Information on EC 3.2.1.115 - branched-dextran exo-1,2-alpha-glucosidase

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The expected taxonomic range for this enzyme is: Flavobacterium sp.

EC NUMBER
COMMENTARY hide
3.2.1.115
-
RECOMMENDED NAME
GeneOntology No.
branched-dextran exo-1,2-alpha-glucosidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of (1->2)-alpha-D-glucosidic linkages at the branch points of dextrans and related polysaccharides, producing free D-glucose
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis
-
-
hydrolysis of O-glycosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
(1->2)-alpha-D-glucosyl-branched-dextran 2-glucohydrolase
Does not hydrolyse disaccharides or oligosaccharides containing linear 1,2-alpha-glucosidic linkages.
CAS REGISTRY NUMBER
COMMENTARY hide
72840-94-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain M-73
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2(3),2(4)-di-O-alpha-glucosyl-isomaltotetraose + H2O
isomaltotetraose + 2 alpha-D-glucose
show the reaction diagram
-
-
-
-
?
2(3)-O-alpha-D-glucosyl-isomaltotetraose + H2O
isomaltotetraose + alpha-D-glucose
show the reaction diagram
-
-
-
-
?
2(3)-O-alpha-D-glucosyl-isomaltotriose + H2O
isomaltotriose + alpha-D-glucose
show the reaction diagram
-
-
-
-
?
B-1298 soluble dextran + H2O
D-glucose + ?
show the reaction diagram
-
incubation at 40C for 24 h, specifically splitz alpha-1,2-glucosidic linkages
-
-
?
B-1299 soluble dextran + H2O
D-glucose + ?
show the reaction diagram
-
incubation at 40C for 24 h
-
-
?
B-1397 soluble dextran + H2O
D-glucose + ?
show the reaction diagram
-
incubation at 40C for 24 h
-
-
?
dextran + H2O
alpha-D-glucose
show the reaction diagram
mutan IG-1 + H2O
?
show the reaction diagram
-
major linkages: alpha-1,3-, alpha-1,6-, 18% as effective as soluble dextran for induction of enzyme
-
-
?
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
additional information
?
-
-
hydrolysis of alpha-1,2-glucosidic linkages at branching points of dextran
-
-
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Al3+
-
1.33 mM, 0.9% relative activity
Cu2+
-
1.33 mM, 1.7% relative activity
D-glucono-1,5-lactone
-
strong inhibitor, 34.2% relative activity
Fe3+
-
1.33 mM, 2.6% relative activity
Hg2+
-
1.33 mM, 1.2% relative activity
iodoacetic acid
-
still 60.1% relative activity
Sodium dodecyl sulfate
-
strong inhibitor, 37.9% relative activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
effect of different carbon sources on enzyme activity, inducibility of enzyme
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.21
B-1298 soluble dextran
-
mg/ml
-
0.27
B-1299 soluble dextran
-
mg/ml
-
0.91
B-1397 soluble dextran
-
mg/ml
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
66
-
pH 5.6, 40C
additional information
-
5.8 micro-g glucose/ml, substrate B-1298 soluble dextran; 5.8 micro-g glucose/ml, substrate B-1299 soluble dextran; 5.8 micro-g glucose/ml, substrate B-1397 soluble dextran
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6
-
assay at
6
-
highest activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
assay at
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
125000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 125000, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9
-
incubation at 4C for 24 h
697134
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
up to 40C on heating for 10 min
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE