EC Number   |
General Information |
Reference |
|---|
  2.4.1.B34 | 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 |
759033 |
| 2.4.1.B34 | 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 |
-, 759033 |
| 2.4.1.B34 | 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 |
-, 759033 |
| 2.4.1.B34 | 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 |
759033 |
| 2.4.1.B34 | 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) |
-, 760207 |
| 2.4.1.B34 | evolution |
the enzyme belongs to the GH70 family |
-, 759381 |
| 2.4.1.B34 | more |
structural modeling of Lactobacillus aviarius subsp. aviarius GtfX, compared to the crystal structure of Lactobacillus reuteri GtfB |
-, 759213 |
| 2.4.1.B34 | more |
structural modeling of Lactobacillus aviarius subsp. aviarius GtfY, compared to the crystal structure of Lactobacillus reuteri GtfB |
-, 759213 |
| 2.4.1.B34 | more |
structure-function analysis, modeling and docking, overview. Mechanism and mode of action of GtfB in comparison with alpha-amylase and glucansucrase |
-, 760207 |
| 2.4.1.B34 | 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 |
-, 760020 |
