2.4.1.B34: 4,6-alpha-glucanotransferase
This is an abbreviated version!
For detailed information about 4,6-alpha-glucanotransferase, go to the full flat file.
Reaction
The enzyme uses maltooligosaccharides as donor and acceptor substrates. It cleaves alpha1->4 glucosidic bonds and synthesizes 1->6 and 1->4 glucosidic linkages. =
Synonyms
4, 6-alpha-glucanotransferase, 4,6-alpha-GT, 4,6-alpha-GTase, Achr_35950, Exig_2648, GflML4, 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, Lreu_1346, UDP-N-acetylglucosamine-peptide N-acetylglucosaminyltransferase stabilizing protein
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General Information
General Information on EC 2.4.1.B34 - 4,6-alpha-glucanotransferase
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evolution
physiological function
additional information
-
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
-
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
-
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 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)
-
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
Limosilactobacillus reuteri TMW1.106
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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 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
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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 LMG 18388
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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
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structural modeling of Lactobacillus aviarius subsp. aviarius GtfX, compared to the crystal structure of Lactobacillus reuteri GtfB
additional information
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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
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structural modeling of Lactobacillus aviarius subsp. aviarius GtfX, compared to the crystal structure of Lactobacillus reuteri GtfB
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additional information
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structural modeling of Lactobacillus aviarius subsp. aviarius GtfY, compared to the crystal structure of Lactobacillus reuteri GtfB
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additional information
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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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