Information on EC 2.4.1.B34 - 4,6-alpha-glucanotransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.1.B34
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
4,6-alpha-glucanotransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
The enzyme uses maltooligosaccharides as donor and acceptor substrates. It cleaves alpha1->4 glucosidic bonds and synthesizes 1->6 and 1->4 glucosidic linkages.
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
(1->4)-alpha-D-glucan:(1->4),(1->6)-alpha-D-glucan alpha-glucanotransferase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme GtfC differs in the domain order from dextransucrase and GtfB enzymes, and it completely lacks domain V
UniProt
Manually annotated by BRENDA team
enzyme GtfC differs in the domain order from dextransucrase and GtfB enzymes, and it completely lacks domain V
UniProt
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
amylose + maltose
maltotriose + panose
show the reaction diagram
amylose V
?
show the reaction diagram
amylose V + H2O
?
show the reaction diagram
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both hydrolysis and transferase activities occur. Besides the presence of alpha1->4 linkages, alpha1->6 linkages are newly formed. In the product mixture derived from amylose V, the alpha1->6/alpha1->4 linkage ratio increases up to 90:10. In the product mixture, free glucose, 4-substituted reducing glucose residues [-(1->4)-alpha-D-Glc], and a small amount of reducing-end glucose residues which are 6 substituted are detected
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?
amylose V + maltose
maltoriose + maltotetraose + ?
show the reaction diagram
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?
maltodextrin + H2O
?
show the reaction diagram
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i.e. short-chain alpha1->4-linked maltodextrins
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-
?
Maltoheptaose
?
show the reaction diagram
maltoheptaose + H2O
?
show the reaction diagram
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-
?
maltoheptaose + H2O
D-glucose + maltotriose + maltohexose
show the reaction diagram
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first clear products of the reaction
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?
Maltohexaose
?
show the reaction diagram
maltohexaose + H2O
D-glucose + maltopentaose
show the reaction diagram
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first clear reaction products accumulating after 1 h, longer incubation leads to 4-substituted, 6-substituted, and terminal glucose residues at a molar ratio of 63, 17, and 20%
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?
maltooligosaccharide
?
show the reaction diagram
maltopentaose
?
show the reaction diagram
maltopentaose + H2O
D-glucose + maltotetraose
show the reaction diagram
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first clear reaction products accumulating after 1 h, longer incubation leads to 4-substituted, 6-substituted, and terminal glucose residues at a molar ratio of 63, 17, and 20%
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?
maltose
?
show the reaction diagram
Maltotetraose
?
show the reaction diagram
maltotetraose + H2O
D-glucose + maltotetraose
show the reaction diagram
maltotriose
?
show the reaction diagram
potato starch
?
show the reaction diagram
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?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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1 mM, hydrolysis reaction increases to 111%, transfer reaction to 422% of initial value, respectively
EDTA
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1 mM, 25% inhibition of hydrolysis reaction, transfer reaction increases to 388%
Fe2+
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1 mM, 50% inhibition of hydrolysis reaction, transfer reaction increases to 175%
K+
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1 mM, 14% inhibition of hydrolysis reaction, transfer reaction to 435% of initial value, respectively
Mg2+
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1 mM, 6% inhibition of hydrolysis reaction, transfer reaction increases to 378% of initial value, respectively
Mn2+
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1 mM, hydrolysis reaction increases to 125%, transfer reaction to 425% of initial value, respectively
Na+
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1 mM, hydrolysis reaction increases to 118%, transfer reaction to 404% of initial value, respectively
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
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1 mM, 49% inhibition of hydrolysis reaction, complete inhibition of transfer reaction
EDTA
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1 mM, 25% inhibition of hydrolysis reaction, transfer reaction increases to 388%
Fe2+
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1 mM, 50% inhibition of hydrolysis reaction, transfer reaction increases to 175%
Fe3+
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1 mM, 65% inhibition of hydrolysis reaction, 15% inhibition of transfer reaction
K+
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1 mM, 14% inhibition of hydrolysis reaction, transfer reaction to 435% of initial value, respectively
Mg2+
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1 mM, 6% inhibition of hydrolysis reaction, transfer reaction increases to 378% of initial value, respectively
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
1 mM, slight activation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
150
maltose
relaese of glucose, pH 4.7, 37C
additional information
amylose V
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Km value for hydrolysis reaction 0.5 g/l, for transfer reaction 0.69 g/l, pH 5.0, 55C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.06 - 36.22
amylose V
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37
maltose
Lactobacillus reuteri
A5VL73, Q5SBN1
relaese of glucose, pH 4.7, 37C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
amylose V
Lactobacillus reuteri
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Km/kcat value for hydrolysis reaction 18.5 l per s and g, for transfer reaction 53.0 l/s and g, pH 5.0, 55C
210492
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 5
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substrate: maltotetraose
5
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both hydrolysis and transfer reactions
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 7.5
more than 50% of maximum activity
5.5 - 7
more than 70% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 37
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substrate: maltotetraose
55
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both hydrolysis and transfer reactions
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
30% of maximum activity
55
drastic decrease above
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
86400
x * 90000, SDS-PAGE, x * 86400, calculated
90000
x * 90000, SDS-PAGE, x * 86400, calculated
99000
x * 99000, calculated
154000
x * 154000, calculated; x * 154000, calculated
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
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stable for more than 2 h
55
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half-life below 10 min
60
stable for at least 10 min
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Esdcherichia coli
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expression of N-terminally truncated variant, in Escherichia coli; expression of N-terminally truncated variant, in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D1015N
additional information
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removal of the variable N-terminal region of the GTFB enzyme (yielding construct GTFB734-1619) results in increased expression of soluble and active enzyme in Escherichia coli