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Information on EC 2.4.1.394 - 4,6-alpha-glucanotransferase (linear substrates/linear products)
for references in articles please use BRENDA:EC2.4.1.394
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EC Tree 2 Transferases
2.4 Glycosyltransferases
2.4.1 Hexosyltransferases
2.4.1.394 4,6-alpha-glucanotransferase (linear substrates/linear products)
IUBMB Comments
The enzyme, originally discovered in lactic acid bacteria but later found in other organisms, is similar to EC 2.4.1.395, reuteransucrase, yet is not able to act on sucrose. The enzyme, which belongs to the glycoside hydrolase 70 (GH70) family, possesses both hydrolase and transglycosylase activities, cleaving α(1→4) linkages from the non-reducing end of linear maltooligosaccharides and synthesizing linear α(1→6)-glucan chains. It also possesses an endo-α(1→4)-glycosidase activity. Due to its narrow binding groove, it is not able to act on branched substrates. cf. EC 2.4.1.396, 4,6-α-glucanotransferase (linear and branched substrates, branched products).
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showThe enzyme uses maltooligosaccharides as donor and acceptor substrates. It cleaves alpha1->4 glucosidic bonds and synthesizes 1->6 and 1->4 glucosidic linkages.
formation of a linear isomalto/malto-polysaccharide from linear malto-oligosaccharides
Synonyms
(1->4)-alpha-D-glucan:(1->4),(1->6)-alpha-D-glucan alpha-glucanotransferase, 4, 6-alpha-glucanotransferase, 4,6 alpha-glucanotransferase, 4,6,-alpha-GT, 4,6-alpha-glucanotransferase, 4,6-alpha-glucanotransferase GtfB, 4,6-alpha-GT, 4,6-alpha-GTase, 4,6-alphaGT, Achr_35950, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(1->4)-alpha-D-glucan:(1->4),(1->6)-alpha-D-glucan alpha-glucanotransferase
4, 6-alpha-glucanotransferase
4,6 alpha-glucanotransferase
4,6,-alpha-GT
4,6-alpha-glucanotransferase
4,6-alpha-glucanotransferase GtfB
4,6-alpha-GT
4,6-alpha-GTase
4,6-alphaGT
Achr_35950
Exig_2648
GflML4
GH70 GtfC-like 4,6-alpha-glucanotransferase
Gtf106b
GtfB
GTFB protein
GTFB-like 4,6-alpha-glucanotransferase
GtfB-like 4,6-alpha-glucanotransferases
GTFB-like 4,6-alpha-GT
GTFC
GTFC-like 4,6-alpha-glucanotransferase
GTFC-like 4,6-alpha-GT
GtfD
GtfML4
GtfW
GtfX
GtfY
Lr 121 GtfB
Lreu_1346
UDP-N-acetylglucosamine-peptide N-acetylglucosaminyltransferase stabilizing protein
(1->4)-alpha-D-glucan:(1->4),(1->6)-alpha-D-glucan alpha-glucanotransferase
-
-
(1->4)-alpha-D-glucan:(1->4),(1->6)-alpha-D-glucan alpha-glucanotransferase
-
-
-
(1->4)-alpha-D-glucan:(1->4),(1->6)-alpha-D-glucan alpha-glucanotransferase
-
-
-
4,6-alpha-glucanotransferase
-
-
GtfB
-
-
ambiguous, gene name
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GtfB
-
-
GTFC
-
-
-
-
UDP-N-acetylglucosamine-peptide N-acetylglucosaminyltransferase stabilizing protein
UniProt
UDP-N-acetylglucosamine-peptide N-acetylglucosaminyltransferase stabilizing protein
UniProt
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
formation of a linear isomalto/malto-polysaccharide from linear malto-oligosaccharides
-
-
-
-
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
linear (1->4)-alpha-D-glucan:(1->4)/(1->6)-alpha-D-glucan 6-alpha-D-glucosyltransferase
The enzyme, originally discovered in lactic acid bacteria but later found in other organisms, is similar to EC 2.4.1.395, reuteransucrase, yet is not able to act on sucrose. The enzyme, which belongs to the glycoside hydrolase 70 (GH70) family, possesses both hydrolase and transglycosylase activities, cleaving alpha(1->4) linkages from the non-reducing end of linear maltooligosaccharides and synthesizing linear alpha(1->6)-glucan chains. It also possesses an endo-alpha(1->4)-glycosidase activity. Due to its narrow binding groove, it is not able to act on branched substrates. cf. EC 2.4.1.396, 4,6-alpha-glucanotransferase (linear and branched substrates, branched products).
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
amylose V
D-glucose + maltose
Substrates: low activity
Products: -
Products: -
?
amylose V
maltose + maltotriose
-
Substrates: the enzyme cleaves off predominantly maltose units from amylose, attaching them with an (alpha1->6)-linkage to acceptor substrates, yielding a unique polymer with alternating (alpha1->6)/(alpha1->4)-linked glucose units but without branches
Products: -
Products: -
?
amylose V + maltoheptaose
?
-
Substrates: transglycosylation activity
Products: -
Products: -
?
amylose V + maltohexaose
?
-
Substrates: transglycosylation activity
Products: -
Products: -
?
amylose V + maltopentaose
?
-
Substrates: transglycosylation activity
Products: -
Products: -
?
amylose V + maltotetraose
?
-
Substrates: transglycosylation activity
Products: -
Products: -
?
amylose V + maltotriose
?
-
Substrates: transglycosylation activity
Products: -
Products: -
?
malto-oligosaccharide
?
Substrates: the N-terminally truncated enzyme can only use maltooligosaccharides with a degree of polymerizaion above 2. When malto-oligosaccharides with a degree of polymerizaion of above 4 are used as the substrate, polymer with high degree of polymerizaion is formed by transglycosylation
Products: -
Products: -
?
maltodextrin + H2O
?
Substrates: i.e. short-chain alpha1->4-linked maltodextrins
Products: -
Products: -
?
maltohexaose + H2O
?
-
Substrates: hydrolytic activity
Products: -
Products: -
?
maltohexaose + H2O
D-glucose + maltopentaose
Substrates: -
Products: 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%
Products: 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
D-glucose + maltotetraose
Substrates: with 43 mM of maltopentaose as substrate, the initial rate of glucose formation is 56% of that of maltotetraose formation, showing that the enzyme is rather hydrolytic at the start of the reaction. However, when reaction products start to accumulate, transglycosylation becomes more efficient
Products: -
Products: -
?
maltopentaose
maltotetraose + a DP6 compound
Substrates: -
Products: -
Products: -
?
maltopentaose + H2O
D-glucose + maltotetraose
Substrates: -
Products: 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%
Products: 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%
?
starch + acceptor
?
-
Substrates: transglycosylation activity
Products: -
Products: -
?
amylopectin
?
-
Substrates: the segments from the reducing end to the nearest branch point in amylopectin act as donor substrates
Products: -
Products: -
?
amylopectin
?
-
Substrates: the segments from the reducing end to the nearest branch point in amylopectin act as donor substrates
Products: -
Products: -
?
amylopectin + acceptor
?
-
Substrates: transglycosylation activity
Products: -
Products: -
?
amylopectin + acceptor
?
-
Substrates: transglycosylation activity
Products: -
Products: -
?
amylopectin + H2O
?
-
Substrates: hydrolytic activity
Products: -
Products: -
?
amylopectin + H2O
?
-
Substrates: hydrolytic activity
Products: -
Products: -
?
amylopectin + H2O
?
-
Substrates: hydrolytic activity
Products: -
Products: -
?
amylopectin + H2O
?
-
Substrates: hydrolytic activity
Products: -
Products: -
?
amylose
isomalto-/maltopolysaccharides
Substrates: -
Products: -
Products: -
?
amylose
isomalto-/maltopolysaccharides
Substrates: -
Products: -
Products: -
?
amylose
linear isomalto-/maltopolysaccharides
Substrates: the enzyme cleaves (alpha1->4)-linkages in amylose and introduces (alpha1->6)-linkages
Products: -
Products: -
?
amylose
linear isomalto-/maltopolysaccharides
Substrates: the enzyme cleaves (alpha1->4)-linkages in amylose and introduces (alpha1->6)-linkages
Products: -
Products: -
?
amylose
linear isomalto/malto polysaccharide
Substrates: the enzyme synthesizes linear isomalto/malto polysaccharides having (alpha1->6) linkages attached to the nonreducing ends of (alpha1->4) linked maltose oligosaccharide segments using starch or maltodextrin as a substrate
Products: -
Products: -
?
amylose
linear isomalto/malto polysaccharide
Substrates: the enzyme synthesizes linear isomalto/malto polysaccharides having (alpha1->6) linkages attached to the nonreducing ends of (alpha1->4) linked maltose oligosaccharide segments using starch or maltodextrin as a substrate
Products: -
Products: -
?
amylose + maltose
maltotriose + panose
Substrates: the enzyme synthesizes larger saccharides with alpha1->4 and alpha1->6 glucosidic linkages
Products: panose i.e. Glc-alpha-(1->6)-maltose
Products: panose i.e. Glc-alpha-(1->6)-maltose
?
amylose + maltose
maltotriose + panose
-
Substrates: the enzyme synthesizes larger saccharides with alpha1->4 and alpha1->6 glucosidic linkages
Products: panose i.e. Glc-alpha-(1->6)-maltose
Products: panose i.e. Glc-alpha-(1->6)-maltose
?
amylose + maltose
maltotriose + panose
-
Substrates: the enzyme synthesizes larger saccharides with alpha1->4 and alpha1->6 glucosidic linkages
Products: panose i.e. Glc-alpha-(1->6)-maltose
Products: panose i.e. Glc-alpha-(1->6)-maltose
?
amylose V
?
Substrates: -
Products: GtfB produces a high molecular mass polymer with a molecular mass about 80 times greater than that of the starting amylose V
Products: GtfB produces a high molecular mass polymer with a molecular mass about 80 times greater than that of the starting amylose V
?
amylose V
?
Substrates: -
Products: GtfB produces a high molecular mass polymer with a molecular mass about 80 times greater than that of the starting amylose V
Products: GtfB produces a high molecular mass polymer with a molecular mass about 80 times greater than that of the starting amylose V
?
amylose V
isomalto-/maltopolysaccharide
-
Substrates: the enzyme converts amylose V to isomalto-/maltopolysaccharide with low molecular mass (3.1 kDa) containing 72% alpha(1-6) glycosidic bonds
Products: -
Products: -
?
amylose V
isomalto-/maltopolysaccharide
Substrates: the low molecular mass isomalto-/maltopolysaccharide product of the N-terminally truncated enzyme (GtfBDELTAN) contains 72% alpha(1->6) glycosidic bonds. It is approximately of 3.1 kDa and has 64% indigestible content
Products: -
Products: -
?
amylose V
isomalto-/maltopolysaccharide
Limosilactobacillus fermentum NCC 3057
-
Substrates: the enzyme converts amylose V to isomalto-/maltopolysaccharide with low molecular mass (3.1 kDa) containing 72% alpha(1-6) glycosidic bonds
Products: -
Products: -
?
amylose V + acceptor
?
-
Substrates: transglycosylation activity
Products: -
Products: -
?
amylose V + acceptor
?
-
Substrates: transglycosylation activity
Products: -
Products: -
?
amylose V + H2O
?
-
Substrates: hydrolytic activity
Products: -
Products: -
?
amylose V + H2O
?
Substrates: -
Products: 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
Products: 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 + H2O
?
Substrates: hydrolytic activity, amylose V with Mw 170 kDa
Products: -
Products: -
?
amylose V + H2O
?
Substrates: hydrolytic activity, amylose V with Mw 170 kDa
Products: -
Products: -
?
amylose V + H2O
?
-
Substrates: hydrolytic activity
Products: -
Products: -
?
amylose V + maltose
?
Substrates: transglycosylation activity, amylose V with 170 kDa
Products: -
Products: -
?
amylose V + maltose
?
Substrates: transglycosylation activity, amylose V with 170 kDa
Products: -
Products: -
?
amylose V + maltose
maltotriose + maltotetraose + ?
Substrates: -
Products: -
Products: -
?
amylose V + maltose
maltotriose + maltotetraose + ?
Substrates: -
Products: -
Products: -
?
linear maltooligosaccharide
?
-
Substrates: -
Products: -
Products: -
?
linear maltooligosaccharide
?
-
Substrates: -
Products: -
Products: -
?
linear maltooligosaccharides
isomalto-/maltooligosaccharides
Substrates: the 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
Products: -
Products: -
?
linear maltooligosaccharides
isomalto-/maltooligosaccharides
Substrates: the 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
Products: -
Products: -
?
linear maltooligosaccharides
isomalto-/maltooligosaccharides
Substrates: the 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
Products: -
Products: -
?
linear maltooligosaccharides
linear isomalto-/maltooligomers
-
Substrates: the enzyme acts on maltooligosaccharides, thereby yielding elongated gluco-oligomers/polymers containing besides (alpha1->4) also (alpha1->6) glycosidic linkages
Products: -
Products: -
?
linear maltooligosaccharides
linear isomalto-/maltooligomers
-
Substrates: the enzyme acts on maltooligosaccharides, thereby yielding elongated gluco-oligomers/polymers containing besides (alpha1->4) also (alpha1->6) glycosidic linkages
Products: -
Products: -
?
linear maltooligosaccharides
linear isomalto-/maltooligosaccharides
Substrates: -
Products: -
Products: -
?
linear maltooligosaccharides
linear isomalto-/maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltodextrin
linear isomalto-/maltopolysaccharides
Substrates: -
Products: -
Products: -
?
maltodextrin
linear isomalto-/maltopolysaccharides
Substrates: -
Products: -
Products: -
?
maltodextrin
linear isomalto/malto polysaccharide
Substrates: the enzyme synthesizes linear isomalto/malto polysaccharides having (alpha1->6) linkages attached to the nonreducing ends of (alpha1->4) linked maltose oligosaccharide segments using starch or maltodextrin as a substrate
Products: -
Products: -
?
maltodextrin
linear isomalto/malto polysaccharide
Substrates: the enzyme synthesizes linear isomalto/malto polysaccharides having (alpha1->6) linkages attached to the nonreducing ends of (alpha1->4) linked maltose oligosaccharide segments using starch or maltodextrin as a substrate
Products: -
Products: -
?
Maltoheptaose
?
Substrates: when maltoheptaose is used as a substrate, the first clear products of the reaction are D-glucose, maltotriose (G3), and maltohexaose. Besides, small peaks at retention times longer than that of the donor are detected that did not fit with maltooligosaccharides retention times and that probably correspond to oligosaccharides containing alpha1->6 linkages. The release of G3 at the beginning of the reaction suggests that the enzyme has an additional endo-alpha1->4-glycosidase activity, being able to cleave off not only the non-reducing glucose unit but also a maltotetraosyl unit and transfer it to another glucan chain. Later, oligosaccharides with degrees of polymerization (DPs) higher than that of the starting donor start to accumulate. Besides D-glucose and maltooligosaccharides with DP2 to DP7, peaks corresponding to isomaltose, isomaltotriose, and panose are identified, confirming the ability of the enzyme to synthesize alpha1->6 linkages
Products: -
Products: -
?
Maltoheptaose
?
Substrates: 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
Products: -
Products: -
?
Maltoheptaose
?
-
Substrates: 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
Products: -
Products: -
?
Maltoheptaose
?
-
Substrates: 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
Products: -
Products: -
?
maltoheptaose + H2O
?
-
Substrates: hydrolytic activity
Products: -
Products: -
?
maltoheptaose + H2O
D-glucose + ?
-
Substrates: -
Products: -
Products: -
?
maltoheptaose + H2O
D-glucose + maltotriose + maltohexaose
Substrates: -
Products: first clear products of the reaction
Products: first clear products of the reaction
?
maltoheptaose + H2O
D-glucose + maltotriose + maltohexaose
Exiguobacterium artemiae DSM 17290
Substrates: -
Products: first clear products of the reaction
Products: first clear products of the reaction
?
maltooligosaccharide
?
Substrates: 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
Products: -
Products: -
?
maltooligosaccharide
?
-
Substrates: 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
Products: -
Products: -
?
maltooligosaccharide
?
-
Substrates: 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
Products: -
Products: -
?
maltooligosaccharide
isomalto-/maltopolysaccharide
-
Substrates: -
Products: -
Products: -
?
maltooligosaccharide
isomalto-/maltopolysaccharide
-
Substrates: -
Products: -
Products: -
?
maltopentaose
?
Substrates: -
Products: -
Products: -
?
maltopentaose + H2O
?
-
Substrates: hydrolytic activity
Products: -
Products: -
?
maltopentaose + H2O
?
-
Substrates: hydrolytic activity
Products: -
Products: -
?
maltose
D-glucose
Substrates: very low activity
Products: -
Products: -
?
maltose
D-glucose
Substrates: very low activity
Products: -
Products: -
?
maltose
D-glucose
Substrates: very low activity
Products: -
Products: -
?
Maltotetraose
?
-
Substrates: minor activity with maltotetraose
Products: -
Products: -
?
Maltotetraose
?
Substrates: the enzyme has 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
Products: -
Products: -
?
maltotetraose + H2O
?
-
Substrates: hydrolytic activity
Products: -
Products: -
?
maltotetraose + H2O
?
-
Substrates: hydrolytic activity
Products: -
Products: -
?
maltotetraose + H2O
D-glucose + maltotetraose
Substrates: -
Products: 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
Products: 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
Substrates: -
Products: 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
Products: 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
Substrates: -
Products: 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
Products: 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
?
maltotriose + H2O
?
-
Substrates: hydrolytic activity
Products: -
Products: -
?
maltotriose + H2O
?
-
Substrates: hydrolytic activity
Products: -
Products: -
?
starch
?
-
Substrates: the enzyme modifies starch by cleaving (alpha1->4) linkages and introducing non-branched (alpha1->6) linkages to produce functional starch derivatives
Products: -
Products: -
?
starch
?
-
Substrates: the enzyme modifies starch by cleaving (alpha1->4) linkages and introducing non-branched (alpha1->6) linkages to produce functional starch derivatives
Products: -
Products: -
?
starch
isomalto-/maltopolysaccharides
Substrates: -
Products: -
Products: -
?
starch
isomalto-/maltopolysaccharides
-
Substrates: -
Products: -
Products: -
?
starch
linear isomalto-/maltopolysaccharides
Substrates: -
Products: -
Products: -
?
starch
linear isomalto-/maltopolysaccharides
Substrates: -
Products: -
Products: -
?
starch
linear isomalto/malto polysaccharide
Substrates: the enzyme synthesizes linear isomalto/malto polysaccharides having (alpha1->6) linkages attached to the nonreducing ends of (alpha1->4) linked maltose oligosaccharide segments using starch or maltodextrin as a substrate
Products: -
Products: -
?
starch
linear isomalto/malto polysaccharide
Substrates: the enzyme synthesizes linear isomalto/malto polysaccharides having (alpha1->6) linkages attached to the nonreducing ends of (alpha1->4) linked maltose oligosaccharide segments using starch or maltodextrin as a substrate
Products: -
Products: -
?
starch + H2O
?
-
Substrates: hydrolytic activity
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: inactive on sucrose, panose, nigerose, beta-cyclodextrins, and isomalto-oligosaccharides with degree of polymerzation of 2, 3, and 5
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: inactive on sucrose, panose, nigerose, beta-cyclodextrins, and isomalto-oligosaccharides with degree of polymerzation of 2, 3, and 5
Products: -
Products: -
?
additional information
?
-
-
Substrates: similar to the GTFBlike 4,6-alpha-GTs, GTFC catalyzes cleavage of alpha(1->4) glycosidic linkages and synthesis of consecutive alpha(1->6) linkages. GTFC differs from GTFB in converting amylose/starch substrates into isomalto-/malto-oligosaccharides (IMMO), instead of the (modified) polymers (IMMP) synthesized by GTFB
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additional information
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Substrates: 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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Substrates: 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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Substrates: similar to the GTFBlike 4,6-alpha-GTs, GTFC catalyzes cleavage of alpha(1->4) glycosidic linkages and synthesis of consecutive alpha(1->6) linkages. GTFC differs from GTFB in converting amylose/starch substrates into isomalto-/malto-oligosaccharides (IMMO), instead of the (modified) polymers (IMMP) synthesized by GTFB
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additional information
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Substrates: the enzyme is inactive with sucrose, nigerose, panose, reuteran, isomaltobiose, isomaltotriose, isomaltopentaose, maltose or maltotriose
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additional information
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Substrates: the enzyme is inactive with sucrose, nigerose, panose, reuteran, isomaltobiose, isomaltotriose, isomaltopentaose, maltose or maltotriose
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additional information
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Substrates: similar to the GTFBlike 4,6-alpha-GTs, GTFC catalyzes cleavage of alpha(1->4) glycosidic linkages and synthesis of consecutive alpha(1->6) linkages. GTFC differs from GTFB in converting amylose/starch substrates into isomalto-/malto-oligosaccharides (IMMO), instead of the (modified) polymers (IMMP) synthesized by GTFB
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additional information
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Substrates: the enzyme is inactive with sucrose, nigerose, panose, reuteran, isomaltobiose, isomaltotriose, isomaltopentaose, maltose or maltotriose
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additional information
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Substrates: similar to the GTFBlike 4,6-alpha-GTs, GTFC catalyzes cleavage of alpha(1->4) glycosidic linkages and synthesis of consecutive alpha(1->6) linkages. GTFC differs from GTFB in converting amylose/starch substrates into isomalto-/malto-oligosaccharides (IMMO), instead of the (modified) polymers (IMMP) synthesized by GTFB
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additional information
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Substrates: GTFB predominantly cleaves an alpha(1->4) glycosidic linkage from the non-reducing end of the donor substrate [alpha(1->4)-glucan] and transfers the cleaved glucosyl unit to the non-reducing end of another alpha(1->4)-glucan acceptor substrate, forming mainly alpha(1->6) linkages. Products formed with an alpha(1->6) linkage at the non-reducing end become better acceptor substrates and are further elongated in a linear manner with alpha(1->6) linked glucosyl units. This results in the formation of isomalto/malto-oligosaccharide and polysaccharide mixtures with increasing percentages of alpha(1->6) linkages. Linkage specificity of GTFB-like 4,6-alpha-GTs, overview
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additional information
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Substrates: mutant GtfX-DELTANDELTAC is inactive on sucrose, panose, nigerose, isomaltose, isomaltotriose, maltose, maltotriose, alpha-cyclodextrin, pullulan and dextran, but shows clear hydrolase/transglycosylase activity on malto-oligosaccharides (MOS) of DP4-7, amylose V, starch, and amylopectin. Substrate specificity of mutant GtfX-DELTANDELTAC, 1HNMR analysis product analysis, and structural analysis of polysaccharides generated by GtfX-DELTANDELTAC from amylose V, overview
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additional information
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Substrates: mutant GtfY-DELTANDELTAC is inactive on sucrose, panose, nigerose, isomaltose, isomaltotriose, maltose, maltotriose, alpha-cyclodextrin, pullulan and dextran, but shows clear hydrolase/transglycosylase activity on malto-oligosaccharides (MOS) of DP4-7, amylose V, starch, and amylopectin. Substrate specificity of mutant GtfY-DELTANDELTAC, 1HNMR analysis product analysis, and structural analysis of polysaccharides generated by GtfY-DELTANDELTAC from amylose V, overview
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additional information
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Substrates: inactive on sucrose, panose, nigerose, isomaltose, isomaltotriose, maltose, maltotriose, alpha-cyclodextrin, pullulan, and dextran
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additional information
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Substrates: inactive with sucrose, D-glucose, nigerose, panose, maltose, isomaltose and isomaltotriose
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additional information
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Substrates: no activity on glucose, sucrose, isomaltose, isomaltotriose, panose, and nigerose substrates
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additional information
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Limosilactobacillus fermentum NCC 3057
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Substrates: inactive with sucrose, D-glucose, nigerose, panose, maltose, isomaltose and isomaltotriose
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additional information
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Substrates: 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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Substrates: 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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Substrates: 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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Substrates: 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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Substrates: no substrates: maltose, maltotriose, sucrose, turanose and palatinose, raffinose, panose, DP5 and DP6 isomaltooligosaccharides
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additional information
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Substrates: no substrates: maltose, maltotriose, sucrose, turanose and palatinose, raffinose, panose, DP5 and DP6 isomaltooligosaccharides
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additional information
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Substrates: 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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Substrates: 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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Substrates: 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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Substrates: structure of the IMMP product of 4,6-alpha-GTase (e.g. GtfB) with maltodextrins, overview. NMR analysis of EPS samples produced by the GtfB enzyme in vitro and by Lactobacillus reuteri 121 cells in vivo. Enzyme reaction product analysis
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additional information
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Substrates: structure of the IMMP product of 4,6-alpha-GTase (e.g. GtfB) with maltodextrins, overview. NMR analysis of EPS samples produced by the GtfB enzyme in vitro and by Lactobacillus reuteri 121 cells in vivo. Enzyme reaction product analysis
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additional information
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Substrates: structure of the IMMP product of 4,6-alpha-GTase GtfW with maltodextrins, overview. Enzyme reaction product analysis
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additional information
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Substrates: structure of the IMMP product of 4,6-alpha-GTase GtfW with maltodextrins, overview. Enzyme reaction product analysis
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additional information
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Substrates: structure of the IMMP product of 4,6-alpha-GTase GtfML4 with maltodextrins, overview. Enzyme reaction product analysis
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additional information
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Substrates: structure of the IMMP product of 4,6-alpha-GTase GtfML4 with maltodextrins, overview. Enzyme reaction product analysis
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additional information
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Substrates: structure of the IMMP product of 4,6-alpha-GTase Gtf106b with maltodextrins, overview. Enzyme reaction product analysis
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additional information
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Substrates: structure of the IMMP product of 4,6-alpha-GTase Gtf106b with maltodextrins, overview. Enzyme reaction product analysis
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additional information
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Substrates: the enzyme performs transglycosylation and/or hydrolytic activity. The linear alpha(1->4)-linked glucose units disappear and linear alpha(1->6)-linked glucose units appear. The total enzyme activity of GtfB-DELTAN-DELTAV is determined by the amylose-iodine staining method. Synthesis of isomalto/malto-polysaccharides (IMMP) from starch. Reaction product analyses, the IMMP product consists of terminal, and 6-substituted glucosyl units, overview. IMMP with 18.3 kDa
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additional information
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Substrates: the enzyme performs transglycosylation and/or hydrolytic activity. The linear alpha(1->4)-linked glucose units disappear and linear alpha(1->6)-linked glucose units appear. The total enzyme activity of GtfB-DELTAN-DELTAV is determined by the amylose-iodine staining method. Synthesis of isomalto/malto-polysaccharides (IMMP) from starch. Reaction product analyses, the IMMP product consists of terminal, and 6-substituted glucosyl units, overview. IMMP with 18.3 kDa
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additional information
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Substrates: malto-oligosaccharide binding structures with wild-type and mutant enzymes, overview
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additional information
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Substrates: malto-oligosaccharide binding structures with wild-type and mutant enzymes, overview
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additional information
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Substrates: GTFB predominantly cleaves an alpha(1->4) glycosidic linkage from the non-reducing end of the donor substrate [alpha(1->4)-glucan] and transfers the cleaved glucosyl unit to the non-reducing end of another alpha(1->4)-glucan acceptor substrate, forming mainly alpha(1->6) linkages. Products formed with an alpha(1->6) linkage at the non-reducing end become better acceptor substrates and are further elongated in a linear manner with alpha(1->6) linked glucosyl units. This results in the formation of isomalto/malto-oligosaccharide and polysaccharide mixtures with increasing percentages of alpha(1->6) linkages. Linkage specificity of GTFB-like 4,6-alpha-GTs, overview
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additional information
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Substrates: the enzyme does not act on sucrose
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additional information
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Substrates: the enzyme catalyzes hydrolysis and alpha(1->4)/alpha(1->6) transglycosylation. The enzyme is unable to use sucrose as substrate
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additional information
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Substrates: the enzyme is inactive on beta-cyclodextrin
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additional information
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Substrates: inactive with sucrose
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additional information
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Substrates: inactive with sucrose
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additional information
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Substrates: inactive with sucrose, turanose, palatinose, raffinose, panose, isomaltopentaose, isomaltohexaose, reuteran, maltose or maltotriose
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additional information
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Substrates: inactive with sucrose, turanose, palatinose, raffinose, panose, isomaltopentaose, isomaltohexaose, reuteran, maltose or maltotriose
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additional information
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Substrates: inactive with sucrose, trehalose, raffinose, 1-kestose, nystose, isomaltose, and isomaltopentaose
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additional information
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Substrates: inactive with sucrose, trehalose, raffinose, 1-kestose, nystose, isomaltose, and isomaltopentaose
Products: -
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additional information
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-
Substrates: inactive with sucrose, trehalose, raffinose, 1-kestose, nystose, isomaltose, and isomaltopentaose
Products: -
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additional information
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-
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Substrates: inactive with sucrose, maltopentaose, and maltohexaose
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additional information
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-
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Substrates: the enzyme demonstrates both hydrolysis and transglycosylase activity by the appearance of lower- and higher-molecular-mass products than the substrate oligosaccharides(-alditols), including polysaccharide products
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additional information
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Substrates: structure of the IMMP product of 4,6-alpha-GTase (e.g. GtfB) with maltodextrins, overview. NMR analysis of EPS samples produced by the GtfB enzyme in vitro and by Lactobacillus reuteri 121 cells in vivo. Enzyme reaction product analysis
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additional information
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Substrates: the enzyme performs transglycosylation and/or hydrolytic activity. The linear alpha(1->4)-linked glucose units disappear and linear alpha(1->6)-linked glucose units appear. The total enzyme activity of GtfB-DELTAN-DELTAV is determined by the amylose-iodine staining method. Synthesis of isomalto/malto-polysaccharides (IMMP) from starch. Reaction product analyses, the IMMP product consists of terminal, and 6-substituted glucosyl units, overview. IMMP with 18.3 kDa
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Products: -
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additional information
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Substrates: the enzyme performs transglycosylation and/or hydrolytic activity. The linear alpha(1->4)-linked glucose units disappear and linear alpha(1->6)-linked glucose units appear. The total enzyme activity of GtfB-DELTAN-DELTAV is determined by the amylose-iodine staining method. Synthesis of isomalto/malto-polysaccharides (IMMP) from starch. Reaction product analyses, the IMMP product consists of terminal, and 6-substituted glucosyl units, overview. IMMP with 18.3 kDa
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additional information
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Substrates: malto-oligosaccharide binding structures with wild-type and mutant enzymes, overview
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additional information
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Substrates: malto-oligosaccharide binding structures with wild-type and mutant enzymes, overview
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additional information
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-
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Substrates: GTFB predominantly cleaves an alpha(1->4) glycosidic linkage from the non-reducing end of the donor substrate [alpha(1->4)-glucan] and transfers the cleaved glucosyl unit to the non-reducing end of another alpha(1->4)-glucan acceptor substrate, forming mainly alpha(1->6) linkages. Products formed with an alpha(1->6) linkage at the non-reducing end become better acceptor substrates and are further elongated in a linear manner with alpha(1->6) linked glucosyl units. This results in the formation of isomalto/malto-oligosaccharide and polysaccharide mixtures with increasing percentages of alpha(1->6) linkages. Linkage specificity of GTFB-like 4,6-alpha-GTs, overview
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additional information
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Substrates: the enzyme does not act on sucrose
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additional information
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Substrates: the enzyme catalyzes hydrolysis and alpha(1->4)/alpha(1->6) transglycosylation. The enzyme is unable to use sucrose as substrate
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additional information
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Substrates: the enzyme is inactive on beta-cyclodextrin
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additional information
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Substrates: 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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Substrates: inactive with sucrose, maltopentaose, and maltohexaose
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additional information
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Substrates: the enzyme demonstrates both hydrolysis and transglycosylase activity by the appearance of lower- and higher-molecular-mass products than the substrate oligosaccharides(-alditols), including polysaccharide products
Products: -
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additional information
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Substrates: 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
Products: -
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additional information
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Substrates: 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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Substrates: 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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Substrates: GTFB predominantly cleaves an alpha(1->4) glycosidic linkage from the non-reducing end of the donor substrate [alpha(1->4)-glucan] and transfers the cleaved glucosyl unit to the non-reducing end of another alpha(1->4)-glucan acceptor substrate, forming mainly alpha(1->6) linkages. Products formed with an alpha(1->6) linkage at the non-reducing end become better acceptor substrates and are further elongated in a linear manner with alpha(1->6) linked glucosyl units. This results in the formation of isomalto/malto-oligosaccharide and polysaccharide mixtures with increasing percentages of alpha(1->6) linkages. Linkage specificity of GTFB-like 4,6-alpha-GTs, overview
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additional information
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-
-
Substrates: inactive with sucrose, trehalose, raffinose, 1-kestose, nystose, isomaltose, and isomaltopentaose
Products: -
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additional information
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Substrates: inactive with sucrose, trehalose, raffinose, 1-kestose, nystose, isomaltose, and isomaltopentaose
Products: -
Products: -
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additional information
?
-
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Substrates: structure of the IMMP product of 4,6-alpha-GTase GtfW with maltodextrins, overview. Enzyme reaction product analysis
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additional information
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Substrates: structure of the IMMP product of 4,6-alpha-GTase GtfML4 with maltodextrins, overview. Enzyme reaction product analysis
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additional information
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Substrates: structure of the IMMP product of 4,6-alpha-GTase Gtf106b with maltodextrins, overview. Enzyme reaction product analysis
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additional information
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Limosilactobacillus reuteri LMG 18388
Substrates: structure of the IMMP product of 4,6-alpha-GTase (e.g. GtfB) with maltodextrins, overview. NMR analysis of EPS samples produced by the GtfB enzyme in vitro and by Lactobacillus reuteri 121 cells in vivo. Enzyme reaction product analysis
Products: -
Products: -
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additional information
?
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Substrates: 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
Products: -
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additional information
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Substrates: 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
Products: -
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additional information
?
-
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Substrates: structure of the IMMP product of 4,6-alpha-GTase GtfW with maltodextrins, overview. Enzyme reaction product analysis
Products: -
Products: -
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additional information
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Substrates: structure of the IMMP product of 4,6-alpha-GTase GtfML4 with maltodextrins, overview. Enzyme reaction product analysis
Products: -
Products: -
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additional information
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Substrates: structure of the IMMP product of 4,6-alpha-GTase Gtf106b with maltodextrins, overview. Enzyme reaction product analysis
Products: -
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additional information
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-
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Substrates: GTFB predominantly cleaves an alpha(1->4) glycosidic linkage from the non-reducing end of the donor substrate [alpha(1->4)-glucan] and transfers the cleaved glucosyl unit to the non-reducing end of another alpha(1->4)-glucan acceptor substrate, forming mainly alpha(1->6) linkages. Products formed with an alpha(1->6) linkage at the non-reducing end become better acceptor substrates and are further elongated in a linear manner with alpha(1->6) linked glucosyl units. This results in the formation of isomalto/malto-oligosaccharide and polysaccharide mixtures with increasing percentages of alpha(1->6) linkages. Linkage specificity of GTFB-like 4,6-alpha-GTs, overview
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additional information
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Substrates: inactive with sucrose, trehalose, raffinose, 1-kestose, nystose, isomaltose, and isomaltopentaose
Products: -
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additional information
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-
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Substrates: inactive with sucrose, trehalose, raffinose, 1-kestose, nystose, isomaltose, and isomaltopentaose
Products: -
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additional information
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Limosilactobacillus reuteri TMW1.106
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Substrates: structure of the IMMP product of 4,6-alpha-GTase GtfW with maltodextrins, overview. Enzyme reaction product analysis
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additional information
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Limosilactobacillus reuteri TMW1.106
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Substrates: structure of the IMMP product of 4,6-alpha-GTase GtfML4 with maltodextrins, overview. Enzyme reaction product analysis
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additional information
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Limosilactobacillus reuteri TMW1.106
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Substrates: structure of the IMMP product of 4,6-alpha-GTase Gtf106b with maltodextrins, overview. Enzyme reaction product analysis
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additional information
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Substrates: the enzyme GtfD shows both hydrolysis and transglycosylase (disproportionation) activity. 1HNMR analysis of the product mixture generated from amylose V reveals the presence of two broad anomeric signals corresponding to the (alpha1->4) and the newly formed (alpha1->6) linkages. Substrate specificity with maltooligosaccharides, overview. The Paenibacillus beijingensis GtfD enzyme is inactive on sucrose, panose, nigerose, and isomalto-oligosaccharides with DP2, DP3, and DP5, while the enzyme catalyzes the conversion of malto-oligosaccharides (MOS) of DP3 to 7 showing both hydrolysis and transglycosylase (disproportionation) activity revealing the formation of lower- and higher-molecular-mass products
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additional information
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-
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Substrates: GTFB predominantly cleaves an alpha(1->4) glycosidic linkage from the non-reducing end of the donor substrate [alpha(1->4)-glucan] and transfers the cleaved glucosyl unit to the non-reducing end of another alpha(1->4)-glucan acceptor substrate, forming mainly alpha(1->6) linkages. Products formed with an alpha(1->6) linkage at the non-reducing end become better acceptor substrates and are further elongated in a linear manner with alpha(1-> 6) linked glucosyl units. This results in the formation of isomalto/malto-oligosaccharide and polysaccharide mixtures with increasing percentages of alpha(1->6) linkages. Linkage specificity of GTFB-like 4,6-alpha-GTs, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: purified recombinant truncated GtfB shows transglycosylation activities toward starch, resulting in branch points of alpha(1->6)-glycosidic linkages plus linear chains of alpha(1->4)-glycosidic linkages. GtfB catalyzes the transglycosylation reactions of amylose through cleaving alpha(1->4)-glycosidic linkage and synthesizing alpha(1->6)-glycosidic linkages. Usage of modified wheat starch, after the GtfB-modified wheat starches are gelatinized and stored at 4°C for 1-2 weeks, their endothermic enthalpies are significantly lower than that of the control sample, indicating low retrogradation rates. The GtfB-treated amylose is significantly different from the GtfB-untreated amylose, with more short-branch chains (DP1-4) of alpha(1->4)-glycosidic linkages. Amylose and amylopectin contents of natural and GtfB modified wheat starches, and conformational structure of GtfB-modified wheat starch, overview
Products: -
Products: -
?
additional information
?
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Streptococcus thermophilus NCC2408
-
Substrates: purified recombinant truncated GtfB shows transglycosylation activities toward starch, resulting in branch points of alpha(1->6)-glycosidic linkages plus linear chains of alpha(1->4)-glycosidic linkages. GtfB catalyzes the transglycosylation reactions of amylose through cleaving alpha(1->4)-glycosidic linkage and synthesizing alpha(1->6)-glycosidic linkages. Usage of modified wheat starch, after the GtfB-modified wheat starches are gelatinized and stored at 4°C for 1-2 weeks, their endothermic enthalpies are significantly lower than that of the control sample, indicating low retrogradation rates. The GtfB-treated amylose is significantly different from the GtfB-untreated amylose, with more short-branch chains (DP1-4) of alpha(1->4)-glycosidic linkages. Amylose and amylopectin contents of natural and GtfB modified wheat starches, and conformational structure of GtfB-modified wheat starch, overview
Products: -
Products: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
linear maltooligosaccharide
?
-
Substrates: -
Products: -
Products: -
?
linear maltooligosaccharide
?
-
Substrates: -
Products: -
Products: -
?
linear maltooligosaccharides
isomalto-/maltooligosaccharides
Substrates: the 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
Products: -
Products: -
?
linear maltooligosaccharides
isomalto-/maltooligosaccharides
Substrates: the 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
Products: -
Products: -
?
linear maltooligosaccharides
isomalto-/maltooligosaccharides
Substrates: the 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
Products: -
Products: -
?
linear maltooligosaccharides
linear isomalto-/maltooligomers
-
Substrates: the enzyme acts on maltooligosaccharides, thereby yielding elongated gluco-oligomers/polymers containing besides (alpha1->4) also (alpha1->6) glycosidic linkages
Products: -
Products: -
?
linear maltooligosaccharides
linear isomalto-/maltooligomers
-
Substrates: the enzyme acts on maltooligosaccharides, thereby yielding elongated gluco-oligomers/polymers containing besides (alpha1->4) also (alpha1->6) glycosidic linkages
Products: -
Products: -
?
linear maltooligosaccharides
linear isomalto-/maltooligosaccharides
Substrates: -
Products: -
Products: -
?
linear maltooligosaccharides
linear isomalto-/maltooligosaccharides
-
Substrates: -
Products: -
Products: -
?
maltooligosaccharide
isomalto-/maltopolysaccharide
-
Substrates: -
Products: -
Products: -
?
maltooligosaccharide
isomalto-/maltopolysaccharide
-
Substrates: -
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
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+
Na+
1 mM, hydrolysis reaction increases to 118%, transfer reaction to 404% of initial value, respectively
additional information
Ca2+
Ca2+ slightly activates. 1 mM Ca2+ is used in assay conditions
Ca2+
1 mM, hydrolysis reaction increases to 111%, transfer reaction to 422% of initial value, respectively
Mn2+
1 mM, hydrolysis reaction increases to 125%, transfer reaction to 425% of initial value, respectively
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Cu2+
1 mM, 49% inhibition of hydrolysis reaction, complete inhibition of transfer reaction; strong inhibition
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%; strong inhibition
Fe3+
1 mM, 65% inhibition of hydrolysis reaction, 15% inhibition of transfer reaction; strong inhibition
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
Km: 8.15 mg/ml, pH 5.0, 40°C, wild-type enzyme
additional information
amylose
Km: 7.95 mg/ml, pH 5.0, 40°C, mutant enzyme N1019D
additional information
amylose
Km: 12.35 mg/ml, pH 5.0, 40°C, mutant enzyme N1019H
additional information
amylose
Km: 11.5 mg/ml, pH 5.0, 40°C, mutant enzyme P968Y
additional information
amylose
Km: 11.65 mg/ml, pH 5.0, 40°C, mutant enzyme Y1079S
additional information
amylose
Km: 7.45 mg/ml, pH 5.0, 40°C, mutant enzyme Y1079N
additional information
amylose
Km: 9.55 mg/ml, pH 5.0, 40°C, mutant enzyme N1019R
additional information
amylose
Km: 0.09 mg/ml, pH 5.0, 40°C, mutant enzyme N1019K
additional information
amylose
Km: 3.36 mg/ml, pH 5.0, 40°C, mutant enzyme N1019E
additional information
amylose
Km: 9.18 mg/ml, pH 5.0, 40°C, mutant enzyme N1019S
additional information
amylose
Km: 22.1 mg/ml, pH 5.0, 40°C, mutant enzyme N1019G
additional information
amylose
Km: 18.54 mg/ml, pH 5.0, 40°C, mutant enzyme N1019I
additional information
amylose
Km: 16.67 mg/ml, pH 5.0, 40°C, mutant enzyme N1019T
additional information
amylose
Km: 28.53 mg/ml, pH 5.0, 40°C, mutant enzyme N1019Y
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
-
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
kcat/Km: 4.17 mg/min*ml, pH 5.0, 40°C, wild-type enzyme
additional information
amylose
kcat/Km: 24.78 mg/min*ml, pH 5.0, 40°C, mutant enzyme N1019D
additional information
amylose
kcat/Km: 8.47 mg/min*ml, pH 5.0, 40°C, mutant enzyme N1019H
additional information
amylose
kcat/Km: 3.65 mg/min*ml, pH 5.0, 40°C, mutant enzyme P968Y
additional information
amylose
kcat/Km: 2.84 mg/min*ml, pH 5.0, 40°C, mutant enzyme Y1079S
additional information
amylose
kcat/Km: 3.53 mg/min*ml, pH 5.0, 40°C, mutant enzyme Y1079N
additional information
amylose
kcat/Km: 1.52 mg/min*ml, pH 5.0, 40°C, mutant enzyme N1019R
additional information
amylose
kcat/Km: 23.07 mg/min*ml, pH 5.0, 40°C, mutant enzyme N1019K
additional information
amylose
kcat/Km: 1.28 mg/min*ml, pH 5.0, 40°C, mutant enzyme N1019E
additional information
amylose
kcat/Km: 6.03 mg/min*ml, pH 5.0, 40°C, mutant enzyme N1019S
additional information
amylose
kcat/Km: 3.0 mg/min*ml, pH 5.0, 40°C, mutant enzyme N1019G
additional information
amylose
kcat/Km: 2.32 mg/min*ml, pH 5.0, 40°C, mutant enzyme N1019I
additional information
amylose
kcat/Km: 3.64 mg/min*ml, pH 5.0, 40°C, mutant enzyme N1019T
additional information
amylose
kcat/Km: 1.64 mg/min*ml, pH 5.0, 40°C, mutant enzyme N1019Y
additional information
amylose V
-
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
-
additional information
amylose V
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
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
17.9
-
purified recombinant enzyme mutant GtfX-DELTANDELTAC, pH 4.0, 53°C, substrate 0.125% w/v amylose V
19.6
-
purified recombinant enzyme mutant GtfY-DELTANDELTAC, pH 5.0, 62°C, substrate 0.125% w/v amylose V
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
4.7
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.5 - 5.5
3 - 7
4 - 7.5
4 - 9
pH 4.0: about 40% of maximal activity, pH 9.0: about 45% of maximal activity, N-terminally truncated enzyme (GtfBDELTAN)
4.5 - 6.5
-
less than 10% of maximal activity at pH 4.5 and pH 6.5
5 - 7
-
more than 70% activity at pH 5.0-7.0 in phosphoric acid-citric acid, about 50% activity at pH 8.0, about 40% activity at pH 4.0
2.5 - 5.5
-
enzyme mutant GtfY-DELTANDELTAC shows more than 60% of maximal activity within this pH range
2.5 - 5.5
-
isoform GtfY retains more than 60% of activity from pH 2.5 to 5.5
3 - 7
-
enzyme mutant GtfX-DELTANDELTAC shows more than 60% of maximal activity within this pH range
3 - 7
-
isoform GtfX retains more than 60% of its activity over a pH range from 3.0 to 7.0
4 - 7.5
the enzyme has more than 50% activity over a pH range of 4.0 to 7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
37
40
45
53
55
60
62
45
optimal temperature for mutant enzymes N1019K, N1019S, N1019I
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 50
30 - 55
35 - 50
the enzyme is most active between 35 and 50°C, its activity decreases drastically when the reaction is carried out at 55°C. The enzyme exhibits 30% of its maximum activity when the temperature is decreased to 30°C
58 - 73
30 - 50
30°C: about 70% of maximal activity, 50°C: about 70% of maximal activity, N-terminally truncated enzyme (GtfBDELTAN)
30 - 55
-
enzyme mutant GtfX-DELTANDELTAC shows more than 60% of maximal activity within this temperature range
30 - 55
-
isoform GtfX retains more than 60% of its activity over a temperature range from 30 to 55°C
58 - 73
-
enzyme mutant GtfY-DELTANDELTAC shows more than 90% of maximal activity within this temperature range
58 - 73
-
isoform GtfY retains more than 90% of its activity over a range of temperatures from 58 to 73°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Exiguobacterium artemiae DSM 17290
enzyme GtfC differs in the domain order from dextransucrase and GtfB enzymes, and it completely lacks domain V
UniProt
brenda
enzyme GtfC differs in the domain order from dextransucrase and GtfB enzymes, and it completely lacks domain V
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
additional information
evolution
-
structure-function relationships of family GH70 glucansucrase and 4,6-alpha-glucanotransferase enzymes, and their evolutionary relationships with family GH13 enzymes, phylogenetic analysis, detailed overview. GH70 subfamilies (GTFB- and GTFC-like) are identified as 4,6-alpha-glucanotransferases (4,6-alpha-GTs) that represent evolutionary intermediates between the family GH13 and classical GH70 enzymes. These enzymes are not active on sucrose, instead, they use alpha(1->4) glucans (i.e. malto-oligosaccharides and starch) as substrates to synthesize other alpha-glucans by introducing linear chains of alpha(1->6) linkages. 4,6-alpha-Glucanotransferases, structure comparisons
evolution
-
structure-function relationships of family GH70 glucansucrase and 4,6-alpha-glucanotransferase enzymes, and their evolutionary relationships with family GH13 enzymes, phylogenetic analysis, detailed overview. GH70 subfamilies (GTFB- and GTFC-like) are identified as 4,6-alpha-glucanotransferases (4,6-alpha-GTs) that represent evolutionary intermediates between the family GH13 and classical GH70 enzymes. These enzymes are not active on sucrose, instead, they use alpha(1->4) glucans (i.e. malto-oligosaccharides and starch) as substrates to synthesize other alpha-glucans by introducing linear chains of alpha(1->6) linkages. 4,6-alpha-Glucanotransferases, structure comparisons
evolution
the crystal structure analysis of 4,6-alpha-glucanotransferase supports diet-driven evolution of GH70 enzymes from alpha-amylases in oral bacteria, overview. Mode of action and detailing the structural changes accompanying the proposed evolution of glycoside hydrolase family 70 (GH70). The enzyme belongs to the glycoside hydrolase family 70 (GH70)
evolution
-
structure-function relationships of family GH70 glucansucrase and 4,6-alpha-glucanotransferase enzymes, and their evolutionary relationships with family GH13 enzymes, phylogenetic analysis, detailed overview. GH70 subfamilies (GTFB- and GTFC-like) are identified as 4,6-alpha-glucanotransferases (4,6-alpha-GTs) that represent evolutionary intermediates between the family GH13 and classical GH70 enzymes. These enzymes are not active on sucrose, instead, they use alpha(1->4) glucans (i.e. malto-oligosaccharides and starch) as substrates to synthesize other alpha-glucans by introducing linear chains of alpha(1->6) linkages. The GTFB-like 4,6-alpha-GT enzymes show about 50% amino acid sequence identity with GH70 GSs and clearly belong to family GH70. Primary structure analysis reveals that GTFB-like 4,6-alpha-GTs, like GH70 GSs, have the same domain organization in that domains A, B, C and IV are made up from discontinuous N- and C-terminal stretches of the polypeptide chain, structure comparisons
evolution
-
structure-function relationships of family GH70 glucansucrase and 4,6-alpha-glucanotransferase enzymes, and their evolutionary relationships with family GH13 enzymes, phylogenetic analysis, detailed overview. GH70 subfamilies (GTFB- and GTFC-like) are identified as 4,6-alpha-glucanotransferases (4,6-alpha-GTs) that represent evolutionary intermediates between the family GH13 and classical GH70 enzymes. These enzymes are not active on sucrose, instead, they use alpha(1->4) glucans (i.e. malto-oligosaccharides and starch) as substrates to synthesize other alpha-glucans by introducing linear chains of alpha(1->6) linkages. The GTFB-like 4,6-alpha-GT enzymes show about 50% amino acid sequence identity with GH70 GSs and clearly belong to family GH70. Primary structure analysis reveals that GTFB-like 4,6-alpha-GTs, like GH70 GSs, have the same domain organization in that domains A, B, C and IV are made up from discontinuous N- and C-terminal stretches of the polypeptide chain, structure comparisons. Except for three from Pediococcus strains, GTFB-like 4,6-alpha-GT enzymes are all found within the genus Lactobacillus
evolution
-
structure-function relationships of family GH70 glucansucrase and 4,6-alpha-glucanotransferase enzymes, and their evolutionary relationships with family GH13 enzymes, phylogenetic analysis, detailed overview. GH70 subfamilies (GTFB- and GTFC-like) are identified as 4,6-alpha-glucanotransferases (4,6-alpha-GTs) that represent evolutionary intermediates between the family GH13 and classical GH70 enzymes. These enzymes are not active on sucrose, instead, they use alpha(1->4) glucans (i.e. malto-oligosaccharides and starch) as substrates to synthesize other alpha-glucans by introducing linear chains of alpha(1->6) linkages. The GTFB-like 4,6-alpha-GT enzymes show about 50% amino acid sequence identity with GH70 GSs and clearly belong to family GH70. Primary structure analysis reveals that GTFB-like 4,6-alpha-GTs, like GH70 GSs, have the same domain organization in that domains A, B, C and IV are made up from discontinuous N- and C-terminal stretches of the polypeptide chain, structure comparisons. Except for three from Pediococcus strains, GTFB-like 4,6-alpha-GT enzymes are all found within the genus Lactobacillus
evolution
-
structure-function relationships of family GH70 glucansucrase and 4,6-alpha-glucanotransferase enzymes, and their evolutionary relationships with family GH13 enzymes, phylogenetic analysis, detailed overview. GH70 subfamilies (GTFB- and GTFC-like) are identified as 4,6-alpha-glucanotransferases (4,6-alpha-GTs) that represent evolutionary intermediates between the family GH13 and classical GH70 enzymes. These enzymes are not active on sucrose, instead, they use alpha(1->4) glucans (i.e. malto-oligosaccharides and starch) as substrates to synthesize other alpha-glucans by introducing linear chains of alpha(1->6) linkages. 4,6-alpha-Glucanotransferases, structure comparisons. The GTFC of Exiguobacterium sibiricum strain 255-15 shows that it has a similar activity as GTFB-like 4,6-alpha-GTs, but, like GH13 family enzymes, lacks a permutated (beta/alpha)8 barrel
evolution
-
the phylogenetic tree shows that within the GtfC clade, the Geobacillus 12AMOR1 GtfC is in a rather unique position
evolution
-
the crystal structure analysis of 4,6-alpha-glucanotransferase supports diet-driven evolution of GH70 enzymes from alpha-amylases in oral bacteria, overview. Mode of action and detailing the structural changes accompanying the proposed evolution of glycoside hydrolase family 70 (GH70). The enzyme belongs to the glycoside hydrolase family 70 (GH70)
-
evolution
-
structure-function relationships of family GH70 glucansucrase and 4,6-alpha-glucanotransferase enzymes, and their evolutionary relationships with family GH13 enzymes, phylogenetic analysis, detailed overview. GH70 subfamilies (GTFB- and GTFC-like) are identified as 4,6-alpha-glucanotransferases (4,6-alpha-GTs) that represent evolutionary intermediates between the family GH13 and classical GH70 enzymes. These enzymes are not active on sucrose, instead, they use alpha(1->4) glucans (i.e. malto-oligosaccharides and starch) as substrates to synthesize other alpha-glucans by introducing linear chains of alpha(1->6) linkages. The GTFB-like 4,6-alpha-GT enzymes show about 50% amino acid sequence identity with GH70 GSs and clearly belong to family GH70. Primary structure analysis reveals that GTFB-like 4,6-alpha-GTs, like GH70 GSs, have the same domain organization in that domains A, B, C and IV are made up from discontinuous N- and C-terminal stretches of the polypeptide chain, structure comparisons
-
evolution
-
structure-function relationships of family GH70 glucansucrase and 4,6-alpha-glucanotransferase enzymes, and their evolutionary relationships with family GH13 enzymes, phylogenetic analysis, detailed overview. GH70 subfamilies (GTFB- and GTFC-like) are identified as 4,6-alpha-glucanotransferases (4,6-alpha-GTs) that represent evolutionary intermediates between the family GH13 and classical GH70 enzymes. These enzymes are not active on sucrose, instead, they use alpha(1->4) glucans (i.e. malto-oligosaccharides and starch) as substrates to synthesize other alpha-glucans by introducing linear chains of alpha(1->6) linkages. 4,6-alpha-Glucanotransferases, structure comparisons. The GTFC of Exiguobacterium sibiricum strain 255-15 shows that it has a similar activity as GTFB-like 4,6-alpha-GTs, but, like GH13 family enzymes, lacks a permutated (beta/alpha)8 barrel
-
evolution
-
structure-function relationships of family GH70 glucansucrase and 4,6-alpha-glucanotransferase enzymes, and their evolutionary relationships with family GH13 enzymes, phylogenetic analysis, detailed overview. GH70 subfamilies (GTFB- and GTFC-like) are identified as 4,6-alpha-glucanotransferases (4,6-alpha-GTs) that represent evolutionary intermediates between the family GH13 and classical GH70 enzymes. These enzymes are not active on sucrose, instead, they use alpha(1->4) glucans (i.e. malto-oligosaccharides and starch) as substrates to synthesize other alpha-glucans by introducing linear chains of alpha(1->6) linkages. The GTFB-like 4,6-alpha-GT enzymes show about 50% amino acid sequence identity with GH70 GSs and clearly belong to family GH70. Primary structure analysis reveals that GTFB-like 4,6-alpha-GTs, like GH70 GSs, have the same domain organization in that domains A, B, C and IV are made up from discontinuous N- and C-terminal stretches of the polypeptide chain, structure comparisons
-
evolution
-
structure-function relationships of family GH70 glucansucrase and 4,6-alpha-glucanotransferase enzymes, and their evolutionary relationships with family GH13 enzymes, phylogenetic analysis, detailed overview. GH70 subfamilies (GTFB- and GTFC-like) are identified as 4,6-alpha-glucanotransferases (4,6-alpha-GTs) that represent evolutionary intermediates between the family GH13 and classical GH70 enzymes. These enzymes are not active on sucrose, instead, they use alpha(1->4) glucans (i.e. malto-oligosaccharides and starch) as substrates to synthesize other alpha-glucans by introducing linear chains of alpha(1->6) linkages. The GTFB-like 4,6-alpha-GT enzymes show about 50% amino acid sequence identity with GH70 GSs and clearly belong to family GH70. Primary structure analysis reveals that GTFB-like 4,6-alpha-GTs, like GH70 GSs, have the same domain organization in that domains A, B, C and IV are made up from discontinuous N- and C-terminal stretches of the polypeptide chain, structure comparisons
-
physiological function
Lactobacillus reuteri strain 121 possesses a 4,6-alpha-glucanotransferase (4,6-alpha-GTase) enzyme. Purified 4,6-alpha-GTase GtfB acts on starches (hydrolysates), cleaving alpha(1->4) linkages and synthesizing alpha(1->6) linkages, yielding isomalto-/maltopolysaccharides (IMMP). Lactobacillus reuteri cells with these extracellular, cell-associated 4,6-alpha-GTases synthesize homoexopolysaccharides (EPS, alpha-glucan) from starches (hydrolysates). NMR, SEC, and enzymatic hydrolysis of EPS synthesized by Lactobacillus reuteri srain 121 cells show that the EPS have similar linkage specificities but generally are much bigger in size than IMMP produced by the GtfB enzyme. 4,6-alpha-GTase enzymes are essential for EPS formation by Lactobacillus reuteri in vivo
physiological function
Lactobacillus reuteri strain DSM20016 possesses a 4,6-alpha-glucanotransferase (4,6-alpha-GTase) enzyme. Purified 4,6-alpha-GTase GtfW acts on starches (hydrolysates), cleaving alpha(1->4) linkages and synthesizing alpha(1->6) linkages, yielding isomalto-/maltopolysaccharides (IMMP). Lactobacillus reuteri cells with extracellular, cell-associated 4,6-alpha-GTases synthesize homoexopolysaccharides (EPS, alpha-glucan) from starches (hydrolysates). 4,6-alpha-GTase enzymes are essential for EPS formation by Lactobacillus reuteri in vivo
physiological function
Lactobacillus reuteri strain DSM20016 possesses a 4,6-alpha-glucanotransferase (4,6-alpha-GTase) enzyme. Purified 4,6-alpha-GTase GtfML4 acts on starches (hydrolysates), cleaving alpha(1->4) linkages and synthesizing alpha(1->6) linkages, yielding isomalto-/maltopolysaccharides (IMMP). Lactobacillus reuteri cells with extracellular, cell-associated 4,6-alpha-GTases synthesize homoexopolysaccharides (EPS, alpha-glucan) from starches (hydrolysates). 4,6-alpha-GTase enzymes are essential for EPS formation by Lactobacillus reuteri in vivo
physiological function
Lactobacillus reuteri strain DSM20016 possesses a 4,6-alpha-glucanotransferase (4,6-alpha-GTase) enzyme. Purified 4,6-alpha-GTase Gtf106b acts on starches (hydrolysates), cleaving alpha(1->4) linkages and synthesizing alpha(1->6) linkages, yielding isomalto-/maltopolysaccharides (IMMP). Lactobacillus reuteri cells with extracellular, cell-associated 4,6-alpha-GTases synthesize homoexopolysaccharides (EPS, alpha-glucan) from starches (hydrolysates). 4,6-alpha-GTase enzymes are essential for EPS Fformation by Lactobacillus reuteri in vivo
physiological function
identification of 4,6-alpha-glucanotransferase enzymes of the glycosyl hydrolase (GH) family 70 (GH70) that cleave alpha(1->4)-linkages in amylose and introduce alpha(1->6)-linkages in linear chains. The 4,6-alpha-glucanotransferase of Lactobacillus reuteri strain 121 converts amylose into an isomalto/malto-polysaccharide (IMMP) with 90% alpha(1->6)-linkages
physiological function
4,6-alpha-glucanotransferase from Lactobacillus reuteri strain 121 (GTFB) can convert starch or starch hydrolysates into isomalto/maltopolysaccharides (IMMPs). This enzyme can transfer the non-reducing glucose moiety of an alpha-1,4 glucan chain to the non-reducing end of another alpha-glucan through alpha-1,6 linkages, generating a linear chain with alpha-1,6 linkages. This specific activity makes GTFB an interesting target enzyme for producing distict starches in planta
physiological function
-
Lactobacillus reuteri strain 121 possesses a 4,6-alpha-glucanotransferase (4,6-alpha-GTase) enzyme. Purified 4,6-alpha-GTase GtfB acts on starches (hydrolysates), cleaving alpha(1->4) linkages and synthesizing alpha(1->6) linkages, yielding isomalto-/maltopolysaccharides (IMMP). Lactobacillus reuteri cells with these extracellular, cell-associated 4,6-alpha-GTases synthesize homoexopolysaccharides (EPS, alpha-glucan) from starches (hydrolysates). NMR, SEC, and enzymatic hydrolysis of EPS synthesized by Lactobacillus reuteri srain 121 cells show that the EPS have similar linkage specificities but generally are much bigger in size than IMMP produced by the GtfB enzyme. 4,6-alpha-GTase enzymes are essential for EPS formation by Lactobacillus reuteri in vivo
-
physiological function
-
identification of 4,6-alpha-glucanotransferase enzymes of the glycosyl hydrolase (GH) family 70 (GH70) that cleave alpha(1->4)-linkages in amylose and introduce alpha(1->6)-linkages in linear chains. The 4,6-alpha-glucanotransferase of Lactobacillus reuteri strain 121 converts amylose into an isomalto/malto-polysaccharide (IMMP) with 90% alpha(1->6)-linkages
-
physiological function
-
4,6-alpha-glucanotransferase from Lactobacillus reuteri strain 121 (GTFB) can convert starch or starch hydrolysates into isomalto/maltopolysaccharides (IMMPs). This enzyme can transfer the non-reducing glucose moiety of an alpha-1,4 glucan chain to the non-reducing end of another alpha-glucan through alpha-1,6 linkages, generating a linear chain with alpha-1,6 linkages. This specific activity makes GTFB an interesting target enzyme for producing distict starches in planta
-
physiological function
Limosilactobacillus reuteri TMW1.106
-
Lactobacillus reuteri strain DSM20016 possesses a 4,6-alpha-glucanotransferase (4,6-alpha-GTase) enzyme. Purified 4,6-alpha-GTase GtfW acts on starches (hydrolysates), cleaving alpha(1->4) linkages and synthesizing alpha(1->6) linkages, yielding isomalto-/maltopolysaccharides (IMMP). Lactobacillus reuteri cells with extracellular, cell-associated 4,6-alpha-GTases synthesize homoexopolysaccharides (EPS, alpha-glucan) from starches (hydrolysates). 4,6-alpha-GTase enzymes are essential for EPS formation by Lactobacillus reuteri in vivo
-
physiological function
Limosilactobacillus reuteri TMW1.106
-
Lactobacillus reuteri strain DSM20016 possesses a 4,6-alpha-glucanotransferase (4,6-alpha-GTase) enzyme. Purified 4,6-alpha-GTase GtfML4 acts on starches (hydrolysates), cleaving alpha(1->4) linkages and synthesizing alpha(1->6) linkages, yielding isomalto-/maltopolysaccharides (IMMP). Lactobacillus reuteri cells with extracellular, cell-associated 4,6-alpha-GTases synthesize homoexopolysaccharides (EPS, alpha-glucan) from starches (hydrolysates). 4,6-alpha-GTase enzymes are essential for EPS formation by Lactobacillus reuteri in vivo
-
physiological function
Limosilactobacillus reuteri TMW1.106
-
Lactobacillus reuteri strain DSM20016 possesses a 4,6-alpha-glucanotransferase (4,6-alpha-GTase) enzyme. Purified 4,6-alpha-GTase Gtf106b acts on starches (hydrolysates), cleaving alpha(1->4) linkages and synthesizing alpha(1->6) linkages, yielding isomalto-/maltopolysaccharides (IMMP). Lactobacillus reuteri cells with extracellular, cell-associated 4,6-alpha-GTases synthesize homoexopolysaccharides (EPS, alpha-glucan) from starches (hydrolysates). 4,6-alpha-GTase enzymes are essential for EPS Fformation by Lactobacillus reuteri in vivo
-
physiological function
-
Lactobacillus reuteri strain DSM20016 possesses a 4,6-alpha-glucanotransferase (4,6-alpha-GTase) enzyme. Purified 4,6-alpha-GTase GtfW acts on starches (hydrolysates), cleaving alpha(1->4) linkages and synthesizing alpha(1->6) linkages, yielding isomalto-/maltopolysaccharides (IMMP). Lactobacillus reuteri cells with extracellular, cell-associated 4,6-alpha-GTases synthesize homoexopolysaccharides (EPS, alpha-glucan) from starches (hydrolysates). 4,6-alpha-GTase enzymes are essential for EPS formation by Lactobacillus reuteri in vivo
-
physiological function
-
Lactobacillus reuteri strain DSM20016 possesses a 4,6-alpha-glucanotransferase (4,6-alpha-GTase) enzyme. Purified 4,6-alpha-GTase GtfML4 acts on starches (hydrolysates), cleaving alpha(1->4) linkages and synthesizing alpha(1->6) linkages, yielding isomalto-/maltopolysaccharides (IMMP). Lactobacillus reuteri cells with extracellular, cell-associated 4,6-alpha-GTases synthesize homoexopolysaccharides (EPS, alpha-glucan) from starches (hydrolysates). 4,6-alpha-GTase enzymes are essential for EPS formation by Lactobacillus reuteri in vivo
-
physiological function
-
Lactobacillus reuteri strain DSM20016 possesses a 4,6-alpha-glucanotransferase (4,6-alpha-GTase) enzyme. Purified 4,6-alpha-GTase Gtf106b acts on starches (hydrolysates), cleaving alpha(1->4) linkages and synthesizing alpha(1->6) linkages, yielding isomalto-/maltopolysaccharides (IMMP). Lactobacillus reuteri cells with extracellular, cell-associated 4,6-alpha-GTases synthesize homoexopolysaccharides (EPS, alpha-glucan) from starches (hydrolysates). 4,6-alpha-GTase enzymes are essential for EPS Fformation by Lactobacillus reuteri in vivo
-
physiological function
Limosilactobacillus reuteri LMG 18388
-
Lactobacillus reuteri strain 121 possesses a 4,6-alpha-glucanotransferase (4,6-alpha-GTase) enzyme. Purified 4,6-alpha-GTase GtfB acts on starches (hydrolysates), cleaving alpha(1->4) linkages and synthesizing alpha(1->6) linkages, yielding isomalto-/maltopolysaccharides (IMMP). Lactobacillus reuteri cells with these extracellular, cell-associated 4,6-alpha-GTases synthesize homoexopolysaccharides (EPS, alpha-glucan) from starches (hydrolysates). NMR, SEC, and enzymatic hydrolysis of EPS synthesized by Lactobacillus reuteri srain 121 cells show that the EPS have similar linkage specificities but generally are much bigger in size than IMMP produced by the GtfB enzyme. 4,6-alpha-GTase enzymes are essential for EPS formation by Lactobacillus reuteri in vivo
-
physiological function
-
Lactobacillus reuteri strain DSM20016 possesses a 4,6-alpha-glucanotransferase (4,6-alpha-GTase) enzyme. Purified 4,6-alpha-GTase GtfW acts on starches (hydrolysates), cleaving alpha(1->4) linkages and synthesizing alpha(1->6) linkages, yielding isomalto-/maltopolysaccharides (IMMP). Lactobacillus reuteri cells with extracellular, cell-associated 4,6-alpha-GTases synthesize homoexopolysaccharides (EPS, alpha-glucan) from starches (hydrolysates). 4,6-alpha-GTase enzymes are essential for EPS formation by Lactobacillus reuteri in vivo
-
physiological function
-
Lactobacillus reuteri strain DSM20016 possesses a 4,6-alpha-glucanotransferase (4,6-alpha-GTase) enzyme. Purified 4,6-alpha-GTase GtfML4 acts on starches (hydrolysates), cleaving alpha(1->4) linkages and synthesizing alpha(1->6) linkages, yielding isomalto-/maltopolysaccharides (IMMP). Lactobacillus reuteri cells with extracellular, cell-associated 4,6-alpha-GTases synthesize homoexopolysaccharides (EPS, alpha-glucan) from starches (hydrolysates). 4,6-alpha-GTase enzymes are essential for EPS formation by Lactobacillus reuteri in vivo
-
physiological function
-
Lactobacillus reuteri strain DSM20016 possesses a 4,6-alpha-glucanotransferase (4,6-alpha-GTase) enzyme. Purified 4,6-alpha-GTase Gtf106b acts on starches (hydrolysates), cleaving alpha(1->4) linkages and synthesizing alpha(1->6) linkages, yielding isomalto-/maltopolysaccharides (IMMP). Lactobacillus reuteri cells with extracellular, cell-associated 4,6-alpha-GTases synthesize homoexopolysaccharides (EPS, alpha-glucan) from starches (hydrolysates). 4,6-alpha-GTase enzymes are essential for EPS Fformation by Lactobacillus reuteri in vivo
-
additional information
-
structural modeling of Lactobacillus aviarius subsp. aviarius GtfX, compared to the crystal structure of Lactobacillus reuteri GtfB
additional information
-
structural modeling of Lactobacillus aviarius subsp. aviarius GtfY, compared to the crystal structure of Lactobacillus reuteri GtfB
additional information
structure-function analysis, modeling and docking, overview. Mechanism and mode of action of GtfB in comparison with alpha-amylase and glucansucrase
additional information
structure-function analysis, modeling and docking, overview. Mechanism and mode of action of GtfB in comparison with alpha-amylase and glucansucrase
additional information
-
structure-function analysis, modeling and docking, overview. Mechanism and mode of action of GtfB in comparison with alpha-amylase and glucansucrase
-
additional information
-
structural modeling of Lactobacillus aviarius subsp. aviarius GtfX, compared to the crystal structure of Lactobacillus reuteri GtfB
-
additional information
-
structural modeling of Lactobacillus aviarius subsp. aviarius GtfY, compared to the crystal structure of Lactobacillus reuteri GtfB
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A0C4WTK3_9GAMM
780
1
86953
TrEMBL
-
A0A1Z2RUD1_LIMFE
1047
0
117346
TrEMBL
-
A5VL73_LIMRD
Limosilactobacillus reuteri (strain DSM 20016)
1363
0
154301
TrEMBL
-
B1YMN6_EXIS2
Exiguobacterium sibiricum (strain DSM 17290 / CCUG 55495 / CIP 109462 / JCM 13490 / 255-15)
893
0
99064
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
154000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
?
-
x * 100000, about, recombinant enzyme mutant GtfX-DELTANDELTAC, SDS-PAGE
?
-
x * 100000, about, recombinant enzyme mutant GtfY-DELTANDELTAC, SDS-PAGE
?
-
x * 100000, about, recombinant enzyme mutant GtfX-DELTANDELTAC, SDS-PAGE
-
?
-
x * 100000, about, recombinant enzyme mutant GtfY-DELTANDELTAC, SDS-PAGE
-
?
Limosilactobacillus fermentum NCC 3057
-
x * about 97000, N-terminally truncated enzyme, SDS-PAGE
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 0.1 M imidazole/hydrochloric acid (pH 8.5), 0.2 M calcium acetate, and 10% (w/v) PEG 8000
-
purified recombinant wild-type enzyme in apoform and in complex with maltohexaose, and enzyme mutant D1015N in complex with maltopentaose, crystallized by the hanging-drop vapor diffusion method and a microseeding protocol, X-ray diffraction structre determination and analysis at 1.80-2.19 A resolution, molecular replacement using domains A, B, C, and IV of the crystal structure of Lactobacillus reuteri 180 GTF180-DELTAN (PDB ID 3KLK) as a search model
truncated enzyme bound to maltopentaose or maltohexaose, hanging drop vapor diffusion method
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A473P
-
after heat treatment, the mutant exhibits 1.63fold greater activity than the wild type enzyme
D262P
-
after heat treatment, the mutant exhibits 1.38fold greater activity than the wild type enzyme
D420P
-
after heat treatment, the mutant exhibits 1.45fold greater activity than the wild type enzyme
D474P
-
after heat treatment, the mutant exhibits 1.25fold greater activity than the wild type enzyme
M765L/N839D
-
after heat treatment, the mutant exhibits 1.38fold greater activity than the wild type enzyme
N247P
-
after heat treatment, the mutant exhibits 1.55fold greater activity than the wild type enzyme
T517M/T534P
-
after heat treatment, the mutant exhibits 1.24fold greater activity than the wild type enzyme
Y134V
-
after heat treatment, the mutant exhibits 1.34fold greater activity than the wild type enzyme
Y134V/Y241P/N247P/D420P/A473P/T517M/M765L/ L777P/S813P
-
the activity of the mutant is 2.08fold the activity of the wild type, accompanied by a 5°C higher optimal temperature, a 5.76°C higher melting point (59.46°C), and an 11.95fold longer half-life time
Y241P
-
after heat treatment, the mutant exhibits 1.51fold greater activity than the wild type enzyme
A473P
Limosilactobacillus fermentum NCC 3057
-
after heat treatment, the mutant exhibits 1.63fold greater activity than the wild type enzyme
-
D262P
Limosilactobacillus fermentum NCC 3057
-
after heat treatment, the mutant exhibits 1.38fold greater activity than the wild type enzyme
-
N247P
Limosilactobacillus fermentum NCC 3057
-
after heat treatment, the mutant exhibits 1.55fold greater activity than the wild type enzyme
-
Y134V/Y241P/N247P/D420P/A473P/T517M/M765L/ L777P/S813P
Limosilactobacillus fermentum NCC 3057
-
the activity of the mutant is 2.08fold the activity of the wild type, accompanied by a 5°C higher optimal temperature, a 5.76°C higher melting point (59.46°C), and an 11.95fold longer half-life time
-
Y241P
Limosilactobacillus fermentum NCC 3057
-
after heat treatment, the mutant exhibits 1.51fold greater activity than the wild type enzyme
-
D1015N
H1056G
the mutant shows decreased catalytic efficiency compared to the wild type enzyme. The mutant enzyme shows a 9% decrease in the ratio of (alpha1->6) over (alpha1->4) linkages in maltodextrin-derived products
I1020M
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
K1128
the mutant mainly displays endo-alpha-1,4-glycosidase activity and hydrolyzes the amylose polymer to maltooligosaccharides
N1019D
the mutation does not alter the product specificity, increases the catalytic activity and efficiency by 420% and 590%, respectively, and maintains more than 80% relative activity in the pH 3.5-6.5 interval
N1019H
activity of the mutant increases by 217%, catalytic efficiency increases 2fold
N1019I
mutant enzyme with improved thermostability and decreased enzyme activity
N1019K
mutant enzyme with improved thermostability, mutant enzyme almost loses activity
N1019R
mutant enzyme with improved thermostability, mutant enzyme almost loses activity
N1019S
mutant enzyme with increased transglycosylation activity
N1019Y
Q1126I
the mutant shows considerably improved catalytic efficiency compared to the wild type enzyme. The mutant enzyme shows an 11% increase in the ratio of (alpha1->6) over (alpha1->4) linkages in maltodextrin-derived products
S1057P
the mutant shows considerably improved catalytic efficiency compared to the wild type enzyme
Y1055G
the mutant mainly displays endo-alpha-1,4-glycosidase activity and hydrolyzes the amylose polymer to maltooligosaccharides
D1015N
-
mutant enzyme shows no activity on maltooligosaccharides (maltose to maltoheptaose)
-
H1056G
-
the mutant shows decreased catalytic efficiency compared to the wild type enzyme. The mutant enzyme shows a 9% decrease in the ratio of (alpha1->6) over (alpha1->4) linkages in maltodextrin-derived products
-
I1020M
-
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
-
K1128
-
the mutant mainly displays endo-alpha-1,4-glycosidase activity and hydrolyzes the amylose polymer to maltooligosaccharides
-
N1019D
-
the mutation does not alter the product specificity, increases the catalytic activity and efficiency by 420% and 590%, respectively, and maintains more than 80% relative activity in the pH 3.5-6.5 interval
-
N1019H
-
activity of the mutant increases by 217%, catalytic efficiency increases 2fold
-
Q1126I
-
the mutant shows considerably improved catalytic efficiency compared to the wild type enzyme. The mutant enzyme shows an 11% increase in the ratio of (alpha1->6) over (alpha1->4) linkages in maltodextrin-derived products
-
S1057P
-
the mutant shows considerably improved catalytic efficiency compared to the wild type enzyme
-
Y1055G
-
the mutant mainly displays endo-alpha-1,4-glycosidase activity and hydrolyzes the amylose polymer to maltooligosaccharides
-
D1015N
-
mutant enzyme shows no activity on maltooligosaccharides (maltose to maltoheptaose)
-
additional information
D1015N
mutant enzyme shows no activity on maltooligosaccharides (maltose to maltoheptaose)
D1015N
mutation in putative nucleophile, mutant shows no activity on maltooligosaccharides
additional information
-
construction of deletion mutant GtfX-DELTANDELTAC encoding residues 448-1304, determination of the mutant product specificity, 1HNMR analysis is performed with the product mixtures obtained from MOS DP3-7, amylose V, starch, and amylopectin
additional information
-
construction of deletion mutant GtfY-DELTANDELTAC encoding residues 438-1290, determination of the mutant product specificity, 1HNMR analysis is performed with the product mixtures obtained from MOS DP3-7, amylose V, starch, and amylopectin
additional information
-
construction of deletion mutant GtfX-DELTANDELTAC encoding residues 448-1304, determination of the mutant product specificity, 1HNMR analysis is performed with the product mixtures obtained from MOS DP3-7, amylose V, starch, and amylopectin
-
additional information
-
construction of deletion mutant GtfY-DELTANDELTAC encoding residues 438-1290, determination of the mutant product specificity, 1HNMR analysis is performed with the product mixtures obtained from MOS DP3-7, amylose V, starch, and amylopectin
-
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
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
additional information
-
construction of the GtfB-DELTAN-DELTAV mutant, a truncated variant (amino acids 761 to 1619) of GtfB of Lactobacillus reuteri strain 121 lacking both the N-terminal variable domain and domain V
additional information
construction of the GtfB-DELTAN-DELTAV mutant, a truncated variant (amino acids 761 to 1619) of GtfB of Lactobacillus reuteri strain 121 lacking both the N-terminal variable domain and domain V
additional information
construction of deletion GtfB-DELTANDELTAV mutant D1015N
additional information
construction of deletion GtfB-DELTANDELTAV mutant D1015N
additional information
an (engineered) 4,6-alpha-glucanotransferase (GTFB) from Lactobacillus reuteri 121 is introduced into two potato genetic backgrounds: amylose-containing line Kardal and amylose-free mutant amf. The resulting starches show severe changes in granule morphology regardless of genetic backgrounds. Modified starches from amf background exhibit a significant increase in granule size and starch phosphate content relative to the control, while starches from Kardal background display a higher digestibility, but do not show changes in granule size and phosphate content. Transcriptome analysis reveal the existence of a mechanism to restore the regular packing of double helices in starch granules, which possibly results in the removal of novel glucose chains potentially introduced by the (engineered) GTFB. This amendment mechanics can also explain the difficulties to detect alterations in starch fine structure in the transgenic lines
additional information
-
construction of the GtfB-DELTAN-DELTAV mutant, a truncated variant (amino acids 761 to 1619) of GtfB of Lactobacillus reuteri strain 121 lacking both the N-terminal variable domain and domain V
-
additional information
-
construction of deletion GtfB-DELTANDELTAV mutant D1015N
-
additional information
-
an (engineered) 4,6-alpha-glucanotransferase (GTFB) from Lactobacillus reuteri 121 is introduced into two potato genetic backgrounds: amylose-containing line Kardal and amylose-free mutant amf. The resulting starches show severe changes in granule morphology regardless of genetic backgrounds. Modified starches from amf background exhibit a significant increase in granule size and starch phosphate content relative to the control, while starches from Kardal background display a higher digestibility, but do not show changes in granule size and phosphate content. Transcriptome analysis reveal the existence of a mechanism to restore the regular packing of double helices in starch granules, which possibly results in the removal of novel glucose chains potentially introduced by the (engineered) GTFB. This amendment mechanics can also explain the difficulties to detect alterations in starch fine structure in the transgenic lines
-
additional information
-
construction of a GtfB enzyme 4,6-alpha-glucanotransferase lacking 761 N-terminal amino acids
additional information
Streptococcus thermophilus NCC2408
-
construction of a GtfB enzyme 4,6-alpha-glucanotransferase lacking 761 N-terminal amino acids
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
45
-
the half-lives of soluble and refolded enzyme are around 3.5 min at 45°C. The half-life of non-classical inclusion bodies enzyme protein is 3fold longer. Even after 30 min incubation, 20% of the original activity of non-classical inclusion bodies enzyme remains, while soluble and refolded enzymes become completely inactivated
45 - 51
the enzyme is resistant to thermal inactivation up to 45°C in sodium acetate buffer (pH 5.5), but at 51°C, it loses half of its activity in 10 min
50 - 55
at 50 and 55°C, the half-lives of both enzymes are less than 10 min. At 40°C, both enzymes are stable for more than 2 h. At lower temperature, the activities of both enzymes remain relatively high. The transferase activity does not change significantly in the range of 40 to 55°C
53.7
-
the enzyme has a half-life of 27.62 min at 50°C. The melting temperature is 53.7°C
60
68
-
melting temperature is 68°C. The enzyme activity is slightly reduced after 1 h at 60°C
40
-
incubation at 40°C for 10 min results in a decrease in residual enzyme activity to 81%. The half-life of putative N-terminally truncated enzyme at 40°C in phosphate-citric acid buffer at pH 7.0 is around 2 h
40
stable below 40°C, N-terminally truncated enzyme (GtfBDELTAN). 10 min, 81% decrease in residual enzyme activity. The half-life of GtfBDELTAN at 40°C in phosphate citric acid buffer at pH 7.0 is around 2 h
40
when incubated at 40°C, the enzyme shows about 75%, less than 50%, less than 40%, about 30%, and about 20% activity after 25 min, 1 h, 2 h, 3 h, and 4 h, respectively
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HiTrap column chromatography and Resource Q column chromatography
Hitrap column chromatography and Resource-Q column chromatography
Ni-immobilized-metal affinity chromatography, Ni-NTA column chromatography and HiTrap column chromatography
Ni-NTA column chromatography
Ni-NTA column chromatography and HiTrap Q column chromatography
-
recombinant C-terminally His-tagged enzyme mutant GtfB-DELTAN-DELTAV from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged truncated GtfB mutant 5.93fold from Escherichia coli strain BL21-CodonPlus-(DE3) by nickel affinity chromatography, ultrafiltration, and dialysis
-
recombinant N-terminally His6-tagged GtfD enzyme without its putative signal peptide-encoding sequence (amino acids 31 to 776) from Escherichia coli strain BL21 Star (DE3) by nickel affinity chromatography and ultrafiltration
-
recombinant soluble His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
4,6-alpha-GTase and 4,3-alpha-GTase (cf. EC 2.4.1.390) genes from Limosilactobacillus reuteri E81 and Limosilactobacillus fermentum PFC282 respectively are transformed into the plasmid pLEB124 vector having the signal peptide usp45 under the P45 continuous promoter and are successfully expressed in Lactococcus lactis MG1363
-
a truncated variant is expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21 cells. Trehalose addition significantly reduces inclusion bodies, resulting in an increase in enzyme activity 4.2times higher than that of the control group
-
expressed in Escherichia coli BL21 Star (DE3) cells
expressed in Escherichia coli BL21 Star (DE3) cells. Removing the variable N-terminal region results in increased expression of the soluble and active enzyme
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
expression of N-terminally truncated variant, in Escherichia coli
gene gftB, recombinant expression in Solanum tuberosum amylose-containing line Kardal and amylose-free mutant amf, the gene is cloned in frame with GBSSI transit peptide to allow amyloplast targeting and is driven by the potato GBSSI promoter for tuber expression, quantitative RT-PCR expression analysis
gene gtfB, genomic mapping and phylogenetic analysis, recombinant expression of wild-type and truncated mutant enzymes
gene gtfB, recombinant expression of C-terminally His-tagged enzyme mutant GtfB-DELTAN-DELTAV in Escherichia coli strain BL21(DE3)
gene gtfB, recombinant expression of His-tagged truncated GtfB mutant in Escherichia coli strain BL21-CodonPlus-(DE3)
-
gene gtfD, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant expression of N-terminally His6-tagged full-length GtfD enzyme without its putative signal peptide-encoding sequence (amino acids 31 to 776) in Escherichia coli strain BL21 Star (DE3)
-
gene gtfX, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
gene gtfY, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
GTFB-like 4,6-alpha-glucanotransferases, phylogenetic analysis, detailed overview
GTFC-like 4,6-alpha-glucanotransferases, sequence comparisons and phylogenetic analysis, detailed overview. A Tyr residue in GTFC-like 4,6-alpha-GTs proteins replaces the subsite +1/+2 Trp residue conserved in almost all GH70 GSs (W1065 in GTF180-DELTAN)
N-terminally truncated enzyme is expressed in Escherichia coli BL21(DE3) cells
-
the N-terminally truncated enzyme (GtfBDELTAN) is expressed in Escherichia coli
GTFB-like 4,6-alpha-glucanotransferases, phylogenetic analysis, detailed overview
-
GTFB-like 4,6-alpha-glucanotransferases, phylogenetic analysis, detailed overview
-
GTFB-like 4,6-alpha-glucanotransferases, phylogenetic analysis, detailed overview
-
GTFC-like 4,6-alpha-glucanotransferases, sequence comparisons and phylogenetic analysis, detailed overview. A Tyr residue in GTFC-like 4,6-alpha-GTs proteins replaces the subsite +1/+2 Trp residue conserved in almost all GH70 GSs (W1065 in GTF180-DELTAN)
-
GTFC-like 4,6-alpha-glucanotransferases, sequence comparisons and phylogenetic analysis, detailed overview. A Tyr residue in GTFC-like 4,6-alpha-GTs proteins replaces the subsite +1/+2 Trp residue conserved in almost all GH70 GSs (W1065 in GTF180-DELTAN)
-
GTFC-like 4,6-alpha-glucanotransferases, sequence comparisons and phylogenetic analysis, detailed overview. A Tyr residue in GTFC-like 4,6-alpha-GTs proteins replaces the subsite +1/+2 Trp residue conserved in almost all GH70 GSs (W1065 in GTF180-DELTAN)
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
dialysis against 20 mM Tris/HCl (pH 8.0), 1 mM CaCl2, and 1 mM dithiothreitol
refolding of the enzyme is most efficient in double distilled H2O
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
food industry
industry
food industry
-
during the process of cooking wheat, semicrystallized chains of raw starch are hydrated into an amorphous form. After they have cooled for a sufficiently long period, linear molecules, amylose, and linear parts of amylopectin molecules expel water and rearrange into a more crystalline structure. This recrystallization, called retrogradation, often leads to the formation of hard and digestive enzyme-inaccessible textures in some wheat-based foods, resulting in poor sensory quality, short shelf life, and low consumer acceptance. After the GtfB-modified wheat starches are gelatinized and stored at 4°C for 1-2 weeks, their endothermic enthalpies are significantly lower than that of the control sample, indicating low retrogradation rates
food industry
-
the enzyme shows clear antistaling effects in bread bakery products
food industry
the enzyme allows the synthesis of starch derived alpha-glucans with markedly reduced digestibility
food industry
-
the enzyme converts starch into product with increased alpha(1-6) glycosidic bonds ratio, and this product is a soluble dietary fiber with property of escaping small intestine digestion
food industry
the enzyme can synthesize soluble dietary starch fibers and displayes high conversion yields at relatively high substrate concentrations
food industry
-
4,3-alpha-GTase (cf. EC 2.4.1.390) and 4,6-alpha-GTase produced by Lactococcus lactis by extracellular secretion have technological and health functional effects in bakery products, such as bread and bun. The enzymes successfully lower the glycemic index and delayed staling
food industry
-
the enzyme allows the synthesis of starch derived alpha-glucans with markedly reduced digestibility
-
food industry
-
the enzyme can synthesize soluble dietary starch fibers and displayes high conversion yields at relatively high substrate concentrations
-
food industry
Streptococcus thermophilus NCC2408
-
during the process of cooking wheat, semicrystallized chains of raw starch are hydrated into an amorphous form. After they have cooled for a sufficiently long period, linear molecules, amylose, and linear parts of amylopectin molecules expel water and rearrange into a more crystalline structure. This recrystallization, called retrogradation, often leads to the formation of hard and digestive enzyme-inaccessible textures in some wheat-based foods, resulting in poor sensory quality, short shelf life, and low consumer acceptance. After the GtfB-modified wheat starches are gelatinized and stored at 4°C for 1-2 weeks, their endothermic enthalpies are significantly lower than that of the control sample, indicating low retrogradation rates
-
food industry
Limosilactobacillus fermentum NCC 3057
-
the enzyme converts starch into product with increased alpha(1-6) glycosidic bonds ratio, and this product is a soluble dietary fiber with property of escaping small intestine digestion
-
food industry
-
4,3-alpha-GTase (cf. EC 2.4.1.390) and 4,6-alpha-GTase produced by Lactococcus lactis by extracellular secretion have technological and health functional effects in bakery products, such as bread and bun. The enzymes successfully lower the glycemic index and delayed staling
-
industry
N1019D mutation does not alter the product specificity, increases the catalytic activity and efficiency by 420% and 590%, respectively, and maintains more than 80% relative activity in the pH 3.5-6.5 interval. Improving activity and catalytic efficiency enables industrial application of Lr 121 GtfB for the efficient production of alpha-glucans
industry
-
N1019D mutation does not alter the product specificity, increases the catalytic activity and efficiency by 420% and 590%, respectively, and maintains more than 80% relative activity in the pH 3.5-6.5 interval. Improving activity and catalytic efficiency enables industrial application of Lr 121 GtfB for the efficient production of alpha-glucans
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kralj, S.; Grijpstra, P.; van Leeuwen, S.S.; Leemhuis, H.; Dobruchowska, J.M.; van der Kaaij, R.M.; Malik, A.; Oetari, A.; Kamerling, J.P.; Dijkhuizen, L.
4,6-alpha-Glucanotransferase, a novel enzyme that structurally and functionally provides an evolutionary link between glycoside hydrolase enzyme families 13 and 70
Appl. Environ. Microbiol.
77
8154-8163
2011
Limosilactobacillus reuteri, Limosilactobacillus reuteri (Q5SBM0), Limosilactobacillus reuteri 121, Limosilactobacillus reuteri DSM 20016
brenda
Bai, Y.; van der Kaaij, R.M.; Leemhuis, H.; Pijning, T.; van Leeuwen, S.S.; Jin, Z.; Dijkhuizen, L.
Biochemical characterization of the Lactobacillus reuteri glycoside hydrolase family 70 GTFB type of 4,6-alpha-glucanotransferase enzymes that synthesize soluble dietary starch fibers
Appl. Environ. Microbiol.
81
7223-7232
2015
Limosilactobacillus reuteri, Limosilactobacillus reuteri (Q5SBM0), Limosilactobacillus reuteri 121
brenda
Gangoiti, J.; Pijning, T.; Dijkhuizen, L.
The Exiguobacterium sibiricum 255-15 GtfC enzyme represents a novel glycoside hydrolase 70 subfamily of 4,6-alpha-glucanotransferase enzymes
Appl. Environ. Microbiol.
82
756-766
2016
Exiguobacterium artemiae, Exiguobacterium artemiae (B1YMN6), Exiguobacterium artemiae 255-15, Exiguobacterium artemiae DSM 17290 (B1YMN6)
brenda
Leemhuis, H.; Dijkman, W.; Dobruchowska, J.; Pijning, T.; Grijpstra, P.; Kralj, S.; Kamerling, J.; Dijkhuizen, L.
4,6-alpha-Glucanotransferase activity occurs more widespread in Lactobacillus strains and constitutes a separate GH70 subfamily
Appl. Microbiol. Biotechnol.
97
181-193
2013
Limosilactobacillus reuteri, Limosilactobacillus reuteri (A5VL73), Limosilactobacillus reuteri (Q5SBN1), Limosilactobacillus reuteri DSM 20016, Limosilactobacillus reuteri DSM 20016 (A5VL73), Limosilactobacillus reuteri ML1 (Q5SBN1), Limosilactobacillus reuteri ML1
brenda
Gangoiti, J.; van Leeuwen, S.S.; Vafiadi, C.; Dijkhuizen, L.
The Gram-negative bacterium Azotobacter chroococcum NCIMB 8003 employs a new glycoside hydrolase family 70 4,6-alpha-glucanotransferase enzyme (GtfD) to synthesize a reuteran like polymer from maltodextrins and starch
Biochim. Biophys. Acta
1860
1224-1236
2016
Azotobacter chroococcum (A0A0C4WTK3), Azotobacter chroococcum NCIMB 8003 (A0A0C4WTK3)
brenda
Meng, X.; Gangoiti, J.; Bai, Y.; Pijning, T.; Van Leeuwen, S.S.; Dijkhuizen, L.
Structure-function relationships of family GH70 glucansucrase and 4,6-alpha-glucanotransferase enzymes, and their evolutionary relationships with family GH13 enzymes
Cell. Mol. Life Sci.
73
2681-2706
2016
Exiguobacterium sp., Bacillus sp. (in: firmicutes), Limosilactobacillus reuteri, Lactobacillus sp., Pediococcus sp., Exiguobacterium artemiae, Limosilactobacillus reuteri 121, Exiguobacterium artemiae 255-15, Limosilactobacillus reuteri DSM 20016, Limosilactobacillus reuteri ML1
brenda
Meng, X.; Gangoiti, J.; de Kok, N.; van Leeuwen, S.S.; Pijning, T.; Dijkhuizen, L.
Biochemical characterization of two GH70 family 4,6-alpha-glucanotransferases with distinct product specificity from Lactobacillus aviarius subsp. aviarius DSM 20655
Food Chem.
253
236-246
2018
Ligilactobacillus aviarius, Ligilactobacillus aviarius DSM 20655
brenda
Bai, Y.; Boeger, M.; van der Kaaij, R.M.; Woortman, A.J.; Pijning, T.; van Leeuwen, S.S.; van Bueren, A.L.; Dijkhuizen, L.
Lactobacillus reuteri strains convert starch and maltodextrins into homoexopolysaccharides using an extracellular and cell-associated 4,6-alpha-glucanotransferase
J. Agric. Food Chem.
64
2941-2952
2016
Limosilactobacillus reuteri, Limosilactobacillus reuteri (A0A0U5F702), no activity in Lactobacillus reuteri strain 180, no activity in Lactobacillus reuteri strain ATCC55730, Limosilactobacillus reuteri 121 (A0A0U5F702), Limosilactobacillus reuteri TMW1.106, Limosilactobacillus reuteri ML1, Limosilactobacillus reuteri LMG 18388 (A0A0U5F702), Limosilactobacillus reuteri DSM20016
brenda
Li, X.; Fei, T.; Wang, Y.; Zhao, Y.; Pan, Y.; Li, D.
Wheat starch with low retrogradation properties produced by modification of the GtfB enzyme 4,6-alpha-glucanotransferase from Streptococcus thermophilus
J. Agric. Food Chem.
66
3891-3898
2018
Streptococcus thermophilus, Streptococcus thermophilus NCC2408
brenda
Te Poele, E.; Corwin, S.; Hamaker, B.R.; Lamothe, L.; Vafeiadi, C.; Dijkhuizen, L.
Development of slowly digestible starch derived alpha-glucans with 4,6-alpha-glucanotransferase and branching sucrase enzymes
J. Agric. Food Chem.
68
6664-6671
2020
Limosilactobacillus reuteri, Limosilactobacillus reuteri (A0A0U5F702), Limosilactobacillus reuteri 121, Limosilactobacillus reuteri 121 (A0A0U5F702)
brenda
Xu, X.; Dechesne, A.; Visser, R.G.; Trindade, L.M.
Expression of an (engineered) 4,6-alpha-glucanotransferase in potato results in changes in starch characteristics
PLoS ONE
11
e0166981
2016
Limosilactobacillus reuteri (A0A0U5F702), Limosilactobacillus reuteri 121 (A0A0U5F702)
brenda
Gangoiti, J.; Lamothe, L.; van Leeuwen, S.S.; Vafiadi, C.; Dijkhuizen, L.
Characterization of the Paenibacillus beijingensis DSM 24997 GtfD and its glucan polymer products representing a new glycoside hydrolase 70 subfamily of 4,6-alpha-glucanotransferase enzymes
PLoS ONE
12
e0172622
2017
Paenibacillus beijingensis, Paenibacillus beijingensis DSM 24997
brenda
Bai, Y.; Gangoiti, J.; Dijkstra, B.W.; Dijkhuizen, L.; Pijning, T.
Crystal structure of 4,6-alpha-glucanotransferase supports diet-driven evolution of GH70 enzymes from alpha-amylases in oral bacteria
Structure
25
231-242
2017
Limosilactobacillus reuteri (Q5SBM0), Limosilactobacillus reuteri (A0A0U5F702), Limosilactobacillus reuteri 121 (A0A0U5F702), Limosilactobacillus reuteri 121 (Q5SBM0)
brenda
Bai, Y.; van der Kaaij, R.; Jacob Woortman, A.; Jin, Z.; Dijkhuizen, L.
Characterization of the 4,6-alpha-glucanotransferase GTFB enzyme of Lactobacillus reuteri 121 isolated from inclusion bodies
BMC Biotechnol.
15
49
2015
Limosilactobacillus reuteri, Limosilactobacillus reuteri 121
brenda
Liu, Y.; Wu, Y.; Ji, H.; Li, X.; Jin, Z.; Svensson, B.; Bai, Y.
Cost-effective and controllable synthesis of isomalto/malto-polysaccharides from beta-cyclodextrin by combined action of cyclodextrinase and 4,6-alpha-glucanotransferase GtfB
Carbohydr. Polym.
310
120716
2023
Limosilactobacillus reuteri, Limosilactobacillus reuteri 121
brenda
Biyikli, A.; Nicin, R.; Dertli, E.; Simsek, O.
Extracellular recombinant production of 4,6 and 4,3 alpha-glucanotransferases in Lactococcus lactis
Enzyme Microb. Technol.
164
110175
2023
Limosilactobacillus reuteri, Limosilactobacillus reuteri E81
brenda
Yang, W.; Sheng, L.; Chen, S.; Wang, L.; Su, L.; Wu, J.
Characterization of a new 4,6-alpha-glucanotransferase from Limosilactobacillus fermentum NCC 3057 with ability of synthesizing low molecular mass isomalto-/maltopolysaccharide
Food Biosci.
46
101514
2022
Limosilactobacillus fermentum, Limosilactobacillus fermentum NCC 3057
-
brenda
Dobruchowska, J.; Gerwig, G.; Kralj, S.; Grijpstra, P.; Leemhuis, H.; Dijkhuizen, L.; Kamerling, J.
Structural characterization of linear isomalto-/malto-oligomer products synthesized by the novel GTFB 4,6-alpha-glucanotransferase enzyme from Lactobacillus reuteri 121
Glycobiology
22
517-528
2012
Limosilactobacillus reuteri, Limosilactobacillus reuteri 121
brenda
Rao, D.; Wang, L.; Huo, R.; Su, L.; Guo, Z.; Yang, W.; Wei, B.; Tao, X.; Chen, S.; Wu, J.
Trehalose promotes high-level heterologous expression of 4,6-alpha-glucanotransferase GtfR2 in Escherichia coli and mechanistic analysis
Int. J. Biol. Macromol.
210
315-323
2022
Burkholderia sp.
brenda
Rao, D.; Huo, R.; Yan, Z.; Guo, Z.; Liu, W.; Lu, M.; Luo, H.; Tao, X.; Yang, W.; Su, L.; Chen, S.; Wang, L.; Wu, J.
Multiple approaches of loop region modification for thermostability improvement of 4,6-alpha-glucanotransferase from Limosilactobacillus fermentum NCC 3057
Int. J. Biol. Macromol.
233
123536
2023
Limosilactobacillus fermentum, Limosilactobacillus fermentum NCC 3057
brenda
Li, X.; Jiang, T.; Wang, Y.; Dong, J.; Jin, Z.; Bai, Y.
Exploring the roles of amylopectin in starch modification with Limosilactobacillus reuteri 121 4,6-alpha-glucanotransferase via developed methods
Int. J. Biol. Macromol.
243
125040
2023
Limosilactobacillus reuteri, Limosilactobacillus reuteri 121
brenda
Te Poele, E.; Van Der Hoek, S.; Chatziioannou, A.; Gerwig, G.; Duisterwinkel, W.; Oudhuis, L.; Gangoiti, J.; Dijkhuizen, L.; Leemhuis, H.
GtfC enzyme of Geobacillus sp. 12AMOR1 represents a novel thermostable type of GH70 4,6-alpha-glucanotransferase that synthesizes a linear alternating (alpha1->6)/(alpha1->4) alpha-glucan and delays bread staling
J. Agric. Food Chem.
69
9859-9868
2021
Geobacillus sp. 12AMOR1
brenda
Pijning, T.; Te Poele, E.; De Leeuw, T.; Guskov, A.; Dijkhuizen, L.
Crystal structure of 4,6-alpha-glucanotransferase GtfC-DELTAC from thermophilic Geobacillus 12AMOR1 Starch transglycosylation in non-permuted GH70 enzymes
J. Agric. Food Chem.
70
15283-15295
2022
Geobacillus sp. 12AMOR1
brenda
Jiang, Y.; Li, X.; Pijning, T.; Bai, Y.; Dijkhuizen, L.
Mutations in amino acid residues of Limosilactobacillus reuteri 121 GtfB 4,6-alpha-glucanotransferase that affect reaction and product specificity
J. Agric. Food Chem.
70
1952-1961
2022
Limosilactobacillus reuteri (Q5SBM0), Limosilactobacillus reuteri 121 (Q5SBM0)
brenda
Kralj, S.; van Geel-Schutten, G.; Dondorff, M.; Kirsanovs, S.; van der Maarel, M.; Dijkhuizen, L.
Glucan synthesis in the genus Lactobacillus Isolation and characterization of glucansucrase genes, enzymes and glucan products from six different strains
Microbiology
150
3681-3690
2004
Limosilactobacillus reuteri, Limosilactobacillus reuteri 121
brenda
Dong, J.; Wang, Y.; Li, X.; Chen, Y.; Fan, R.; Wang, N.; Jin, Z.; Bai, Y.
Comparison of a novel GtfB-type 4,6-alpha-glucanotransferase from Fructilactobacillus sanfranciscensis Gs2 for converting starch in the gelatinized and granular systems
Food Biosci.
59
104118
2024
Limosilactobacillus fermentum (A0A1Z2RUD1)
-
brenda
Nicin, R.T.; Zehir-Sentuerk, D.; Oezkan, B.; Goeksungur, Y.; Simsek, O.e.
Optimization of 4,6-alpha and 4,3-alpha-glucanotransferase production in Lactococcus lactis and determination of their effects on some quality characteristics of bakery products
Foods
13
432
2024
Limosilactobacillus fermentum, Limosilactobacillus fermentum PFC282
brenda
Wang, N.; Dong, J.; Li, X.; Svensson, B.; Jin, Z.; Bai, Y.
N1019D mutant of Limosilactobacillus reuteri 121 4,6-alpha-glucanotransferase GtfB significantly improved catalytic activity
J. Agric. Food Chem.
72
6509-6518
2024
Limosilactobacillus reuteri (Q5SBM0), Limosilactobacillus reuteri 121 (Q5SBM0)
brenda
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