Information on EC 3.2.1.68 - isoamylase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
3.2.1.68
-
RECOMMENDED NAME
GeneOntology No.
isoamylase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen, amylopectin and their beta-limit dextrins
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
hydrolysis of O-glycosyl bond
-
-
hydrolysis of O-glycosyl bond
-
hydrolysis of O-glycosyl bond
-
-
hydrolysis of O-glycosyl bond
;
hydrolysis of O-glycosyl bond
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
starch biosynthesis
-
-
starch degradation II
-
-
trehalose biosynthesis V
-
-
metabolism of disaccharids
-
-
SYSTEMATIC NAME
IUBMB Comments
glycogen 6-alpha-D-glucanohydrolase
Also readily hydrolyses amylopectin. Differs from EC 3.2.1.41 (pullulanase) and EC 3.2.1.142 (limit dextrinase) by its inability to hydrolyse pullulan, and by limited action on alpha-limit dextrins. Maltose is the smallest sugar it can release from an alpha-(1->6)-linkage.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
alkaline isoamylase
-
alkaliphilic Bacillus sp KSM-3309, isolated from soil
alkaline isoamylase
Bacillus sp. KSM-K16
-
alkaliphilic Bacillus sp KSM-3309, isolated from soil
-
alpha 1,6-glucan hydrolase
-
-
-
alpha-1,6-glucosidase
-
-
AtISA1
Arabidopsis thaliana Col-0
-
-
AtISA1/AtISA2 isoamylase
-
-
AtISA2
Arabidopsis thaliana Col-0
-
-
bacterial isoamylase
-
-
bacterial isoamylase
Bacillus sp. KSM-K16
-
-
-
bacterial isoamylase
-
-
bacterial isoamylase
Pseudomonas amyloderamosa JD210, Pseudomonas amyloderamosa SMP1
-
-
-
CrISA1
Chlamydomonas reinhardtii 330
-
-
Cythophaga isoamylase
-
-
debranching enzyme
-
-
-
-
debranching enzyme
-
glycogen 6-glucanohydrolase
-
-
glycogen 6-glucanohydrolase
-
-
-
glycogen 6-glucanohydrolase
-
-
glycogen 6-glucanohydrolase
-
-
glycogen 6-glucanohydrolase
-
-
glycogen 6-glucanohydrolase
Pseudomonas amyloderamosa SMP1, Pseudomonas amyloderamosa WU7211-2
-
-
-
glycogen alpha-1,6-glucanohydrolase
-
-
glycogen alpha-1,6-glucanohydrolase
-
glycogen alpha-1,6-glucanohydrolase
-
glycogen alpha-1,6-glucanohydrolase
-
-
glycogen alpha-1,6-glucanohydrolase
-
-
glycogen debranching enzyme
-
-
glycogen debranching enzyme
-
-
-
glycogen-6-glucanogydrolase
-
glycogen-6-glucanogydrolase
Bacillus sp. CICIM 304
-
-
glycogen-6-glucanohydrolase
-
-
glycogen-6-glucanohydrolase
-
glycogen-6-glucanohydrolase
Pseudomonas amyloderamosa SB-15
-
-
glycogen-debranching enzyme
-
-
IAM
Bacillus sp. CICIM 304
-
-
ISA1
Arabidopsis thaliana Col-0
-
-
ISA1
Chlamydomonas reinhardtii 330
-
-
ISA2
Arabidopsis thaliana Col-0
-
-
ISA2
Chlamydomonas reinhardtii 330
-
-
ISA2
-
-
ISA3
-
-
isoamylase
-
-
isoamylase
-
isoamylase 1
Chlamydomonas reinhardtii 330
-
-
isoamylase 2
Chlamydomonas reinhardtii 330
-
-
isoamylase 3
-
-
isoamylase II
-
-
isoamylase-type debranching enzyme
-
isoamylase-type starch debranching enzyme 1
-
isoamylase-type starch debranching enzyme 1
Arabidopsis thaliana Col-0
-
-
isoamylase-type starch debranching enzyme 1
-
isoamylase-type starch debranching enzyme 2
-
isoamylase-type starch debranching enzyme 2
Arabidopsis thaliana Col-0
-
-
isoamylase-type starch debranching enzyme 2
-
-
isoamylase-type starch-debranching enzyme
-
isoamylase1
-
-
isoamylase1
-
-
maize Sugary-1 isoamylase
-
-
pancreatic isoamylase isoA
-
-
plant isoamylase
-
-
-
potato isoamylase
-
-
Pseudomonas isoamylase
-
-
rice isoamylase
-
-
starch debranching enzyme
-
starch debranching enzyme
Chlamydomonas reinhardtii 330
-
-
SU1 isoamylase
-
-
TreX
-
gene name
TreX
-
gene name
-
TreX
-
trehalose gene cluster has isoamylase activities
yeast isoamylase
-
-
-
ZmISA2
-
-
CAS REGISTRY NUMBER
COMMENTARY
9067-73-6
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ecotype Columbia
-
-
Manually annotated by BRENDA team
gene isa1
SwissProt
Manually annotated by BRENDA team
gene isa2
SwissProt
Manually annotated by BRENDA team
isozyme ISA1; genes isa1 and isa2
SwissProt
Manually annotated by BRENDA team
isozyme ISA2; genes isa1 and isa2
SwissProt
Manually annotated by BRENDA team
Arabidopsis thaliana Col-0
gene isa1
SwissProt
Manually annotated by BRENDA team
Arabidopsis thaliana Col-0
gene isa2
SwissProt
Manually annotated by BRENDA team
gene treX, component of a treXYZ operon
-
-
Manually annotated by BRENDA team
gene treX, component of a treXYZ operon
-
-
Manually annotated by BRENDA team
isolated by screening a soil sample collected from a hot spring of Tengchong volcano in Yunnan, China
UniProt
Manually annotated by BRENDA team
KSM.3309, gram-positive, isolated from soil
-
-
Manually annotated by BRENDA team
KSM.3309, gram-positive, isolated from soil; KSM-K16
-
-
Manually annotated by BRENDA team
Bacillus sp. CICIM 304
isolated by screening a soil sample collected from a hot spring of Tengchong volcano in Yunnan, China
UniProt
Manually annotated by BRENDA team
Bacillus sp. KSM-K16
KSM-K16
-
-
Manually annotated by BRENDA team
Chlamydomonas reinhardtii 330
-
UniProt
Manually annotated by BRENDA team
Dickeya chrysanthemi PY35
PY35
-
-
Manually annotated by BRENDA team
yeast, strain IGC 4051
-
-
Manually annotated by BRENDA team
cv. Nanicao
-
-
Manually annotated by BRENDA team
cultivar Kinmaze
-
-
Manually annotated by BRENDA team
cultivar Nipponbare
-
-
Manually annotated by BRENDA team
L. cv. Fujikari
-
-
Manually annotated by BRENDA team
L. cv. Nipponbare
-
-
Manually annotated by BRENDA team
L. cv. Nipponbare
SwissProt
Manually annotated by BRENDA team
mutants sugary and shrunken, contain reduced activities of isoamylase1
-
-
Manually annotated by BRENDA team
kidney bean
Swissprot
Manually annotated by BRENDA team
different isoforms Psisa1-Psisa3
-
-
Manually annotated by BRENDA team
gram-negative soil bacterium, strain SB-15
-
-
Manually annotated by BRENDA team
SMP1; strain JD210, isoamylase-hyperproducing mutant
-
-
Manually annotated by BRENDA team
strain KlC, revertant strain of Kl
-
-
Manually annotated by BRENDA team
strain MI-414, isomylase-hyperproducing mutant of SB-15
-
-
Manually annotated by BRENDA team
strain WU-5315, isoamylase hyperproducing mutant derived from JD-210
-
-
Manually annotated by BRENDA team
strain WU7211-2
-
-
Manually annotated by BRENDA team
Pseudomonas amyloderamosa JD210
strain JD210, isoamylase-hyperproducing mutant
-
-
Manually annotated by BRENDA team
Pseudomonas amyloderamosa MI-414
strain MI-414, isomylase-hyperproducing mutant of SB-15
-
-
Manually annotated by BRENDA team
Pseudomonas amyloderamosa SB-15
-
UniProt
Manually annotated by BRENDA team
Pseudomonas amyloderamosa SMP1
SMP1
-
-
Manually annotated by BRENDA team
Pseudomonas amyloderamosa WU-5315
strain WU-5315, isoamylase hyperproducing mutant derived from JD-210
-
-
Manually annotated by BRENDA team
Pseudomonas amyloderamosa WU7211-2
strain WU7211-2
-
-
Manually annotated by BRENDA team
isozyme Stisa1
SwissProt
Manually annotated by BRENDA team
isozyme Stisa2
SwissProt
Manually annotated by BRENDA team
multimeric complex of Stisa1 and Stisa2
-
-
Manually annotated by BRENDA team
potato, L. cul. var. 'Danshaku'
-
-
Manually annotated by BRENDA team
gene isa2
-
-
Manually annotated by BRENDA team
gene su-1
UniProt
Manually annotated by BRENDA team
isoform ISA2
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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; 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 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
Bacillus sp. CICIM 304
-
the enzyme harbors a carbohydrate-binding module family 48 (CBM48) domain
-
evolution
Chlamydomonas reinhardtii 330
-
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; 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
-
malfunction
-
both overexpression and loss of function of isoamylase 3 in the endosperm generated pleomorphic amyloplasts and starch granules
malfunction
mutants of the STA8 locus accumulate both phytoglycogen and a reduced amount of high amylose starch; 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; 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
loss of isozyme ISA1 or ISA2 causes phytoglycogen accumulation
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 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
-
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
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; 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
isoamylase catalyzes hydrolysis of alpha-D-(1,6)-glucosidic branch linkages in amylopectin and glycogen to release amylose and linear maltooligosaccharides
physiological function
the ISA1 class of DBE is the one primarily associated with amylopectin synthesis
physiological function
Bacillus sp. CICIM 304
-
isoamylase catalyzes hydrolysis of alpha-D-(1,6)-glucosidic branch linkages in amylopectin and glycogen to release amylose and linear maltooligosaccharides
-
physiological function
Chlamydomonas reinhardtii 330
-
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; 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
-
malfunction
Chlamydomonas reinhardtii 330
-
mutants of the STA8 locus accumulate both phytoglycogen and a reduced amount of high amylose starch; mutation of the STA7 locus leads to a very severe reduction of starch content and its replacement by a water-soluble polysaccharide phytoglycogen
-
additional information
subunit ISA2 interacts physically with ISA1, presence of both homomeric ISA1 and heteromeric ISA1-ISA2 complexes in vivo; 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; 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
-
Zea mays subunit ISA1 is active by itself and does not require subunit ISA2 for activity, subunit ISA 2 alone is catalytically inactive; 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
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
Arabidopsis thaliana Col-0
-
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; 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
Chlamydomonas reinhardtii 330
-
subunit ISA2 interacts physically with ISA1, presence of both homomeric ISA1 and heteromeric ISA1-ISA2 complexes in vivo; 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
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-D-glucan + H2O
?
show the reaction diagram
-
cleavage of alpha-D-glucosidic linkages of certain branched alpha-D-glucans
-
-
?
alpha-limit dextrin + H2O
linear maltooligosaccharides
show the reaction diagram
-
-
-
?
alpha-limit dextrin + H2O
linear maltooligosaccharides
show the reaction diagram
Pseudomonas amyloderamosa, Pseudomonas amyloderamosa SB-15
-
-
?
amylomaize + H2O
?
show the reaction diagram
-
debranching
-
-
?
amylopectin + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
-
?
amylopectin + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
-
-
r
amylopectin + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
waxy maize amylopectin, potato amylopectin, amylopectin beta-dextrin
-
?
amylopectin + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
specific cleavage of alpha 1,6-glucosidic inter-chain linkages producing essentially linear chains
-
-
amylopectin + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
or the beta-limit dextrins, cleaves the branching points completely in vitro
-
r
amylopectin + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
or the beta-limit dextrins, cleaves the branching points completely in vitro
-
-
amylopectin + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
or the beta-limit dextrins, cleaves the branching points completely in vitro
-
?
amylopectin + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
or the beta-limit dextrins, cleaves the branching points completely in vitro
-
-
amylopectin + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
or the beta-limit dextrins, cleaves the branching points completely in vitro
-
?
amylopectin + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
or the beta-limit dextrins, cleaves the branching points completely in vitro
-
?
amylopectin + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
or the beta-limit dextrins, cleaves the branching points completely in vitro
-
?
amylopectin + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
or the beta-limit dextrins, cleaves the branching points completely in vitro
-
?
amylopectin + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
or the beta-limit dextrins, cleaves the branching points completely in vitro
-
?
amylopectin + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
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
show the reaction diagram
Pseudomonas amyloderamosa SMP1
-
or the beta-limit dextrins, cleaves the branching points completely in vitro
-
-
amylopectin + H2O
maltose + maltooligosaccharides
show the reaction diagram
Pseudomonas amyloderamosa SB-15
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
?
show the reaction diagram
-
-
-
-
?
amylopectin + H2O
?
show the reaction diagram
-
-
-
-
?
amylopectin + H2O
?
show the reaction diagram
-
-
-
?
amylopectin + H2O
?
show the reaction diagram
-
-
-
?
amylopectin + H2O
?
show the reaction diagram
-
-
-
?
amylopectin + H2O
?
show the reaction diagram
-
-
-
?
amylopectin + H2O
?
show the reaction diagram
-
-
-
-
?
amylopectin + H2O
?
show the reaction diagram
-
-
hydrolysis of alpha-1,6-linkages
-
?
amylopectin + H2O
?
show the reaction diagram
Chlamydomonas reinhardtii 330
-
-
-
?
amylopectin + H2O
?
show the reaction diagram
Arabidopsis thaliana Col-0
-
-
-
?
amylopectin + H2O
?
show the reaction diagram
Dickeya chrysanthemi PY35
-
-
hydrolysis of alpha-1,6-linkages
-
?
amylopectin + H2O
linear maltooligosaccharides
show the reaction diagram
-
-
-
?
amylopectin + H2O
linear maltooligosaccharides
show the reaction diagram
-
-
-
?
amylopectin + H2O
linear maltooligosaccharides
show the reaction diagram
-
-
?
amylopectin + H2O
amylose + linear maltooligosaccharides
show the reaction diagram
Bacillus sp., Bacillus sp. CICIM 304
-
-
?
amylopectin phi-dextrin + H2O
maltotetraose
show the reaction diagram
-
substrate on which all 3 types of debranching enzymes act
-
?
amylose + H2O
?
show the reaction diagram
-
short chain
-
-
?
amylose-extender amylopectin + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
-
?
Arabidopsis starch + H2O
?
show the reaction diagram
-
-
-
?
Arabidopsis starch + H2O
?
show the reaction diagram
Arabidopsis thaliana Col-0
-
-
-
?
beta limit dextrin + H2O
linear maltooligosaccharides
show the reaction diagram
-
-
?
beta limit dextrin + H2O
maltose + maltooligosaccharides
show the reaction diagram
from maize
-
?
beta-limit dextrin + H2O
?
show the reaction diagram
-
-
-
-
?
beta-limit dextrin + H2O
?
show the reaction diagram
-
-
-
?
beta-limit dextrin + H2O
?
show the reaction diagram
-
-
-
?
beta-limit dextrin + H2O
?
show the reaction diagram
-
-
-
?
beta-limit dextrin + H2O
?
show the reaction diagram
-
-
-
-
?
beta-limit dextrin + H2O
?
show the reaction diagram
best substrate
-
-
?
beta-limit dextrin + H2O
?
show the reaction diagram
medium activity
-
-
?
beta-limit dextrin + H2O
?
show the reaction diagram
Chlamydomonas reinhardtii 330
-
-
-
?
beta-limit dextrin + H2O
?
show the reaction diagram
Arabidopsis thaliana Col-0
-
-
-
?
beta-limit dextrin + H2O
maltose + ?
show the reaction diagram
-
-
-
?
beta-limit dextrin + H2O
linear maltooligosaccharides
show the reaction diagram
-
-
-
?
beta-limit dextrin + H2O
linear maltooligosaccharides
show the reaction diagram
Pseudomonas amyloderamosa, Pseudomonas amyloderamosa SB-15
-
-
?
branched chain oligosaccharides + H2O
maltotriose + higher maltosaccharides
show the reaction diagram
-
-
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
?
corn amylopectin + H2O
?
show the reaction diagram
Pseudomonas amyloderamosa, Pseudomonas amyloderamosa WU7211-2
-
-
-
-
?
D-glucose + H2O
?
show the reaction diagram
-
59% of the activity with dextrin as substrate
-
-
?
dextrin + H2O
?
show the reaction diagram
-
enzyme activity 100%
-
-
?
di-O-alpha-maltosyl-beta-cyclodextrin + H2O
maltose + beta-cyclodextrin
show the reaction diagram
-
-
-
r
glycogen + H2O
?
show the reaction diagram
-
-
-
?
glycogen + H2O
?
show the reaction diagram
-
-
-
?
glycogen + H2O
?
show the reaction diagram
-
80% activity compared to amylopectin
-
-
?
glycogen + H2O
?
show the reaction diagram
Chlamydomonas reinhardtii 330
-
-
-
?
glycogen + H2O
?
show the reaction diagram
Bacillus sp. CICIM 304
-
-
-
?
glycogen + H2O
?
show the reaction diagram
Dickeya chrysanthemi PY35
-
80% activity compared to amylopectin
-
-
?
glycogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
-
-
?
glycogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
-
-
r
glycogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
-
-
?
glycogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
-
-
?
glycogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
-
?
glycogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
-
?
glycogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
cleaves the branching points completely in vitro
-
r
glycogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
cleaves the branching points completely in vitro
-
?
glycogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
cleaves the branching points completely in vitro
-
?
glycogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
cleaves the branching points completely in vitro
-
?
glycogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
cleaves the branching points completely in vitro
-
?
glycogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
cleaves the branching points completely in vitro
-
?
glycogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
cleaves the branching points completely in vitro
-
?
glycogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
cleaves the branching points completely in vitro
-
?
glycogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
cleaves the branching points completely in vitro
-
?
glycogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
cleaves the branching points completely in vitro
-
?
glycogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
cleaves the branching points completely in vitro
-
?
glycogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
oyster glycogen, glycogen beta-dextrin, rabbit liver glycogen
-
?
glycogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
or the beta-limit dextrins
-
r
glycogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
or the beta-limit dextrins
-
?
glycogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
or the beta-limit dextrins
-
?
glycogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
or the beta-limit dextrins
-
?
glycogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
or the beta-limit dextrins
-
?
glycogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
or the beta-limit dextrins
-
?
glycogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
or the beta-limit dextrins
-
?
glycogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
or the beta-limit dextrins
-
?
glycogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
or the beta-limit dextrins
-
?
glycogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
or the beta-limit dextrins
-
?
glycogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
or the beta-limit dextrins
-
?
glycogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
Pseudomonas amyloderamosa SMP1
-
cleaves the branching points completely in vitro, or the beta-limit dextrins
-
?
glycogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
Pseudomonas amyloderamosa SB-15
-
-
?
glycogen + H2O
linear maltooligosaccharides
show the reaction diagram
-
-
-
?
glycogen + H2O
linear maltooligosaccharides
show the reaction diagram
-
-
?
glycogen + H2O
maltodextrin
show the reaction diagram
-
-
-
?
maize beta-limit dextrin + H2O
?
show the reaction diagram
-
-
-
?
maize starch + H2O
?
show the reaction diagram
-
-
-
?
maize starch + H2O
?
show the reaction diagram
-
-
-
?
maize starch + H2O
?
show the reaction diagram
-
-
-
-
?
maltodextrin + H2O
?
show the reaction diagram
Bacillus sp., Bacillus sp. CICIM 304
-
-
-
?
maltopentaose + H2O
?
show the reaction diagram
-
sugar immobilized on Sepharose 4B
-
-
?
maltose + H2O
?
show the reaction diagram
-
-
-
-
?
maltose + H2O
?
show the reaction diagram
-
iam gene induced by maltose
-
-
?
maltose + H2O
?
show the reaction diagram
-
iam gene induced by maltose
-
-
?
maltose + H2O
?
show the reaction diagram
Pseudomonas amyloderamosa JD210, Pseudomonas amyloderamosa SMP1
-
iam gene induced by maltose
-
-
?
maltose + H2O
?
show the reaction diagram
Pseudomonas amyloderamosa MI-414
-
iam gene induced by maltose
-
-
?
oyster glycogen + H2O
?
show the reaction diagram
-
-
-
?
oyster gylcogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
-
?
panose + H2O
D-glucose + maltose
show the reaction diagram
-
acts very slowly, small amounts of product formed after 24 h
-
?
phythoglycogen + H2O
?
show the reaction diagram
-
-
-
-
r
phythoglycogen + H2O
?
show the reaction diagram
-
-
-
-
r
phythoglycogen + H2O
?
show the reaction diagram
-
highly branched polysaccharide, complete hydrolysis of the alpha-1,6-glucosidic bonds
-
-
?
phytoglycogen + H2O
?
show the reaction diagram
-
-
-
?
phytoglycogen + H2O
?
show the reaction diagram
little activty
-
-
?
phytoglycogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
-
?
potato amylopectin + H2O
?
show the reaction diagram
-
-
-
?
potato starch, boiled + H2O
?
show the reaction diagram
best substrate
-
-
?
potato starch, boiled + H2O
?
show the reaction diagram
little activity
-
-
?
potato starch, boiled + H2O
?
show the reaction diagram
little activty
-
-
?
pullulan + H2O
?
show the reaction diagram
-
-
-
?
pullulan + H2O
?
show the reaction diagram
little activity
-
-
?
pullulan + H2O
?
show the reaction diagram
little activty
-
-
?
pullulan + H2O
linear maltooligosaccharides
show the reaction diagram
-
-
?
saccharose + H2O
?
show the reaction diagram
-
activity 67%
-
-
?
soluble starch + H2O
?
show the reaction diagram
Bacillus sp., Bacillus sp. CICIM 304
-
-
-
?
starch + H2O
?
show the reaction diagram
-
-
-
-
r
starch + H2O
?
show the reaction diagram
-
-
-
-
?
starch + H2O
?
show the reaction diagram
-
-
-
-
?
starch + H2O
?
show the reaction diagram
-
-
-
-
?
starch + H2O
?
show the reaction diagram
-
soluble starch, immobilized on Sepharose 4B
-
-
?
starch + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
hydrolysis of alpha-1,6-glycosidic linkages
-
-
?
starch + H2O
?
show the reaction diagram
specific hydrolysis of alpha-1,6-glucosidic linkages
detection of aminobenzamide-labeled maltooligosaccharide products, overview
-
?
starch + H2O
?
show the reaction diagram
Chlamydomonas reinhardtii 330
specific hydrolysis of alpha-1,6-glucosidic linkages
detection of aminobenzamide-labeled maltooligosaccharide products, overview
-
?
starch + H2O
linear maltooligosaccharides
show the reaction diagram
-
-
-
?
starch + H2O
maltose + maltooligosaccharides
show the reaction diagram
-
-
?
sticky rice starch + H2O
?
show the reaction diagram
-
-
-
?
maltotriose + H2O
?
show the reaction diagram
-
activity 28%
-
-
?
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
?
-
-
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
?
-
-
no activity with pullulan
-
-
-
additional information
?
-
involved in starch synthesis
-
-
-
additional information
?
-
-
involved in synthesis of reserve and leaf starches
-
-
-
additional information
?
-
-
no substrate: dextran, amylose
-
-
-
additional information
?
-
-
no substrate: pullulan, 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
?
-
-
ISA1 activity plays a critical role in the stochastic process in starch synthesis in rice endosperm
-
-
-
additional information
?
-
-
isoamylase1 is directly involved in the synthesis of amylopectin
-
-
-
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
?
-
-
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
?
-
-
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
?
-
-
isoform Psisa2 most likely does not have catalytic activity
-
-
-
additional information
?
-
-
no activity towards pullulan
-
-
-
additional information
?
-
no activity towards pullulan
-
-
-
additional information
?
-
-
recombinant isoamylase 3 does not readily hydrolyze red pullulan and amylose
-
-
-
additional information
?
-
-
isoamylase catalyzes the hydrolysis of alpha-1,6-glucosidic linkage specifically in amylopectin, glycogen and derived oligosaccharides
-
-
-
additional information
?
-
synthesis of amylopectin and phytoglycogen by associated and separated ISA1 and ISA2, respectively, overview
-
-
-
additional information
?
-
-
Zea mays subunit ISA 2 alone is catalytically inactive
-
-
-
additional information
?
-
pullulan is a poor substrate
-
-
-
additional information
?
-
pullulan is a poor substrate
-
-
-
additional information
?
-
Chlamydomonas reinhardtii 330
pullulan is a poor substrate
-
-
-
additional information
?
-
Bacillus sp. CICIM 304
pullulan is a poor substrate
-
-
-
additional information
?
-
Pseudomonas amyloderamosa WU7211-2
-
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
?
-
Pseudomonas amyloderamosa SB-15
no activity towards pullulan
-
-
-
additional information
?
-
Dickeya chrysanthemi PY35
-
no substrate: dextran, amylose
-
-
-
additional information
?
-
-
isoamylase catalyzes the hydrolysis of alpha-1,6-glucosidic linkage specifically in amylopectin, glycogen and derived oligosaccharides
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
amylopectin + H2O
?
show the reaction diagram
O04196, Q8L735
-
-
-
?
amylopectin + H2O
?
show the reaction diagram
-
-
-
-
?
amylopectin + H2O
amylose + linear maltooligosaccharides
show the reaction diagram
Bacillus sp., Bacillus sp. CICIM 304
L0C9D3
-
-
?
amylopectin + H2O
?
show the reaction diagram
Arabidopsis thaliana Col-0
O04196, Q8L735
-
-
-
?
Arabidopsis starch + H2O
?
show the reaction diagram
O04196, Q8L735
-
-
-
?
Arabidopsis starch + H2O
?
show the reaction diagram
Arabidopsis thaliana Col-0
O04196, Q8L735
-
-
-
?
beta-limit dextrin + H2O
?
show the reaction diagram
O04196, Q8L735
-
-
-
?
beta-limit dextrin + H2O
?
show the reaction diagram
Arabidopsis thaliana Col-0
O04196, Q8L735
-
-
-
?
glycogen + H2O
maltose + maltooligosaccharides
show the reaction diagram
Q84UE6
-
-
?
glycogen + H2O
maltodextrin
show the reaction diagram
-
-
-
?
starch + H2O
?
show the reaction diagram
-
-
-
-
r
starch + H2O
?
show the reaction diagram
-
-
-
-
?
starch + H2O
?
show the reaction diagram
-
-
-
-
?
starch + H2O
?
show the reaction diagram
A0A0A8IC08
hydrolysis of alpha-1,6-glycosidic linkages
-
-
?
maize starch + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
Q84YG5, Q84YG6, Q84YG7
involved in starch synthesis
-
-
-
additional information
?
-
-
involved in synthesis of reserve and leaf starches
-
-
-
additional information
?
-
O04196, Q8L735, Q9M0S5
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
?
-
-
ISA1 activity plays a critical role in the stochastic process in starch synthesis in rice endosperm
-
-
-
additional information
?
-
-
isoamylase1 is directly involved in the synthesis of amylopectin
-
-
-
additional information
?
-
O04196, Q8L735, Q9M0S5
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
?
-
-
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
?
-
-
isoamylase catalyzes the hydrolysis of alpha-1,6-glucosidic linkage specifically in amylopectin, glycogen and derived oligosaccharides
-
-
-
additional information
?
-
O04196, Q8L735
synthesis of amylopectin and phytoglycogen by associated and separated ISA1 and ISA2, respectively, overview
-
-
-
additional information
?
-
-
Zea mays subunit ISA 2 alone is catalytically inactive
-
-
-
additional information
?
-
Pseudomonas amyloderamosa WU7211-2
-
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
?
-
-
isoamylase catalyzes the hydrolysis of alpha-1,6-glucosidic linkage specifically in amylopectin, glycogen and derived oligosaccharides
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
activates 10% at 0.5 mM, and 25% at 5 mM, Ca2+ highly stabilizes the enzyme at 80C
CaCl2
-
5 mM, 120% of activity
Co2+
activates 12% at 5 mM
Mn2+
activates 28% at 0.5 mM, and 41% at 5 mM
additional information
poor effects by Na+, K+, Mg2+, Li+, and EDTA at 0.5-5 mM. Mn2+ and Mg2+ do not stabilize the enzyme at 70C and 80C
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(NH4)2Mo2O7
-
1 mM 22% inhibition, 10 mM 100% inhibition
-
2,4-Dinitrofluorobenzene
-
-
2-Hydroxy-5-nitrobenzyl bromide
-
-
ammonium sulfate
-
0.5 M, 30% residual activity
beta-cyclodextrin
-
29%, slightly inhibitory at 10 mM
cellobiose
-
10 mM, 0.4% amylose, relative activity 88%
corn amylose
-
-
-
Cu2+
-
relative activity 78%
Cu2+
complete inhibition at 0.5 mM
CuCl2
-
1 mM, 30% inhibition
CuCl2
-
0.1 mM reduce activity to 3%
CuCl2
-
5 mM, 30% residual activity
cyclomaltoheptaose
-
10 mM, 0.4% amylose, relative activity 93%
D-glucono-delta-lactone
-
relative activity 87%
D-glucose
-
10 mM, 0.4% amylose, relative activity 95%
EDTA
-
5 mM, 80% residual activity
Fe3+
59% inhibition at 0.5 mM, 90% at 5 mM
guanidine hydrochloride
-
3 M, activity completely lost
Hg2+
-
52% inhibition
Hg2+
complete inhibition at 0.5 mM
HgCl2
-
0.1 mM 34% inhibition; 1 mM, 41% inhibition
HgCl2
-
1 mM, complete inhibition
Iodine
-
relative activity 93%
iodoacetate
-
10 mM, 13% inhibition
iodoacetate
-
21%, slight inhibition
isomaltose
-
10 mM, 0.4% amylose, relative activity 82%
maltose
-
10 mM, inhibition slightly, with 0.4% amylose relative activity 90%
maltotetraose
-
10 mM, 0.4% amylose, relative activity 50%
maltotriose
-
competitive inhibitor
maltotriose
-
10 mM, 0.4% amylose, relative activity 53%
MgCl2
-
5 mM, 70% residual activity
N-bromosuccinimide
-
0.01 mg abolishes enzyme activity almost completely
N-bromosuccinimide
-
-
NaF
-
1 mM, 19% inhibition
oligosaccharides with alpha-1,4-glucosidic linkages
-
-
p-chloromercuribenzoate
-
reversible inactivation
p-chloromercuribenzoate
-
1 mM 34% inhibition; 1 mM, complete inhibition
p-chloromercuribenzoate
-
-
Phenylmercuriacetate
-
-
phenylmethanesulfonyl fluoride
9% inhibition at 5 mM
SDS
-
0,1%, activity completely lost
SDS
77% inhibition at 30 mM
Sn2+
28% inhibition at 0.5 mM, 73% at 5 mM
sodium dodecylsulfate
-
1 mM, no residual activity
Succinic anhydride
-
relative activity 94%
Urea
-
20% activity retained
Urea
82% inhibition at 2 M
xylose
-
10 mM, 0.4% amylose, relative activity 97%
Zn2+
64% inhibition at 0.5 mM, 88% at 5 mM
ZnCl2
-
5 mM, 20% residual activity
MnCl2
-
5 mM, 80% residual activity
additional information
-
inhibitory effect of pressure and agitation speed on isoamylase activity in supercritical CO2, overview
-
additional information
no inhibition by EDTA, citrate, maltose, and alpha-cyclodextrin
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
polyethyleneglycol 2000
-
maximal activation of 58% at 0.04% PEG 2000 Da
Triton X-100
-
reagent in the preincubation mixture at concentrations 0.05-1% activates the enzyme by 45-72%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00012
amylopectin
hetero-oligomer; hetero-oligomer
0.00025
amylopectin
homo-oligomer
0.00002
amylose-extender amylopectin
hetero-oligomer; hetero-oligomer
0.00004
amylose-extender amylopectin
homo-oligomer
0.00018
beta-limit dextrin
hetero-oligomer; hetero-oligomer
0.00062
oyster glycogen
hetero-oligomer; hetero-oligomer
-
0.00067
oyster glycogen
homo-oligomer
-
0.0054
phytoglycogen
hetero-oligomer; hetero-oligomer
-
0.0065
phytoglycogen
homo-oligomer
-
0.00021
beta-limit dextrin
homo-oligomer
additional information
additional information
-
potatoamylopectin 0.59 mg/ml-1, oyster glycogen 0.45 mg/ml-1
-
additional information
additional information
-
amylopectin 7.2 mg/ml-1, phytoglycogen 11.9 mg/ml-1, beta-limit dextrin 13.1 mg/ml-1, glycogen 21.8 mg/ml-1
-
additional information
additional information
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.77
pullulan as substrate
0.95
pullulan as substrate; pullulan as substrate
3
-
pullulan, recombinant isoamylase
3.51
amylopectin as substrate
6.58
beta limit dextrin as substrate; beta limit dextrin as substrate
8.95
gylcogen as substrate; gylcogen as substrate
14.98
amylopectin as substrate; amylopectin as substrate
17.16
gylcogen as substrate
29.05
beta limit dextrin as substrate
51.2
-
rabbit liver glycogen
54.6
-
amylose, recombinant isoamylase
120
-
potato starch, recombinant isoamylase
154
-
rice starch, recombinant isoamylase
172
-
corn amylopectin, recombinant isoamylase
174
-
rabbit liver glycogen, recombinant isoamylase
182
-
oyster glycogen, recombinant isoamylase
additional information
6535 U/mg, measuring 0.01 increase in absorbance at 600 nm per h at 50C, pH 6.0, per mg protein
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 4
-
starch, 0.1 M acetate-HCl buffer, pH 3.5, 0.1 M phosphate-citric acid buffer, pH 4
5.5 - 6
-
amylopectin
6 - 7
-
-
6.3
-
only isoamylase with neutral pH optimum
6.5
broad optimum, profile overview
6.5 - 7
-
-
6.5 - 7.5
;
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1 - 5
-
starch, 0.1 M acetate-HCl buffer
2.2 - 7.8
-
0.1 M phosphate-citric acid buffer
4 - 8
-
not active below, amylopectin
5.5 - 9
over 90% of maximal activity within this range, profile overview
7.5 - 9.5
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 37
-
-
30
homo-oligomer
40
hetero-oligomer; hetero-oligomer
52
-
starch, 10 min reaction at pH 3.5
70
recombinant enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 60
-
not active above, starch
40 - 70
-
assay at
60
-
not active above, amylopectin
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
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; 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
Manually annotated by BRENDA team
-
only ISA1, no ISA2
Manually annotated by BRENDA team
-
three ISA activity forms are observed in leaves, two ISA1/ISA2 heteromultimers and one ISA1 homomultimer. ISA1 homomultimer activity exists in mutants lacking ISA2. Mutants without ISA2 differ in leaf starch content, granule morphology, and amylopectin structure compared with nonmutants or lines lacking both ISA1 and ISA2. The data imply that both the ISA1 homomultimer and ISA1/ISA2 heteromultimer function in the maize leaf. 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; three ISA activity forms are observed in leaves, two ISA1/ISA2 heteromultimers and one ISA1 homomultimer. ISA1 homomultimer activity exists in mutants lacking ISA2. Mutants without ISA2 differ in leaf starch content, granule morphology, and amylopectin structure compared with nonmutants or lines lacking both ISA1 and ISA2. The data imply that both the ISA1 homomultimer and ISA1/ISA2 heteromultimer function in the maize leaf. 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
Manually annotated by BRENDA team
-
ISA1 and ISA2; ISA1 and ISA2
Manually annotated by BRENDA team
Arabidopsis thaliana Col-0
-
;
-
Manually annotated by BRENDA team
additional information
not detected in the stem, petiole, or root at the four-leaf stage, while at the six-leaf stage the enzyme's mRNA is present in all of the non-storage tissues, quantitative expression analysis, overview
Manually annotated by BRENDA team
additional information
-
not in endosperm
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
TreX may be located at the cell surface due to the proline-rich region
Manually annotated by BRENDA team
-
TreX may be located at the cell surface due to the proline-rich region
-
Manually annotated by BRENDA team
-
granule like structures inside the choloplast
Manually annotated by BRENDA team
Arabidopsis thaliana Col-0
-
;
-
Manually annotated by BRENDA team
Pseudomonas amyloderamosa JD210, Pseudomonas amyloderamosa SMP1
-
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
-
2 subunits, not linked covalently
136804
65000
-
gel filtration, 0.5-m Bio-Gel A
136801
65000
-
SDS-PAGE, gel filtration
136809
75000
-
SU1
136814
79000
-
maize gene su1 recombinant polypeptide, expressed in E. coli
136814
80000
-
-
136808
80000
gel permeation chromatography
678801
80810
-
SB-15, DNA sequence analysis
136799
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
136813
83000
-
-
136815
86000 - 94000
-
SB-15, gel filtration, SDS-PAGE
136799
86000 - 94000
-
86000, undegraded polypeptide chain, SDS-PAGE
136802
86000 - 94000
-
-
136813
88000
-
calculated by comparison with standard proteins
136802
90000
-
undegraded polypeptide chain
136802
94000
-
native enzyme, centrifugation analysis
136802
94000
-
native enzyme, centrifugation analysis; sedimentation equilibrium
136804
94000
-
-
136805, 136806
95000
-
gel electrophoresis, low speed sedimentation
136806
100000
gel filtration
732278
120000
-
-
136805
141000
-
isoamylase II, gel filtration
136814
158000
-
ISA2 dimer, gel filtration and analytical ultracentrifugation
732655
178000
-
native enzyme
136800
180000
subunit ISA1, crystal structure analysis and SDS-PAGE
732146
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
716600
340000
-
native enzyme, gel filtration, TSKgel G3000SWxl
136815
370000
gel permeation chromatography; gel permeation chromatography
678801
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
716600
420000
SDS-PAGE, homooligomer, five OsISA1
682469
450000
native ISA1-ISA2 complex, gel filtration
732750
490000
-
native enzyme, gel filtration, TSKgel G4000SWxl
136815
510000
SDS-PAGE, heterooligomer, hetero-hexamer composed of five OsISA1 and one OsISA2; SDS-PAGE, heterooligomer, hetero-hexamer composed of five OsISA1 and one OsISA2
682469
520000
-
gel filtration
136800
750000
recombinant ISA1-ISA2 complex, gel filtration
732750
830000
-
SDS-PAGE
672691
additional information
comparable mobility in the native PAGE of native enzyme recombinnat enzyme complex
732750
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 74100, deduced from gene sequence, x * 74000, SDS-PAGE
?
-
x * 83400, deduced from genen sequence
?
-
x * 83000, SDS-PAGE
?
x * 95000, SDS-PAGE
?
-
x * 79000, SDS-PAGE
?
x * 90500, about, sequence calculation
?
-
x * 75000, SDS-PAGE; x * 80000, about, SDS-PAGE
?
x * 150000, ISA1 and ISA2 as stable dimer, SDS-PAGE
?
Dickeya chrysanthemi PY35
-
x * 74100, deduced from gene sequence, x * 74000, SDS-PAGE
-
?
Pseudomonas amyloderamosa SB-15
-
x * 95000, SDS-PAGE
-
dimer
-
1 * 83000 + 1 * 95000
dimer
-
2 * 46000, sedimentation equilibrium; 2 * 52000, gel filtration; dimers probably obtained by partial proteolytic degradation
dimer
-
2 * 46000, sedimentation equilibrium; 2 * 50000, not linked covalently
dimer
-
2 * 85000, ISA1 dimer, SDS-PAGE
dimer or tetramer
-
the enzyme exists in two oligomeric states in solution, as a dimer and tetramer
homodimer
2 * 93000, subunit ISA1, crystal structure analysis and SDS-PAGE
homodimer
Chlamydomonas reinhardtii 330
-
2 * 93000, subunit ISA1, crystal structure analysis and SDS-PAGE
-
homooligomer
-
-
monomer
-
gel electrophoresis
monomer
-
purified enzyme has monomeric structure
monomer
1 * 60000, SDS-PAGE
monomer
1 * 100000, SDS-PAGE, 1 * 101155, sequence calculation
monomer
-
1 * 85000, ISA1 monomer, SDS-PAGE
monomer
Bacillus sp. CICIM 304
-
1 * 100000, SDS-PAGE, 1 * 101155, sequence calculation
-
oligomer
-
probably homo-tetramer and homohexamer
oligomer
heterooligomer OsISA1-OsISA2 6*85000, HPLC gel filtration; homooligomer OsISA1 5 * 830000 and heterooligomer OsISA1-OsISA2 6 * 85000, HPLC gel filtration
tetramer
heterotetramer with PvISA1, 2 * 87000 PyISA1 and 2 * 93000 PvISA2, SDS-PAGE; heterotetramer with PvISA2, 2 * 87000 PvISA1 and 2 * 93000 PvISA2, SDS-PAGE
monomer
Pseudomonas amyloderamosa SMP1
-
-
-
additional information
associated with Stisa1 to form a multimeric complex; associated with Stisa2 to form a multimeric complex
additional information
-
enzymic activity lies within a 88000 Da subunit of a multimeric enzyme complex
additional information
-
ISA1 and ISA2 proteins are subunits of the same enzyme
additional information
-
the structural lid, amino acids 99-97, at the active site generated by the tetramerization is closely associated with the bifunctionality and in particular with the alpha-1,4-transferase activity
additional information
-
isozymes Psisa1, Psisa2, and Psisa3, structure comparisons
additional information
the enzym eis an (alphabeta)8-barrel protein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified subunit ISA1 alone and in complex with maltoheptaose, X-ray diffraction structure determination at 2.3 A and 2.4 A, respectively; purified subunit ISA1 alone and in complex with maltoheptaose, X-ray diffrcation structure determination at 2.3 A and 2.4 A, respectively. The subunit structure includes highly conserved catalytic (beta/alpha)8 A-domain (aa 184-750), N-terminal beta-sandwich domain (aa 76-183), and C-terminal beta-sandwich domain (aa 751-875)
crystallized from ammonium sulfate solution, crystals belong to orthorhombic space group P212121
-
TreX in complex with an acarbose ligand, microbatch method under oil at 18C, dimeric crystal from 16% PEG 8000, 0.2 M NaCl, and 0.1 M CHES buffer, pH 9.5, tetrameric crystal form from 2.2 M ammonium phosphate and 0.1 M Tris-HCl buffer, pH 8.5. For the acarbose intermediate complex crystal, 0.1% acarbose is added to the protein, followed by incubation for 1 h prior to the setup of the crystal in 8% PEG 3000, 0.2M lithium sulfate, and 0.1 M imidazole buffer, pH 8.0, cyroprotection by 20% glycerol in mother liquor, in both crystal forms, the asymmetric unit consists of one dimer, X-ray diffraction structure determination and analysis at 2.8-3.0 A resolution
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.5 - 7.5
-
-
136806
3.5 - 5.5
-
-
136803
4.5 - 9
purified native enzyme, 50C, 1 h, over 70% activity remaining
732278
5 - 11.5
-
more than 50% of the original activity detectable between pH 6.6-10.5
136809
6.5 - 7
-
assayed at 22C enzyme displays broader activity and stability optima of pH 5.0 -7.5
136813
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4
-
recombinant wild-type and His-tagged enzyme are more stable at room temperature than at 4C
666093
10 - 40
-
temperature treatment does not influence the enzyme activity
136815
21
-
recombinant wild-type and His-tagged enzyme are more stable at room temperature than at 4C
666093
30 - 70
purified native enzyme, pH 6.0, 1 h, over 70% activity remaining
732278
40
-
stable up to 40C, at temperature below 30C and above 65C enzyme is almost inactive
136809
40
homooligomer, complete loss of activity
682469
40 - 50
hetero-oligomer, loss of 50% activity; hetero-oligomer, loss of 50% activity
682469
45
-
-
136800
45
-
not stable above
136806
50
-
amylopectin, incubated in the absence of substrate enzyme stable only up to 45C
136800
60
-
activity decreased about 95%
136806
65
-
heating 10 min at 65C results in complete loss of activity
136806
75
-
2 h, recombinant wild-type enzyme and His-tagged enzyme are sstable
666093
80
-
2 h, recombinant wild-type enzyme and His-tagged enzyme are sstable
666093
80
purified native enzyme, pH 6.0, 1 h, inactivation
732278
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
very unstable, even at low temperatures
-
Pseudomonas isoamylase immobilized physically by raw starch adsorption results in an increase in pH and temperature stability and a retention of about 75% of activity even after 75 days
quite stable in maltose-containing buffer
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, two weeks, 30% loss of activity
-
4C for 5 months 85% enzyme activity retained, preservation with 0.1% potassium sorbate isoamylase activity was not reduced until 2 months of incubation
-
4C several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
copurification of native isozymes ISA1 and ISA2 partially from leaves by gel filtration, copurification of TAP-tagged ISA1 and ISA2 from Escherichia coli strain BL21(DE3) by tandem-affinity chromatography on TEV and calmodulin, followed by gel filtration
recombinant C-terminally His8-tagged single subunit ISA1 or ISA1 in complex with His8-tagged ISA2 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography; recombinant C-terminally His8-tagged single subunit ISA2 or His8-tagged ISA2 in complex with ISA1 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
native extracellular enzyme 369fold from culture supernatant by ultrafiltration, ammonium sulfate fractionation, gel filtration, two different steps of anion exchange chromatography, and dialysis, to homogeneity
recombinant His-tagged subunit ISA1 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
ammonium sulfate precipitation, DEAE cellulose column chromatography, CM-cellulose column chromatography, and DEAE-Sephadex gel filtration
-
HitrapQ column chromatography and TSKgel DEAE-5PW gel filtration
-
wild type enzyme by HitrapQ HP and TSKgel G3000SWXL column chromatography, recombinant OsISA2 by HitrapQ HP column chromatography; wild type enzyme by HitrapQ HP and TSKgel G3000SWXL column chromatography, recombinant OsISA2 by HitrapQ HP column chromatography
Q sepharose column chromatography; Q sepharose column chromatography; Q sepharose column chromatography
raw starch desorption adsorption
recombinant protein by His tag column chromatography
-
recombinant wild-type and His-tagged enzyme
-
recombinant wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography
-
HiTrapQ column chromatography and Superdex 200 gel filtration
native subunit ISA2 from leaves by anion exchange chromatography, ultrafiltration, and gel filtration, separation from subunit ISA1; native subunit ISAI from leaves by anion exchange chromatography, ultrafiltration, and gel filtration, separation from subunit ISA2
-
recombinant C-terminally His8-tagged single subunit ISA1 or ISA1 in complex with His8-tagged ISA2 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography; recombinant C-terminally His8-tagged single subunit ISA2 or His8-tagged ISA2 in complex with ISA1 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene ArDBE, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
coexpression of wild-type His-tagged ISA1 and ISA2, and of mutant D367A ISA1 with wild-type ISA2, in Escherichia coli strain BL21(DE3)
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
into Agrobacterium tumefaciens strain GV310, GFP/GUS promoter fusion constructs for AtISA1, AtISA2, AtISA3 into Arabidopsis thaliana using the floral dip method
-
gene treX, component of a treXYZ operon, DNA and amino acid sequence determination and analysis, sequence comparison, genetic organization in the treXYZ operon, overview
-
DNA and amino acid sequence determination and analysis, phylogenetic tree
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
iam gene cloned and expressed in Escherichia coli JM101, pMON17481, production of a nonsecreted signal peptide-less isoamylase
-
expression in Escherichia coli
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) Star cells
-
expression of OsISA2 in Escherichia coli; expression of OsISA2in Escherichia coli
isoamylase gene is a single copy in rice genome, located on chromsome 8
-
cloning of cDNAs of different isoforms, Psisa1-Psisa3, DNA and amino acid sequence determination and analysis, phylogenetic analysis and sequence comparisons, overview
-
expressed in Saccharomyces cerevisiae
plasmid pIAM275, pUC9 carrying iam gene, Escherichia coli, recominant plasmid does not direct the synthesis of isoamylase in Escherichia coli , sequenced
-
cloned to an expression vector with a T7lac promoter. Both wild-type and His-tagged isoamylases are expressed in Escherichia coli
-
expression of in Escherichia coli
-
expression of wild-type and mutant enzymes in Escherichia coli, sequence comparison
-
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
-
DNA and amino acid sequence determination and analysis, sequence comparisons
-
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
-
recombinant GST-ISA2 fusion protein is expressed in Escherichia coli Rosetta DE3-pLysS cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the isoform ISA1 transcript level is low during starch degradation
isoform ISA2 transcript is relatively abundant during periods of either starch biosynthesis or catabolism
the isoform ISA1 transcript level is elevated in tissues where starch is synthesized
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D367A
site-directed mutagenesis of the catalytic nucleophile Asp-367 in ISA1, the mutation abolishes the catalytic activity of the enzyme complex
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; 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
Arabidopsis thaliana Col-0
-
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; 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
-
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
Chlamydomonas reinhardtii 330
-
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
-
transgenic plants expressing antisense RNA for Stisa1 or Stisa2, accumulate small amounts of soluble glucan and large numbers of tiny starch granules
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
-
generation of mutant isa2-339; generation of mutant su1-4582
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
bioinformatics, microarray and reporter gene analyses reveal that AtISA1 and AtISA2, AtISA2 and AtISA3 or AtISA1, AtISA2 and AtISA3 are coexpressed under certain conditions
analysis
isoamylase-type debranching enzymes (ISAs) play an important role in determining starch structure
detergent
-
effective additive in dishwashing and laundry detergents
nutrition
-
-
detergent
Bacillus sp. KSM-K16
-
effective additive in dishwashing and laundry detergents
-
analysis
-
structural determination of glycogen and starch components
nutrition
-
industrial production of various syrups from starch
medicine
-
diagnosis of acute pancreatitis in humans
nutrition
-
production of high-maltose syrups and highly purified maltose by a combination of debranching enzymes
analysis
-
elucidating of the finestructures of various polysaccharides
analysis
-
Di-O-a-maltosyl-beta-cyclodextrin is fromed via a transglycosylation reaction using TreX, a Sulfolobus solfataricus P2 debranching enzyme, isoamylase is used to examine the structure of the product and to produce branched cyclodextrins via reverse reaction
analysis
-
composition and starch molecular structure of eight rice varieties are studied, rice starches were debranched using isoamylase, different amount and size of longbranch chain of amylopectin influences the compactness of starch structure
nutrition
-
industrial production of amylose, maltose and D-glucose from starch, alone or in combination with beta-amylase and glucoamylase production
nutrition
-
industrial production of amylose, maltose and D-glucose from starch, alone or in combination with beta-amylase and glucoamylase production; strain MI-414 for industrial use, produces 10fold more isoamylase than SB-15
analysis
Pseudomonas amyloderamosa JD210
-
-
-
analysis
Pseudomonas amyloderamosa MI-414
-
elucidating of the finestructures of various polysaccharides
-
nutrition
Pseudomonas amyloderamosa MI-414
-
industrial production of amylose, maltose and D-glucose from starch, alone or in combination with beta-amylase and glucoamylase production; strain MI-414 for industrial use, produces 10fold more isoamylase than SB-15
-
analysis
Pseudomonas amyloderamosa SMP1
-
-
-
nutrition
Pseudomonas amyloderamosa SMP1
-
-
-
synthesis
-
the enzyme is used for debranching of amylomaize in the production of cycloamylose, natural amylopectin containing starch with enhanced conversion yield after debranching, use of Thermus aquaticus 4-alpha-glucanotransferase for conversion of debranched amylomaize amylose and amylomaize amylopectin into cycloamylose, overview
degradation
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thermophilic enzyme shows a potential to be used in industry to degrade the debranching points of starch at a high temperature
food industry
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saccharification potential of isoamylases is employed in food industry for preparation of high glucose syrup, maltose, maltitol, trehalose, cyclodextrin and resistant starch from starch
additional information
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isoamylase can potentially be used in the elucidation of fine structures of polysaccharides and related alpha-glucans and can be also be used as effective additive in dishwashing and laundry detergents
food industry
saccharification potential of isoamylases is employed in food industry for preparation of high glucose syrup, maltose, maltitol, trehalose, cyclodextrin and resistant starch from starch
additional information
isoamylase can potentially be used in the elucidation of fine structures of polysaccharides and related alpha-glucans and can be also be used as effective additive in dishwashing and laundry detergents
food industry
Pseudomonas amyloderamosa SB-15
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saccharification potential of isoamylases is employed in food industry for preparation of high glucose syrup, maltose, maltitol, trehalose, cyclodextrin and resistant starch from starch
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additional information
Pseudomonas amyloderamosa SB-15
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isoamylase can potentially be used in the elucidation of fine structures of polysaccharides and related alpha-glucans and can be also be used as effective additive in dishwashing and laundry detergents
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