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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
?
-
-
-
?
amylopectin + H2O
?
-
-
-
?
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
?
-
-
-
?
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
?
-
-
-
?
maize starch + H2O
?
-
-
-
?
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 activty
-
-
?
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
-
-
?
potato starch, boiled + H2O
?
little activty
-
-
?
pullulan + H2O

?
-
-
-
?
pullulan + H2O
?
little activity
-
-
?
pullulan + H2O
?
little activty
-
-
?
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
-
-
?
additional information
?
-
pullulan is a poor substrate
-
-
?
additional information
?
-
pullulan is a poor substrate
-
-
?
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: dextran, amylose
-
-
?
additional information
?
-
-
no substrate: dextran, amylose
-
-
?
additional information
?
-
-
no activity with amylose
-
-
?
additional information
?
-
-
no activity with pullulan
-
-
?
additional information
?
-
-
no activity towards pullulan
-
-
?
additional information
?
-
-
ISA1 activity plays a critical role in the stochastic process in starch synthesis in rice endosperm
-
-
?
additional information
?
-
-
recombinant isoamylase 3 does not readily hydrolyze red pullulan and amylose
-
-
?
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
?
-
involved in starch synthesis
-
-
?
additional information
?
-
involved in starch synthesis
-
-
?
additional information
?
-
-
involved in starch synthesis
-
-
?
additional information
?
-
-
involved in synthesis of reserve and leaf starches
-
-
?
additional information
?
-
-
isoamylase1 is directly involved in the synthesis of amylopectin
-
-
?
additional information
?
-
-
Zea mays subunit ISA 2 alone is catalytically inactive
-
-
?
additional information
?
-
Zea mays subunit ISA 2 alone is catalytically inactive
-
-
?
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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
the enzyme belongs to the glycosyl hydrolase family 13 GH13, and harbors a carbohydrate-binding module family 48 (CBM48) domain
evolution
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
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
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
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
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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101155
1 * 100000, SDS-PAGE, 1 * 101155, sequence calculation
141000
-
isoamylase II, gel filtration
150000
x * 150000, ISA1 and ISA2 as stable dimer, SDS-PAGE
158000
ISA2 dimer, gel filtration and analytical ultracentrifugation
180000
subunit ISA1, crystal structure analysis and SDS-PAGE
300000
wild type endosperm contains three high molecular mass ISA complexes resolved by gel filtration and native-PAGE. Two complexes of approximately 400 kDa contain both isoform ISA1 and isoform ISA2, and an approximately 300 kDa complex contains isoform ISA1 but not isoform ISA2
340000
-
native enzyme, gel filtration, TSKgel G3000SWxl
370000
gel permeation chromatography
400000
wild type endosperm contains three high molecular mass ISA complexes resolved by gel filtration and native-PAGE. Two complexes of approximately 400 kDa contain both isoform ISA1 and isoform ISA2, and an approximately 300 kDa complex contains isoform ISA1 but not isoform ISA2
420000
O80403
SDS-PAGE, homooligomer, five OsISA1
450000
native ISA1-ISA2 complex, gel filtration
46000
-
2 * 46000, sedimentation equilibrium
490000
-
native enzyme, gel filtration, TSKgel G4000SWxl
50000
-
2 subunits, not linked covalently
510000
O80403
SDS-PAGE, heterooligomer, hetero-hexamer composed of five OsISA1 and one OsISA2
52000
-
2 * 52000, gel filtration
60000
1 * 60000, SDS-PAGE
74000
-
x * 74100, deduced from gene sequence, x * 74000, SDS-PAGE
74100
-
x * 74100, deduced from gene sequence, x * 74000, SDS-PAGE
750000
recombinant ISA1-ISA2 complex, gel filtration
80810
-
SB-15, DNA sequence analysis
88000
-
calculated by comparison with standard proteins
90000
-
undegraded polypeptide chain
90500
x * 90500, about, sequence calculation
65000

-
SDS-PAGE, gel filtration
65000
-
gel filtration, 0.5-m Bio-Gel A
75000

-
SU1
75000
x * 75000, SDS-PAGE
79000

-
maize gene su1 recombinant polypeptide, expressed in E. coli
79000
-
x * 79000, SDS-PAGE
80000

-
-
80000
gel permeation chromatography
80000
x * 80000, about, SDS-PAGE
83000

-
-
83000
-
SDS-PAGE, co-purified with a second minor band of 75000, probably C-terminal truncation of the native enzyme in vivo or during purification
83000
-
x * 83000, SDS-PAGE
83000
-
1 * 83000 + 1 * 95000
830000

-
SDS-PAGE
830000
O80403
homooligomer OsISA1 5 * 830000 and heterooligomer OsISA1-OsISA2 6 * 85000, HPLC gel filtration
85000

O80403
homooligomer OsISA1 5 * 830000 and heterooligomer OsISA1-OsISA2 6 * 85000, HPLC gel filtration
85000
1 * 85000, ISA1 monomer, SDS-PAGE
85000
2 * 85000, ISA1 dimer, SDS-PAGE
86000 - 94000

-
-
86000 - 94000
-
86000, undegraded polypeptide chain, SDS-PAGE
86000 - 94000
-
SB-15, gel filtration, SDS-PAGE
87000

heterotetramer with PvISA1, 2 * 87000 PyISA1 and 2 * 93000 PvISA2, SDS-PAGE
87000
heterotetramer with PvISA2, 2 * 87000 PvISA1 and 2 * 93000 PvISA2, SDS-PAGE
93000

heterotetramer with PvISA1, 2 * 87000 PyISA1 and 2 * 93000 PvISA2, SDS-PAGE
93000
heterotetramer with PvISA2, 2 * 87000 PvISA1 and 2 * 93000 PvISA2, SDS-PAGE
93000
2 * 93000, subunit ISA1, crystal structure analysis and SDS-PAGE
94000

-
-
94000
-
sedimentation equilibrium
94000
-
native enzyme, centrifugation analysis
95000

-
gel electrophoresis, low speed sedimentation
95000
x * 95000, SDS-PAGE
95000
-
1 * 83000 + 1 * 95000
additional information

comparable mobility in the native PAGE of native enzyme recombinnat enzyme complex
additional information
comparable mobility in the native PAGE of native enzyme recombinnat enzyme complex
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D367A
site-directed mutagenesis of the catalytic nucleophile Asp-367 in ISA1, the mutation abolishes the catalytic activity of the enzyme complex
G608A
-
the kcat/Km values and the specific activity of the mutant are decreased as compared to the wild type enzyme
G608K
-
the kcat/Km values and the specific activity of the mutant are decreased as compared to the wild type enzyme
G608V
-
the kcat/Km values of the mutant are promoted by 49% and the specific activity increases by 33% as compared to the wild type enzyme
N513A
-
the kcat/Km values of the mutant are slightly decreased and the specific activity is decreased as compared to the wild type enzyme
N513K
-
the kcat/Km values and the specific activity of the mutant are decreased as compared to the wild type enzyme
N513V
-
the kcat/Km values and the specific activity of the mutant are strongly decreased as compared to the wild type enzyme
R505A
-
the kcat/Km values of the mutant are promoted and the specific activity is decreased as compared to the wild type enzyme
R505E
-
the acidic stability is enhanced and the specific activity of the mutant is increased by 13% compared to the wild type enzyme
R505P
-
the thermal stability of the mutant is enhanced compared to the wild type enzyme
G608A
-
the kcat/Km values and the specific activity of the mutant are decreased as compared to the wild type enzyme
-
G608V
-
the kcat/Km values of the mutant are promoted by 49% and the specific activity increases by 33% as compared to the wild type enzyme
-
R505A
-
the kcat/Km values of the mutant are promoted and the specific activity is decreased as compared to the wild type enzyme
-
R505E
-
the acidic stability is enhanced and the specific activity of the mutant is increased by 13% compared to the wild type enzyme
-
R505P
-
the thermal stability of the mutant is enhanced compared to the wild type enzyme
-
additional information

construction of a single mutant line isa2-2 by T-DNA insertion mutagenesis. The isa1-1 isa2-2 double mutant line is obtained by a cross between the two corresponding single mutants and screening of the progeny by PCR amplification of genomic DNA using a T-DNA end primer and gene-specific primers. The phenotype of the isa1-1 isa2-2 double mutant is complemented but the ZmISA1 activity
additional information
construction of a single mutant line isa2-2 by T-DNA insertion mutagenesis. The isa1-1 isa2-2 double mutant line is obtained by a cross between the two corresponding single mutants and screening of the progeny by PCR amplification of genomic DNA using a T-DNA end primer and gene-specific primers. The phenotype of the isa1-1 isa2-2 double mutant is complemented but the ZmISA1 activity
additional information
construction of single mutant line isa1-1 by T-DNA insertion mutagenesis. The isa1-1 isa2-2 double mutant line is obtained by a cross between the two corresponding single mutants and screening of the progeny by PCR amplification of genomic DNA using a T-DNA end primer and gene-specific primers. The phenotype of the isa1-1 isa2-2 double mutant is complemented but the ZmISA1 activity, Zea mays ISA1 subunit is expressed via transfection with Agrobacterium tumefaciens strain GV3101 in Arabidopsis thaliana lacking endogenous ISA1 or lacking both native ISA1 and ISA2. The maize protein functions in Arabidopsis leaves to support nearly normal starch metabolism in the absence of any native ISA1 or ISA2
additional information
construction of single mutant line isa1-1 by T-DNA insertion mutagenesis. The isa1-1 isa2-2 double mutant line is obtained by a cross between the two corresponding single mutants and screening of the progeny by PCR amplification of genomic DNA using a T-DNA end primer and gene-specific primers. The phenotype of the isa1-1 isa2-2 double mutant is complemented but the ZmISA1 activity, Zea mays ISA1 subunit is expressed via transfection with Agrobacterium tumefaciens strain GV3101 in Arabidopsis thaliana lacking endogenous ISA1 or lacking both native ISA1 and ISA2. The maize protein functions in Arabidopsis leaves to support nearly normal starch metabolism in the absence of any native ISA1 or ISA2
additional information
-
construction of single mutant line isa1-1 by T-DNA insertion mutagenesis. The isa1-1 isa2-2 double mutant line is obtained by a cross between the two corresponding single mutants and screening of the progeny by PCR amplification of genomic DNA using a T-DNA end primer and gene-specific primers. The phenotype of the isa1-1 isa2-2 double mutant is complemented but the ZmISA1 activity, Zea mays ISA1 subunit is expressed via transfection with Agrobacterium tumefaciens strain GV3101 in Arabidopsis thaliana lacking endogenous ISA1 or lacking both native ISA1 and ISA2. The maize protein functions in Arabidopsis leaves to support nearly normal starch metabolism in the absence of any native ISA1 or ISA2
-
additional information
-
construction of a single mutant line isa2-2 by T-DNA insertion mutagenesis. The isa1-1 isa2-2 double mutant line is obtained by a cross between the two corresponding single mutants and screening of the progeny by PCR amplification of genomic DNA using a T-DNA end primer and gene-specific primers. The phenotype of the isa1-1 isa2-2 double mutant is complemented but the ZmISA1 activity
-
additional information
-
mutant sta8, about 35% residual enzymic activity, loss of two out of three activity bands in zymogram gels, loss of about 50% of mass of the multimeric complex
additional information
functional complementation of sta8 mutant strains BafV13 and BafO6 with ISA2 or ISA2-HA, overview
additional information
functional complementation of sta8 mutant strains BafV13 and BafO6 with ISA2 or ISA2-HA, overview
additional information
-
functional complementation of sta8 mutant strains BafV13 and BafO6 with ISA2 or ISA2-HA, overview
additional information
-
functional complementation of sta8 mutant strains BafV13 and BafO6 with ISA2 or ISA2-HA, overview
-
additional information
-
Cassava starch is debranched by treatment with isoamylase and pullulanase and the yield of resistant starch type III, method optimization with respect to starch solids concentration, incubation time, and enzyme concentration using central composite rotatable design
additional information
-
mutations in the N-terminal region result in a sharp increase in alpha-1,4-transferase activity and a reduced level of alpha-1,6-glucosidase activity, overview
additional information
-
transgenic plants expressing antisense RNA for Stisa1 or Stisa2, accumulate small amounts of soluble glucan and large numbers of tiny starch granules
additional information
-
generation of mutant isa2-339
additional information
generation of mutant isa2-339
additional information
-
generation of mutant su1-4582
additional information
generation of mutant su1-4582
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cloned to an expression vector with a T7lac promoter. Both wild-type and His-tagged isoamylases are expressed in Escherichia coli
-
cloning of cDNAs of different isoforms, Psisa1-Psisa3, DNA and amino acid sequence determination and analysis, phylogenetic analysis and sequence comparisons, overview
-
coexpression of wild-type His-tagged ISA1 and ISA2, and of mutant D367A ISA1 with wild-type ISA2, in Escherichia coli strain BL21(DE3)
DNA and amino acid sequence determination and analysis, phylogenetic tree
DNA and amino acid sequence determination and analysis, sequence comparisons
expressed in Escherichia coli
-
expressed in Escherichia coli BL21 cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) Star cells
-
expressed in Escherichia coli strain MDS42
-
expressed in Saccharomyces cerevisiae
expression in Escherichia coli
-
expression of in Escherichia coli
-
expression of OsISA2 in Escherichia coli
O80403
expression of OsISA2in Escherichia coli
O80403
expression of wild-type and mutant enzymes in Escherichia coli, sequence comparison
-
gene ArDBE, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
gene isa1, single expression of C-terminally His8-tagged subunit in Escherichia coli strain BL21(DE3), co-expression of untagged ISA1 subunit with C-terminally His8-tagged subunit ISA2 in Escherichia coli
gene isa2, single expression of C-terminally His8-tagged subunit in Escherichia coli strain BL21(DE3) or co-expression with untagged ISA1 subunit in Escherichia coli
gene su-1, single expression of C-terminally His8-tagged subunit ISA1 in Escherichia coli strain BL21(DE3), co-expression of untagged ISA1 subunit with C-terminally His8-tagged subunit ISA2 in Escherichia coli. Zea mays ISA1 subunit is heterologously expressed in Arabidopsis thaliana lacking endogenous ISA1 or lacking both native ISA1 and ISA2 via transfection with Agrobacterium tumefaciens strain GV3101. The maize protein functions in Arabidopsis leaves to support nearly normal starch metabolism in the absence of any native ISA1 or ISA2
gene su1, expressed in Escherichia coli, pAR4
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gene treX, component of a treXYZ operon, DNA and amino acid sequence determination and analysis, sequence comparison, genetic organization in the treXYZ operon, overview
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iam gene cloned and expressed in Escherichia coli JM101, pMON17481, production of a nonsecreted signal peptide-less isoamylase
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into Agrobacterium tumefaciens strain GV310, GFP/GUS promoter fusion constructs for AtISA1, AtISA2, AtISA3 into Arabidopsis thaliana using the floral dip method
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introduction of ISA1 gene from Triticum aestivum (TaISA1 from the D genome donor Aegilops tauschii) into a rice sugary-1 mutant line EM914 in which starch is completely replaced by phytoglycogen in the endosperm
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isoamylase gene is a single copy in rice genome, located on chromsome 8
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plasmid pIAM275, pUC9 carrying iam gene, Escherichia coli, recominant plasmid does not direct the synthesis of isoamylase in Escherichia coli , sequenced
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recombinant GST-ISA2 fusion protein is expressed in Escherichia coli Rosetta DE3-pLysS cells
the STA7 locus encodes ISA1, recombinant expression of His-tagged subunit ISA1 in Escherichia coli strain BL21(DE3)
the STA8 locus encodes ISA2, recombinant expression of HA-tagged ISA2 in strain BafV13 and BafO6