require subunit ISA2 for activity
additional information
-
subunit ISA2 interacts physically with ISA1, presence of both homomeric ISA1 and heteromeric ISA1-ISA2 complexes in vivo
-
additional information
-
subunit ISA2 interacts physically with ISA1, presence of both homomeric ISA1 and heteromeric ISA1-ISA2 complexes in vivo. Subunit ISA1 enzyme is also partially functional without subunit ISA2
-
additional information
-
Arabidopsis thaliana subunit ISA1 requires subunit ISA2 as a partner for enzymatic function. Images of purified starch granules of wild-type and mutant lines, overview. Recombinant AtISA1 is capable of enzymatic activity if mixed with recombinant AtISA2 but does not display such function on its own
-
additional information
-
Arabidopsis thaliana subunit ISA1 requires subunit ISA2 as a partner for enzymatic function. Images of purified starch granules of wild-type and mutant lines, overview
-
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Amemura, A.; Chakraborty, R.; Fujita, M.; Noumi, T.; Masamitsu, F.
Cloning and nucleotide sequence of the isoamylase gene from Pseudomonas amyloderamosa SB-15
J. Biol. Chem.
263
9271-9275
1988
Pseudomonas amyloderamosa
brenda
Ishizaki, Y.; Taniguchi, H.; Maruyama, Y.; Nakamura, M.
Debranching enzymes of potato tubers (Solanum tuberosum L.). I. Purification and some properties of potato isoamylase
Agric. Biol. Chem.
47
771-779
1983
Solanum tuberosum
-
brenda
Spencer-Martins, I.
Extracellular isoamylase produced by the yeast Lipomyces kononenkoae
Appl. Environ. Microbiol.
44
1253-1257
1982
Lipomyces kononenkoae
brenda
Amemura, A.; Konishi, Y.; Harada, T.
Molecular weight of the undegraded polypeptide chain of Pseudomonas amyloderamosa isoamylase
Biochim. Biophys. Acta
611
390-393
1980
Pseudomonas amyloderamosa
brenda
Kato, K.; Konishi, Y.; Amemura, A.; Harada, T.
Affinity chromatography of Pseudomonas isoamylase on cross-linked amylose gel
Agric. Biol. Chem.
41
2077-2080
1977
Pseudomonas amyloderamosa
-
brenda
Kitagawa, H.; Amemura, A.; Harada, T.
Studies on the inhibition and molecular properties of crystalline Pseudomonas isoamylase
Agric. Biol. Chem.
39
989-994
1975
Pseudomonas amyloderamosa
-
brenda
Lee, E.Y.C.; Whelan, W.J.
Glycogen and starch debranching enzymes
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
5
191-234
1972
Cytophaga sp., Pseudomonas amyloderamosa
-
brenda
Yokobayashi, K.; Misaki, A.; Harada, T.
Purification and properties of Pseudomonas isoamylase
Biochim. Biophys. Acta
212
458-469
1970
Pseudomonas amyloderamosa
brenda
Fujita, F.; Sakai, S.; Futai, M.; Amemura, A.
Characterization of an isoamylase-hyperproducing mutant of Pseudomonas amyloderamosa
Agric. Biol. Chem.
54
2315-2321
1990
Pseudomonas amyloderamosa, Pseudomonas amyloderamosa MI-414
-
brenda
Katsuya, Y.; Mezaki, Y.; Kubota, M.; Matsuura, Y.
Three-dimensional structure of Pseudomonas isoamylase at 2.2 A resolution
J. Mol. Biol.
281
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1998
Pseudomonas amyloderamosa
brenda
Ara, K.; Saeki, K.; Ito, S.
Purification and characterization of an alkaline isomylase from an alkalophilic strain of Bacillus
J. Gen. Microbiol.
139
781-786
1993
Bacillus sp. (in: Bacteria), Pseudomonas amyloderamosa, Pseudomonas amyloderamosa SMP1
-
brenda
Lin, L.L.; Fang, T.Y.; Chu, W.S.; Hsu, W.H.
Improved elution of isoamylase adsorbed on raw starch and the preservation of purified enzyme
Lett. Appl. Microbiol.
19
383-385
1994
Pseudomonas amyloderamosa, Pseudomonas amyloderamosa WU-5315
-
brenda
Clave, P.; Guillaumes, S.; Blanco, I.; Nabau, N.; Merce, J.; Farre, A.; Marruecos, L.; Lluis, F.
Amylase, lipase, pancreatic isoamylase, and phospholipase A in diagnosis of acute pancreatitis
Clin. Chem.
41
1129-1134
1995
Homo sapiens
brenda
Ito, S.; Kobayashi, T.; Ara, K.; Ozaki, K.; Kawai, S.; Hatada, Y.
Alkaline detergent enzymes from alkaliphiles: enzymatic properties, genetics, and structures
Extremophiles
2
185-190
1998
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) KSM-K16
brenda
Krohn, M.; Barry, G.F.; Kishore, G.M.
An isoamylase with neutral pH optimum from a Flavobacterium species: cloning, characterization and expression of the iam gene
Mol. Gen. Genet.
254
469-478
1997
Flavobacterium sp., Pseudomonas amyloderamosa, Pseudomonas amyloderamosa JD210, Pseudomonas amyloderamosa SMP1
brenda
Rahman, A.; Wong, K.s.; Jane, J.l.; Myers, A.M.; James, M.G.
Characterization of SU1 isoamylase, a determinant of storage starch structure in maize
Plant Physiol.
117
425-435
1998
Zea mays
brenda
Fujita, N.; Kubo, A.; Francisco, P.B.Jr.; Nakakita, M.; Harada, K.; Minaka, N.; Nakamura, Y.
Purification, characterization, and cDNA structure of isoamylase from developing endosperm of rice
Planta
208
283-293
1999
Oryza sativa
brenda
Lim, W.J.; Park, S.R.; Cho, S.J.; Kim, M.K.; Ryu, S.K.; Hong, S.Y.; Seo, W.T.; Kim, H.; Yun, H.D.
Cloning and characterization of an intracellular isoamylase gene from Pectobacterium chrysanthemi PY35
Biochem. Biophys. Res. Commun.
287
348-354
2001
Dickeya chrysanthemi, Dickeya chrysanthemi PY35
brenda
Hussain, H.; Mant, A.; Seale, R.; Zeeman, S.; Hinchliffe, E.; Edwards, A.; Hylton, C.; Bornemann, S.; Smith, A.M.; Martin, C.; Bustos, R.
Three isoforms of isoamylase contribute different catalytic properties for the debranching of potato glucans
Plant Cell
15
133-149
2003
Solanum tuberosum (Q84YG5), Solanum tuberosum (Q84YG6), Solanum tuberosum (Q84YG7), Solanum tuberosum
brenda
Dauvillee, D.; Colleoni, C.; Mouille, G.; Morell, M.K.; d'Hulst, C.; Wattebled, F.; Lienard, L.; Delvalle, D.; Ral, J.P.; Myers, A.M.; Ball, S.G.
Biochemical characterization of wild-type and mutant isoamylases of Chlamydomonas reinhardtii supports a function of the multimeric enzyme organization in amylopectin maturation
Plant Physiol.
125
1723-1731
2001
Chlamydomonas reinhardtii
brenda
Dauvillee, D.; Mestre, V.V.; Colleoni, C.; Slomianny, M.; Mouille, G.; Delrue, B.; d'Hulst, C.; Bliard, C.; Nuzillard, J.; Ball, S.
The debranching enzyme complex missing in glycogen accumulating mutants of Chlamydomonas reinhardtii displays an isoamylase-type specificity
Plant Sci.
157
145-156
2000
Chlamydomonas reinhardtii
brenda
Genschel, U.; Abel, G.; Loerz, H.; Luetticke, S.
The sugary-type isoamylase in wheat: tissue distribution and subcellular localisation
Planta
214
813-820
2002
Triticum aestivum
brenda
Bustos, R.; Fahy, B.; Hylton, C.M.; Seale, R.; Nebane, N.M.; Edwards, A.; Martin, C.; Smith, A.M.
Starch granule initiation is controlled by a heteromultimeric isoamylase in potato tubers
Proc. Natl. Acad. Sci. USA
101
2215-2220
2004
Solanum tuberosum
brenda
Kawagoe, Y.; Kubo, A.; Satoh, H.; Takaiwa, F.; Nakamura, Y.
Roles of isoamylase and ADP-glucose pyrophosphorylase in starch granule synthesis in rice endosperm
Plant J.
42
164-174
2005
Oryza sativa
brenda
Yoon, S.; Robyt, J.F.
Activation and stabilization of 10 starch-degrading enzymes by Triton X-100, polyethylene glycols, and polyvinyl alcohols
Enzyme Microb. Technol.
37
556-562
2005
Pseudomonas amyloderamosa
-
brenda
Bierhals, J.D.; Lajolo, F.M.; Cordenunsi, B.R.; Oliveira do Nascimento, J.R.
Activity, cloning, and expression of an isoamylase-type starch-debranching enzyme from banana fruit
J. Agric. Food Chem.
52
7412-7418
2004
Musa acuminata
brenda
Delatte, T.; Umhang, M.; Trevisan, M.; Eicke, S.; Thorneycroft, D.; Smith, S.M.; Zeeman, S.C.
Evidence for distinct mechanisms of starch granule breakdown in plants
J. Biol. Chem.
281
12050-12059
2006
Arabidopsis thaliana
brenda
Fang, T.; Tseng, W.; Yu, C.; Shih, T.
Characterization of the thermophilic isoamylase from the thermophilic archaeon Sulfolobus solfataricus ATCC 35092
J. Mol. Catal. B
33
99-107
2005
Saccharolobus solfataricus
-
brenda
Delatte, T.; Trevisan, M.; Parker, M.L.; Zeeman, S.C.
Arabidopsis mutants Atisa1 and Atisa2 have identical phenotypes and lack the same multimeric isoamylase, which influences the branch point distribution of amylopectin during starch synthesis
Plant J.
41
815-830
2005
Arabidopsis thaliana
brenda
Kubo, A.; Rahman, S.; Utsumi, Y.; Li, Z.; Mukai, Y.; Yamamoto, M.; Ugaki, M.; Harada, K.; Satoh, H.; Konik-Rose, C.; Morell, M.; Nakamura, Y.
Complementation of sugary-1 phenotype in rice endosperm with the wheat isoamylase1 gene supports a direct role for isoamylase1 in amylopectin biosynthesis
Plant Physiol.
137
43-56
2005
Triticum aestivum
brenda
Wattebled, F.; Dong, Y.; Dumez, S.; Delvalle, D.; Planchot, V.; Berbezy, P.; Vyas, D.; Colonna, P.; Chatterjee, M.; Ball, S.; D'Hulst, C.
Mutants of Arabidopsis lacking a chloroplastic isoamylase accumulate phytoglycogen and an abnormal form of amylopectin
Plant Physiol.
138
184-195
2005
Arabidopsis thaliana (O04196), Arabidopsis thaliana (Q8L735), Arabidopsis thaliana (Q9M0S5)
brenda
Park, H.S.; Park, J.T.; Kang, H.K.; Cha, H.; Kim, D.S.; Kim, J.W.; Park, K.H.
TreX from Sulfolobus solfataricus ATCC 35092 displays isoamylase and 4-alpha-glucanotransferase activities
Biosci. Biotechnol. Biochem.
71
1348-1352
2007
Saccharolobus solfataricus
brenda
Kang, H.K.; Cha, H.; Yang, T.J.; Park, J.T.; Lee, S.; Kim, Y.W.; Auh, J.H.; Okada, Y.; Kim, J.W.; Cha, J.; Kim, C.H.; Park, K.H.
Enzymatic synthesis of dimaltosyl-beta-cyclodextrin via a transglycosylation reaction using TreX, a Sulfolobus solfataricus P2 debranching enzyme
Biochem. Biophys. Res. Commun.
366
98-103
2008
Pseudomonas amyloderamosa
brenda
Takashima, Y.; Senoura, T.; Yoshizaki, T.; Hamada, S.; Ito, H.; Matsui, H.
Differential chain-length specificities of two isoamylase-type starch-debranching enzymes from developing seeds of kidney bean
Biosci. Biotechnol. Biochem.
71
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2007
Phaseolus vulgaris (A4PIS8), Phaseolus vulgaris (A4PIS9), Phaseolus vulgaris (A4PIT0), Phaseolus vulgaris
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Li, L.; Ilarslan, H.; James, M.G.; Myers, A.M.; Wurtele, E.S.
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Arabidopsis thaliana
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Structural and enzymatic characterization of the isoamylase1 homo-oligomer and the isoamylase1-isoamylase2 hetero-oligomer from rice endosperm
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Oryza sativa, Oryza sativa (O80403)
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Pseudomonas amyloderamosa
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Woo, E.J.; Lee, S.; Cha, H.; Park, J.T.; Yoon, S.M.; Song, H.N.; Park, K.H.
Structural Insight into the Bifunctional Mechanism of the Glycogen-debranching Enzyme TreX from the Archaeon Sulfolobus solfataricus
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Pseudomonas sp.
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Hussain, H.; Martin, C.
Comparative analysis of primary and secondary structure for pea isoamylase isoforms predicts different catalytic properties against glucan substrates
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Zea mays (Q84UE6), Zea mays
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Utsumi, Y.; Utsumi, C.; Sawada, T.; Fujita, N.; Nakamura, Y.
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Oryza sativa
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Arthrobacter sp., Arthrobacter sp. Q36
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Xu, Y.; Zhou, X.; Bai, Y.; Wang, J.; Wu, C.; Xu, X.; Jin, Z.
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Chlamydomonas reinhardtii (A8IQR3), Chlamydomonas reinhardtii (Q7X8Q2), Chlamydomonas reinhardtii, Chlamydomonas reinhardtii 330 (A8IQR3), Chlamydomonas reinhardtii 330 (Q7X8Q2)
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Li, Y.; Niu, D.; Zhang, L.; Wang, Z.; Shi, G.
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Zea mays, Zea mays (B6U0X5)
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Zea mays, Zea mays (B6U0X5), Arabidopsis thaliana (O04196), Arabidopsis thaliana (Q8L735), Arabidopsis thaliana Col-0 (O04196), Arabidopsis thaliana Col-0 (Q8L735)
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Sundberg, M.; Pfister, B.; Fulton, D.; Bischof, S.; Delatte, T.; Eicke, S.; Stettler, M.; Smith, S.M.; Streb, S.; Zeeman, S.C.
The heteromultimeric debranching enzyme involved in starch synthesis in Arabidopsis requires both isoamylase1 and isoamylase2 subunits for complex stability and activity
PLoS ONE
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Arabidopsis thaliana (O04196), Arabidopsis thaliana (Q8L735)
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Ran, H.; Wu, J.; Wu, D.; Duan, X.
Enhanced production of recombinant Thermobifida fusca isoamylase in Escherichia coli MDS42
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Thermobifida fusca
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Li, Y.; Xu, J.; Zhang, L.; Ding, Z.; Gu, Z.; Shi, G.
Investigation of debranching pattern of a thermostable isoamylase and its application for the production of resistant starch
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Lederbergia lentus
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Hu, L.; Zheng, Y.; Peng, Y.; Yao, C.; Zhang, H.
The optimization of isoamylase processing conditions for the preparation of high-amylose ginkgo starch
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Pseudomonas sp.
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Li, Y.; Zhang, L.; Ding, Z.; Gu, Z.; Shi, G.
Engineering of isoamylase improvement of protein stability and catalytic efficiency through semi-rational design
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Lederbergia lentus, Lederbergia lentus JNU3
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Nabemoto, M.; Watanabe, R.; Ohsu, M.; Sato, K.; Otani, M.; Nakayachi, O.; Watanabe, M.
Molecular characterization of genes encoding isoamylase-type debranching enzyme in tuberous root of sweet potato, Ipomoea batatas (L.) Lam.
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Ipomoea batatas (Q1AJM7)
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Kobayashi, T.; Sasaki, S.; Utsumi, Y.; Fujita, N.; Umeda, K.; Sawada, T.; Kubo, A.; Abe, J.; Colleoni, C.; Ball, S.; Nakamura, Y.
Comparison of chain-length preferences and glucan specificities of isoamylase-type alpha-glucan debranching enzymes from rice, Cyanobacteria, and Bacteria
PLoS ONE
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Escherichia coli, Oryza sativa, Pseudomonas amyloderamosa, Synechococcus elongatus, Crocosphaera subtropica ATCC 51142, Synechococcus elongatus PCC7942
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Shufen, C.; Yicong, C.; Baobing, F.; Guiai, J.; Zhonghua, S.; Ju, L.; Shaoqing, T.; Jianlong, W.; Peisong, H.; Xiangjin, W.
Editing of rice isoamylase gene ISA1 provides insights into its function in starch formation
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2019
Oryza sativa Japonica Group
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brenda