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Enzyme Nomenclature
Information on EC 2.4.1.B34 - 4,6-alpha-glucanotransferase
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.4.1.B34
preliminary BRENDA-supplied EC number
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RECOMMENDED NAME
GeneOntology No.
4,6-alpha-glucanotransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
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.
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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
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme GtfC differs in the domain order from dextransucrase and GtfB enzymes, and it completely lacks domain V
UniProt
enzyme GtfC differs in the domain order from dextransucrase and GtfB enzymes, and it completely lacks domain V
UniProt
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
amylose V + H2O
?
-
-
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
-
?
amylose V + maltose
maltoriose + maltotetraose + ?
-
-
-
?
maltodextrin + H2O
?
-
i.e. short-chain alpha1->4-linked maltodextrins
-
-
?
maltoheptaose + H2O
D-glucose + maltotriose + maltohexose
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first clear products of the reaction
-
?
maltohexaose + H2O
D-glucose + maltopentaose
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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%
-
?
maltopentaose + H2O
D-glucose + maltotetraose
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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%
-
?
amylose + maltose
maltotriose + panose
the enzyme synthesizes larger saccharides with alpha1->4 and alpha1->6 glucosidic linkages
panose i.e. Glc-alpha-(1->6)-maltose
-
?
amylose + maltose
maltotriose + panose
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the enzyme synthesizes larger saccharides with alpha1->4 and alpha1->6 glucosidic linkages
panose i.e. Glc-alpha-(1->6)-maltose
-
?
amylose V
?
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GtfB produces a high molecular mass polymer with a molecular mass about 80 times greater than that of the starting amylose V
-
?
Maltoheptaose
?
the enzyme synthesize oligosaccharides up to a degree of polymerization of at least 14. The enzyme introduces 1->6 glucosidic linkages (18%) into the final mixture of products
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-
?
Maltoheptaose
?
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the enzyme synthesize oligosaccharides up to a degree of polymerization of at least 14. The enzyme introduces 1->6 glucosidic linkages (18%) into the final mixture of products
-
-
?
maltooligosaccharide
?
the enzyme uses maltooligosaccharides as donor and acceptor substrates. The enzyme disproportionates (cleaves 1->4 and synthesizes 1->6 and 1->4 glucosidic linkages) and 1->6 polymerizes maltotetraose and larger maltooligosaccharide substrates. Only linear products are made and that with increasing degrees of polymerization, more 1->6 glucosidic linkages are introduced into the final products
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-
?
maltooligosaccharide
?
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the enzyme uses maltooligosaccharides as donor and acceptor substrates. The enzyme disproportionates (cleaves 1->4 and synthesizes 1->6 and 1->4 glucosidic linkages) and 1->6 polymerizes maltotetraose and larger maltooligosaccharide substrates. Only linear products are made and that with increasing degrees of polymerization, more 1->6 glucosidic linkages are introduced into the final products
-
-
?
maltotetraose + H2O
D-glucose + maltotetraose
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first clear products of the reaction. The enzyme is rather hydrolytic at the start of the reaction. When reaction products start to accumulate, transglycosylation becomes more efficient
-
?
maltotetraose + H2O
D-glucose + maltotetraose
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first clear products of the reaction. The enzyme is rather hydrolytic at the start of the reaction. When reaction products start to accumulate, transglycosylation becomes more efficient
-
?
additional information
?
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GtfD shows clear hydrolase/transglycosylase activity with malto-oligosaccharides with degree of polymerzation of 3 to 7 and forms a range of shorter and longer oligosaccharides. The enzyme is unable to synthesize consecutive alpha1->6 glucosidic bonds. Instead, it forms a high molecular mass and branched alpha-glucan with alternating alpha1->4 and alpha1->6 linkages from amylose/starch
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-
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additional information
?
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inactive on sucrose, panose, nigerose, beta-cyclodextrins, and isomalto-oligosaccharides with degree of polymerzation of 2, 3, and 5
-
-
-
additional information
?
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GtfD shows clear hydrolase/transglycosylase activity with malto-oligosaccharides with degree of polymerzation of 3 to 7 and forms a range of shorter and longer oligosaccharides. The enzyme is unable to synthesize consecutive alpha1->6 glucosidic bonds. Instead, it forms a high molecular mass and branched alpha-glucan with alternating alpha1->4 and alpha1->6 linkages from amylose/starch
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-
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additional information
?
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inactive on sucrose, panose, nigerose, beta-cyclodextrins, and isomalto-oligosaccharides with degree of polymerzation of 2, 3, and 5
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-
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additional information
?
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GtfC acts on maltooligosaccharides and amylose-V yielding linear gluco-oligomers also containing, besides alpha1->4, alpha1->6 glycosidic linkages. In the product mixture, free glucose units, 4-substituted reducing-end glucose residues and trace amounts of 6-substituted reducing-end glucose residues are present. The higher the degree of polymerization of the substrate, the higher the percentages of alpha1->6 glycosidic linkages introduced into the product. No substrates: maltose, maltotriose, sucrose, nigerose, isomaltooliogosaccharides, panose, reuteran
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-
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additional information
?
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GtfC acts on maltooligosaccharides and amylose-V yielding linear gluco-oligomers also containing, besides alpha1->4, alpha1->6 glycosidic linkages. In the product mixture, free glucose units, 4-substituted reducing-end glucose residues and trace amounts of 6-substituted reducing-end glucose residues are present. The higher the degree of polymerization of the substrate, the higher the percentages of alpha1->6 glycosidic linkages introduced into the product. No substrates: maltose, maltotriose, sucrose, nigerose, isomaltooliogosaccharides, panose, reuteran
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additional information
?
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the enzyme is unable to use sucrose as a donor substrate and is inactive with the sucrose analogs turanose and palatinose, with raffinose, with the DP5 and DP6 isomaltooligosaccharides and with panose
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-
-
additional information
?
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the enzyme is unable to use sucrose as a donor substrate and is inactive with the sucrose analogs turanose and palatinose, with raffinose, with the DP5 and DP6 isomaltooligosaccharides and with panose
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-
-
additional information
?
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enzyme cleaves alpha1->4 glycosidic linkages and adds the released glucose moieties one by one to the non-reducing end of growing linear alpha-glucan chains via alpha1->6 glycosidic linkages (alpha1->4 to alpha1->6 transfer activity). It converts pure maltooligosaccharide substrates into linear alpha-glucan product mixtures with about 50% alpha1->6 glycosidic bonds (isomalto/maltooligosaccharides). Largest products synthesized from maltoheptaose have a degree of polymerizatition bleow 50
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-
-
additional information
?
-
enzyme cleaves alpha1->4 glycosidic linkages and adds the released glucose moieties one by one to the non-reducing end of growing linear alpha-glucan chains via alpha1->6 glycosidic linkages (alpha1->4 to alpha1->6 transfer activity). It converts pure maltooligosaccharide substrates into linear alpha-glucan product mixtures with about 50% alpha1->6 glycosidic bonds (isomalto/maltooligosaccharides). Largest products synthesized from maltoheptaose have a degree of polymerizatition bleow 50
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additional information
?
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enzyme is a alpha-glucanotransferase enzyme with disproportionating (cleaving alpha1->4 and synthesizing alpha1->6 and alpha1->4 glycosidic linkages) and alpha1->6 polymerizing types of activity on maltotetraose and larger maltooligosaccharide substrates. Only linear products are made and with increasing degrees of polymerization, more alpha1->6 glycosidic linkages are introduced into the final products, ranging from 18% in the incubation mixture to 33% in an enriched fraction. In view of its primary structure, GTFB is a member of the glycoside hydrolase 70 family. The GTFB enzyme reaction and product specificities, however, resemble those of the GH13 alpha-amylase type of enzymes
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additional information
?
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enzyme is a alpha-glucanotransferase enzyme with disproportionating (cleaving alpha1->4 and synthesizing alpha1->6 and alpha1->4 glycosidic linkages) and alpha1->6 polymerizing types of activity on maltotetraose and larger maltooligosaccharide substrates. Only linear products are made and with increasing degrees of polymerization, more alpha1->6 glycosidic linkages are introduced into the final products, ranging from 18% in the incubation mixture to 33% in an enriched fraction. In view of its primary structure, GTFB is a member of the glycoside hydrolase 70 family. The GTFB enzyme reaction and product specificities, however, resemble those of the GH13 alpha-amylase type of enzymes
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additional information
?
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no substrates: maltose, maltotriose, sucrose, turanose and palatinose, raffinose, panose, DP5 and DP6 isomaltooligosaccharides
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-
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additional information
?
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no substrates: maltose, maltotriose, sucrose, turanose and palatinose, raffinose, panose, DP5 and DP6 isomaltooligosaccharides
-
-
-
additional information
?
-
-
the enzyme is unable to use sucrose as a donor substrate and is inactive with the sucrose analogs turanose and palatinose, with raffinose, with the DP5 and DP6 isomaltooligosaccharides and with panose
-
-
-
additional information
?
-
enzyme cleaves alpha1->4 glycosidic linkages and adds the released glucose moieties one by one to the non-reducing end of growing linear alpha-glucan chains via alpha1->6 glycosidic linkages (alpha1->4 to alpha1->6 transfer activity). It converts pure maltooligosaccharide substrates into linear alpha-glucan product mixtures with about 50% alpha1->6 glycosidic bonds (isomalto/maltooligosaccharides). Largest products synthesized from maltoheptaose have a degree of polymerizatition bleow 50
-
-
-
additional information
?
-
enzyme cleaves alpha1->4 glycosidic linkages and adds the released glucose moieties one by one to the non-reducing end of growing linear alpha-glucan chains via alpha1->6 glycosidic linkages (alpha1->4 to alpha1->6 transfer activity). It converts pure maltooligosaccharide substrates into linear alpha-glucan product mixtures with about 50% alpha1->6 glycosidic bonds (isomalto/maltooligosaccharides). Largest products synthesized from maltoheptaose have a degree of polymerizatition bleow 50
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
1 mM, hydrolysis reaction increases to 111%, transfer reaction to 422% of initial value, respectively
EDTA
-
1 mM, 25% inhibition of hydrolysis reaction, transfer reaction increases to 388%
Fe2+
-
1 mM, 50% inhibition of hydrolysis reaction, transfer reaction increases to 175%
K+
-
1 mM, 14% inhibition of hydrolysis reaction, transfer reaction to 435% of initial value, respectively
Mg2+
-
1 mM, 6% inhibition of hydrolysis reaction, transfer reaction increases to 378% of initial value, respectively
Mn2+
-
1 mM, hydrolysis reaction increases to 125%, transfer reaction to 425% of initial value, respectively
Na+
-
1 mM, hydrolysis reaction increases to 118%, transfer reaction to 404% of initial value, respectively
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Cu2+
-
1 mM, 49% inhibition of hydrolysis reaction, complete inhibition of transfer reaction
EDTA
-
1 mM, 25% inhibition of hydrolysis reaction, transfer reaction increases to 388%
Fe2+
-
1 mM, 50% inhibition of hydrolysis reaction, transfer reaction increases to 175%
Fe3+
-
1 mM, 65% inhibition of hydrolysis reaction, 15% inhibition of transfer reaction
K+
-
1 mM, 14% inhibition of hydrolysis reaction, transfer reaction to 435% of initial value, respectively
Mg2+
-
1 mM, 6% inhibition of hydrolysis reaction, transfer reaction increases to 378% of initial value, respectively
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
amylose V
-
Km value for hydrolysis reaction 0.5 g/l, for transfer reaction 0.69 g/l, pH 5.0, 55°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
amylose V
Lactobacillus reuteri
-
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, 55°C
210492
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.7
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of N-terminally truncated variant, in Escherichia coli; expression of N-terminally truncated variant, in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D1015N
additional information
-
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
D1015N
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mutant enzyme shows no activity on maltooligosaccharides (maltose to maltoheptaose); mutation in putative nucleophile, mutant shows no activity on maltooligosaccharides
D1015N
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mutant enzyme shows no activity on maltooligosaccharides (maltose to maltoheptaose)
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LINKS TO OTHER DATABASES (specific for EC-Number 2.4.1.B34)
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