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amylopectin + acceptor
?
-
transglycosylation activity
-
-
?
amylose + maltose
maltotriose + panose
amylose V + acceptor
?
-
transglycosylation activity
-
-
?
amylose V + maltoheptaose
?
-
transglycosylation activity
-
-
?
amylose V + maltohexaose
?
-
transglycosylation activity
-
-
?
amylose V + maltopentaose
?
-
transglycosylation activity
-
-
?
amylose V + maltose
maltotriose + maltotetraose + ?
-
-
-
?
amylose V + maltotetraose
?
-
transglycosylation activity
-
-
?
amylose V + maltotriose
?
-
transglycosylation activity
-
-
?
maltodextrin + H2O
?
i.e. short-chain alpha1->4-linked maltodextrins
-
-
?
maltoheptaose + H2O
D-glucose + maltotriose + maltohexaose
-
first clear products of the reaction
-
?
maltohexaose + H2O
D-glucose + maltopentaose
-
first clear reaction products accumulating after 1 h, longer incubation leads to 4-substituted, 6-substituted, and terminal glucose residues at a molar ratio of 63, 17, and 20%
-
?
maltopentaose + H2O
D-glucose + maltotetraose
-
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%
-
?
maltotetraose + H2O
D-glucose + maltotetraose
maltotriose + H2O
?
-
hydrolytic activity
-
-
?
starch + acceptor
?
-
transglycosylation activity
-
-
?
additional information
?
-
amylopectin + H2O
?
-
hydrolytic activity
-
-
?
amylopectin + H2O
?
-
hydrolytic activity
-
-
?
amylopectin + H2O
?
-
hydrolytic activity
-
-
?
amylose + maltose
maltotriose + panose
the enzyme synthesizes larger saccharides with alpha1->4 and alpha1->6 glucosidic linkages
panose i.e. Glc-alpha-(1->6)-maltose
-
?
amylose + maltose
maltotriose + panose
-
the enzyme synthesizes larger saccharides with alpha1->4 and alpha1->6 glucosidic linkages
panose i.e. Glc-alpha-(1->6)-maltose
-
?
amylose V
?
-
GtfB produces a high molecular mass polymer with a molecular mass about 80 times greater than that of the starting amylose V
-
?
amylose V + H2O
?
-
hydrolytic activity
-
-
?
amylose V + H2O
?
-
hydrolytic activity
-
-
?
amylose V + H2O
?
-
both hydrolysis and transferase activities occur. Besides the presence of alpha1->4 linkages, alpha1->6 linkages are newly formed. In the product mixture derived from amylose V, the alpha1->6/alpha1->4 linkage ratio increases up to 90:10. In the product mixture, free glucose, 4-substituted reducing glucose residues [-(1->4)-alpha-D-Glc], and a small amount of reducing-end glucose residues which are 6 substituted are detected
-
?
amylose V + H2O
?
hydrolytic activity, amylose V with Mw 170 kDa
-
-
?
amylose V + H2O
?
hydrolytic activity, amylose V with Mw 170 kDa
-
-
?
amylose V + H2O
?
-
hydrolytic activity
-
-
?
amylose V + maltose
?
transglycosylation activity, amylose V with 170 kDa
-
-
?
amylose V + maltose
?
transglycosylation activity, amylose V with 170 kDa
-
-
?
Maltoheptaose
?
-
-
-
?
Maltoheptaose
?
the enzyme synthesize oligosaccharides up to a degree of polymerization of at least 14. The enzyme introduces 1->6 glucosidic linkages (18%) into the final mixture of products
-
-
?
Maltoheptaose
?
-
the enzyme synthesize oligosaccharides up to a degree of polymerization of at least 14. The enzyme introduces 1->6 glucosidic linkages (18%) into the final mixture of products
-
-
?
maltoheptaose + H2O
?
-
-
-
?
maltoheptaose + H2O
?
-
hydrolytic activity
-
-
?
maltoheptaose + H2O
?
-
hydrolytic activity
-
-
?
Maltohexaose
?
-
-
-
?
maltohexaose + H2O
?
-
hydrolytic activity
-
-
?
maltohexaose + H2O
?
-
hydrolytic activity
-
-
?
maltooligosaccharide
?
the enzyme uses maltooligosaccharides as donor and acceptor substrates. The enzyme disproportionates (cleaves 1->4 and synthesizes 1->6 and 1->4 glucosidic linkages) and 1->6 polymerizes maltotetraose and larger maltooligosaccharide substrates. Only linear products are made and that with increasing degrees of polymerization, more 1->6 glucosidic linkages are introduced into the final products
-
-
?
maltooligosaccharide
?
-
the enzyme uses maltooligosaccharides as donor and acceptor substrates. The enzyme disproportionates (cleaves 1->4 and synthesizes 1->6 and 1->4 glucosidic linkages) and 1->6 polymerizes maltotetraose and larger maltooligosaccharide substrates. Only linear products are made and that with increasing degrees of polymerization, more 1->6 glucosidic linkages are introduced into the final products
-
-
?
maltopentaose
?
-
-
-
?
maltopentaose + H2O
?
-
hydrolytic activity
-
-
?
maltopentaose + H2O
?
-
hydrolytic activity
-
-
?
maltose
?
-
-
-
?
Maltotetraose
?
-
-
-
?
maltotetraose + H2O
?
-
hydrolytic activity
-
-
?
maltotetraose + H2O
?
-
hydrolytic activity
-
-
?
maltotetraose + H2O
D-glucose + maltotetraose
-
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
-
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
?
-
-
-
?
starch + H2O
?
-
hydrolytic activity
-
-
?
starch + H2O
?
-
hydrolytic activity
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
inactive on sucrose, panose, nigerose, beta-cyclodextrins, and isomalto-oligosaccharides with degree of polymerzation of 2, 3, and 5
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
inactive on sucrose, panose, nigerose, beta-cyclodextrins, and isomalto-oligosaccharides with degree of polymerzation of 2, 3, and 5
-
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
the enzyme is unable to use sucrose as a donor substrate and is inactive with the sucrose analogs turanose and palatinose, with raffinose, with the DP5 and DP6 isomaltooligosaccharides and with panose
-
-
?
additional information
?
-
the enzyme is unable to use sucrose as a donor substrate and is inactive with the sucrose analogs turanose and palatinose, with raffinose, with the DP5 and DP6 isomaltooligosaccharides and with panose
-
-
?
additional information
?
-
enzyme cleaves alpha1->4 glycosidic linkages and adds the released glucose moieties one by one to the non-reducing end of growing linear alpha-glucan chains via alpha1->6 glycosidic linkages (alpha1->4 to alpha1->6 transfer activity). It converts pure maltooligosaccharide substrates into linear alpha-glucan product mixtures with about 50% alpha1->6 glycosidic bonds (isomalto/maltooligosaccharides). Largest products synthesized from maltoheptaose have a degree of polymerizatition bleow 50
-
-
?
additional information
?
-
enzyme cleaves alpha1->4 glycosidic linkages and adds the released glucose moieties one by one to the non-reducing end of growing linear alpha-glucan chains via alpha1->6 glycosidic linkages (alpha1->4 to alpha1->6 transfer activity). It converts pure maltooligosaccharide substrates into linear alpha-glucan product mixtures with about 50% alpha1->6 glycosidic bonds (isomalto/maltooligosaccharides). Largest products synthesized from maltoheptaose have a degree of polymerizatition bleow 50
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
no substrates: maltose, maltotriose, sucrose, turanose and palatinose, raffinose, panose, DP5 and DP6 isomaltooligosaccharides
-
-
?
additional information
?
-
no substrates: maltose, maltotriose, sucrose, turanose and palatinose, raffinose, panose, DP5 and DP6 isomaltooligosaccharides
-
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
malto-oligosaccharide binding structures with wild-type and mutant enzymes, overview
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
structure of the IMMP product of 4,6-alpha-GTase Gtf106b with maltodextrins, overview. Enzyme reaction product analysis
-
-
-
additional information
?
-
structure of the IMMP product of 4,6-alpha-GTase Gtf106b with maltodextrins, overview. Enzyme reaction product analysis
-
-
-
additional information
?
-
-
structure of the IMMP product of 4,6-alpha-GTase GtfML4 with maltodextrins, overview. Enzyme reaction product analysis
-
-
-
additional information
?
-
structure of the IMMP product of 4,6-alpha-GTase GtfML4 with maltodextrins, overview. Enzyme reaction product analysis
-
-
-
additional information
?
-
-
structure of the IMMP product of 4,6-alpha-GTase GtfW with maltodextrins, overview. Enzyme reaction product analysis
-
-
-
additional information
?
-
structure of the IMMP product of 4,6-alpha-GTase GtfW with maltodextrins, overview. Enzyme reaction product analysis
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
malto-oligosaccharide binding structures with wild-type and mutant enzymes, overview
-
-
-
additional information
?
-
-
the enzyme is unable to use sucrose as a donor substrate and is inactive with the sucrose analogs turanose and palatinose, with raffinose, with the DP5 and DP6 isomaltooligosaccharides and with panose
-
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
enzyme cleaves alpha1->4 glycosidic linkages and adds the released glucose moieties one by one to the non-reducing end of growing linear alpha-glucan chains via alpha1->6 glycosidic linkages (alpha1->4 to alpha1->6 transfer activity). It converts pure maltooligosaccharide substrates into linear alpha-glucan product mixtures with about 50% alpha1->6 glycosidic bonds (isomalto/maltooligosaccharides). Largest products synthesized from maltoheptaose have a degree of polymerizatition bleow 50
-
-
?
additional information
?
-
-
structure of the IMMP product of 4,6-alpha-GTase Gtf106b with maltodextrins, overview. Enzyme reaction product analysis
-
-
-
additional information
?
-
-
structure of the IMMP product of 4,6-alpha-GTase GtfML4 with maltodextrins, overview. Enzyme reaction product analysis
-
-
-
additional information
?
-
-
structure of the IMMP product of 4,6-alpha-GTase GtfW with maltodextrins, overview. Enzyme reaction product analysis
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
structure of the IMMP product of 4,6-alpha-GTase Gtf106b with maltodextrins, overview. Enzyme reaction product analysis
-
-
-
additional information
?
-
-
structure of the IMMP product of 4,6-alpha-GTase GtfML4 with maltodextrins, overview. Enzyme reaction product analysis
-
-
-
additional information
?
-
-
structure of the IMMP product of 4,6-alpha-GTase GtfW with maltodextrins, overview. Enzyme reaction product analysis
-
-
-
additional information
?
-
enzyme cleaves alpha1->4 glycosidic linkages and adds the released glucose moieties one by one to the non-reducing end of growing linear alpha-glucan chains via alpha1->6 glycosidic linkages (alpha1->4 to alpha1->6 transfer activity). It converts pure maltooligosaccharide substrates into linear alpha-glucan product mixtures with about 50% alpha1->6 glycosidic bonds (isomalto/maltooligosaccharides). Largest products synthesized from maltoheptaose have a degree of polymerizatition bleow 50
-
-
?
additional information
?
-
-
structure of the IMMP product of 4,6-alpha-GTase Gtf106b with maltodextrins, overview. Enzyme reaction product analysis
-
-
-
additional information
?
-
-
structure of the IMMP product of 4,6-alpha-GTase GtfML4 with maltodextrins, overview. Enzyme reaction product analysis
-
-
-
additional information
?
-
-
structure of the IMMP product of 4,6-alpha-GTase GtfW with maltodextrins, overview. Enzyme reaction product analysis
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
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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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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
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additional information
?
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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
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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
-
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. 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
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
the enzyme belongs to the GH70 family
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
-
the enzyme belongs to the GH70 family
-
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
-
the enzyme belongs to the GH70 family
-
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
-
the enzyme belongs to the GH70 family
-
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
-
the enzyme belongs to the GH70 family
-
evolution
-
the enzyme belongs to the GH70 family
-
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
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
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 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 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 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 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 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 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 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 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 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 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
-
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 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 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 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
-
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
-
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
-
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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 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 (Q5SBM0)
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 sibiricum (B1YMN6), Exiguobacterium sibiricum 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 (A5VL73), Limosilactobacillus reuteri (Q5SBN1), Limosilactobacillus reuteri ML1 (Q5SBN1), Limosilactobacillus reuteri DSM 20016 (A5VL73)
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
Bacillus sp. (in: Bacteria), Limosilactobacillus reuteri, Lactobacillus sp., Pediococcus sp., Exiguobacterium sibiricum, Exiguobacterium sp., Exiguobacterium sibiricum 255-15, Limosilactobacillus reuteri ML1, Limosilactobacillus reuteri DSM 20016, Limosilactobacillus reuteri 121
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 ML1, Limosilactobacillus reuteri DSM20016, Limosilactobacillus reuteri 121 (A0A0U5F702), Limosilactobacillus reuteri TMW1.106, Limosilactobacillus reuteri LMG 18388 (A0A0U5F702)
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 (A0A0U5F702), 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 (A0A0U5F702), Limosilactobacillus reuteri 121 (A0A0U5F702)
brenda