Information on EC 3.2.1.94 - glucan 1,6-alpha-isomaltosidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.2.1.94
-
RECOMMENDED NAME
GeneOntology No.
glucan 1,6-alpha-isomaltosidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in polysaccharides, to remove successive isomaltose units from the non-reducing ends of the chains
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
-
-
-
-
hydrolysis of O-glycosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
6-alpha-D-glucan isomaltohydrolase
Optimum activity is on those 1,6-alpha-D-glucans containing 6, 7 and 8 glucose units; those containing 3, 4 and 5 glucose units are hydrolysed at slower rates.
CAS REGISTRY NUMBER
COMMENTARY hide
56467-68-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-linked gluco-oligosaccharide + H2O
isomaltose + D-glucose
show the reaction diagram
-
-
-
?
dextran + 1-butanol
1-butyl alpha-isomaltoside + H2O
show the reaction diagram
-
-
-
r
dextran + 1-propanol
1-propyl alpha-isomaltoside + H2O
show the reaction diagram
-
-
-
r
dextran + ethanol
ethyl alpha-isomaltoside + H2O
show the reaction diagram
-
-
-
r
dextran + H2O
alpha-isomaltose + O-alpha-D-Glcp-(1-3)-O-alpha-D-Glcp-(1-6)-D-Glc + O-alpha-D-Glcp-(1-4)-O-alpha-D-Glcp-(1-6)-D-Glc + O-alpha-D-Glcp-(1-2)-O-alpha-D-Glcp-(1-6)-D-Glc
show the reaction diagram
dextran + methanol
methyl alpha-isomaltoside + H2O
show the reaction diagram
-
-
-
r
dextran + sucrose
6G-alpha-isomaltosylsucrose + H2O
show the reaction diagram
-
-
-
r
dextran + trehalose
6-alpha-isomaltosyltrehalose + H2O
show the reaction diagram
-
-
-
r
glucooligosaccharides + H2O
isomaltose + D-glucose
show the reaction diagram
isomaltoheptaose + H2O
?
show the reaction diagram
-
-
-
-
?
isomaltohexaose + H2O
?
show the reaction diagram
-
-
-
-
?
isomaltohexatiol + H2O
isomaltose + Isomaltitol
show the reaction diagram
-
-
-
?
isomaltooctaose + H2O
?
show the reaction diagram
-
-
-
-
?
isomaltooligosaccharide + H2O
isomaltose + glucose
show the reaction diagram
isomaltopentaose + H2O
?
show the reaction diagram
-
-
-
-
?
isomaltotetraose + H2O
?
show the reaction diagram
-
-
-
-
?
isomaltotriitol + H2O
isomaltose + sorbitol
show the reaction diagram
isomaltotriose + H2O
alpha-isomaltose + D-glucose
show the reaction diagram
panose + H2O
alpha-isomaltose
show the reaction diagram
panose + H2O
isomaltose + D-glucose
show the reaction diagram
pullulan + H2O
isopanose
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
glucooligosaccharides + H2O
isomaltose + D-glucose
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
moderate activation
Li+
moderate activation
Mn2+
moderate activation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-ethyl-3-(3-dimethylaminopropyl)carbodiimide
-
specifically modifies carboxyl residues
4-chloromercuribenzoate
53% inactivation at 1 mM, 93% inactivation at 5 mM
N-bromosuccinimide
-
-
additional information
-
no inhibitors are isopanose and maltotriose
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.4
Dextran
60C, pH 3.5
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
496
Dextran
Arthrobacter dextranolyticus
Q6BE01
60C, pH 3.5
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.3
isomaltose
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.012
-
E420A mutant
0.17
-
D396A mutant
0.22
-
D340A mutant
0.24
-
D373A mutant
0.35
-
D295A mutant
0.45
-
D163A mutant
0.67
-
D107A mutant
0.78
-
wild-type enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.5 - 6
50% activity between pH 2.5 and pH 6
2.5 - 7.5
-
50% of maximum activity at pH 2.5 and 10% at pH 7.5
3 - 7.5
-
10% of maximum activity at pH 3 and 20% at pH 7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 70
-
20% of maximum activity at 30C and 65% at 70C
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65000
-
SDS-PAGE
65990
calculated from amino acid sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 69000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.8 - 8
-
4C, 24 h
136635, 137016
3.5 - 10
enzyme is stable at pH 4-8 and stable at pH 3.5-10 with 50% of the original activity
654317
4.1 - 8
-
45C, 2 h
136635
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
60% activity at pH 5 after 30 min
70
-
20% activity after 10 min
80
-
complete inactivation after 10 min
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Methanol
-
assay with 20% at 37C for 4 min
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
photooxidation with Rose Bengal
-
136635
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Bacillus subtilis
expressed in Escherichia coli
-
expression in Escherichia coli
-
the signal peptide of of Arthrobacter globiformis isomaltodextranase containing the twin-arginine motif is fused with GFP, and the corresponding plasmid pPIGFP is transformed into the wild type, Corynebacterium glutamicum ATCC 1386. The signal peptide of IMD is a bona fide Tat pathway targeting signal
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D107A
-
activity similar to wild-type enzyme
D163A
-
activity similar to wild-type enzyme
D198N
-
0.003% of wild-type activity, largely increased Kd-value
D227A
-
no activity of dextran hydrolysis
D227E
-
decreased activity of dextran hydrolysis
D227N
-
decreased activity of dextran hydrolysis
D227Q
-
decreased activity of dextran hydrolysis
D266N
-
0.011% of wild-type activity, without change in substrate binding ability
D295A
-
activity similar to wild-type enzyme
D313N
-
0.002% of wild-type activity, largely increased Kd-value
D340A
-
activity similar to wild-type enzyme
D342A
-
no activity of dextran hydrolysis
D342E
-
decreased activity of dextran hydrolysis
D342N
-
decreased activity of dextran hydrolysis
D342Q
-
decreased activity of dextran hydrolysis
D373A
-
activity similar to wild-type enzyme
D396A
-
activity similar to wild-type enzyme
E420A
-
activity similar to wild-type enzyme