Literature summary for 2.4.1.B34 extracted from

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 (2016), Cell. Mol. Life Sci., 73, 2681-2706 .

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Cloned(Commentary)

Cloned (Comment)	Organism
GTFB-like 4,6-alpha-glucanotransferases, phylogenetic analysis, detailed overview	Lactobacillus sp.
GTFB-like 4,6-alpha-glucanotransferases, phylogenetic analysis, detailed overview	Limosilactobacillus reuteri
GTFB-like 4,6-alpha-glucanotransferases, phylogenetic analysis, detailed overview	Pediococcus sp.
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)	Bacillus sp. (in: Bacteria)
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)	Exiguobacterium sibiricum
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)	Exiguobacterium sp.

Organism

Organism	UniProt	Comment	Textmining
Bacillus sp. (in: Bacteria)	-	-	-
Exiguobacterium sibiricum	-	-	-
Exiguobacterium sibiricum 255-15	-	-	-
Exiguobacterium sp.	-	-	-
Lactobacillus sp.	-	-	-
Limosilactobacillus reuteri	-	-	-
Limosilactobacillus reuteri 121	-	-	-
Limosilactobacillus reuteri DSM 20016	-	-	-
Limosilactobacillus reuteri ML1	-	-	-
Pediococcus sp.	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
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	Pediococcus sp.	?	-	-
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	Lactobacillus sp.	?	-	-
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	Limosilactobacillus reuteri	?	-	-
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	Bacillus sp. (in: Bacteria)	?	-	-
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	Exiguobacterium sibiricum	?	-	-
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	Exiguobacterium sp.	?	-	-
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	Exiguobacterium sibiricum 255-15	?	-	-
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	Limosilactobacillus reuteri ML1	?	-	-
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	Limosilactobacillus reuteri DSM 20016	?	-	-
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	Limosilactobacillus reuteri 121	?	-	-

Synonyms

Synonyms	Comment	Organism
4,6-alpha-GT	-	Bacillus sp. (in: Bacteria)
4,6-alpha-GT	-	Lactobacillus sp.
4,6-alpha-GT	-	Limosilactobacillus reuteri
4,6-alpha-GT	-	Pediococcus sp.
4,6-alpha-GT	-	Exiguobacterium sibiricum
4,6-alpha-GT	-	Exiguobacterium sp.
GtfB	-	Limosilactobacillus reuteri
GTFB-like 4,6-alpha-glucanotransferase	-	Lactobacillus sp.
GTFB-like 4,6-alpha-glucanotransferase	-	Limosilactobacillus reuteri
GTFB-like 4,6-alpha-glucanotransferase	-	Pediococcus sp.
GTFB-like 4,6-alpha-GT	-	Lactobacillus sp.
GTFB-like 4,6-alpha-GT	-	Limosilactobacillus reuteri
GTFB-like 4,6-alpha-GT	-	Pediococcus sp.
GTFC	-	Exiguobacterium sibiricum
GTFC-like 4,6-alpha-glucanotransferase	-	Bacillus sp. (in: Bacteria)
GTFC-like 4,6-alpha-glucanotransferase	-	Exiguobacterium sibiricum
GTFC-like 4,6-alpha-glucanotransferase	-	Exiguobacterium sp.
GTFC-like 4,6-alpha-GT	-	Bacillus sp. (in: Bacteria)
GTFC-like 4,6-alpha-GT	-	Exiguobacterium sibiricum
GTFC-like 4,6-alpha-GT	-	Exiguobacterium sp.
GtfML4	-	Limosilactobacillus reuteri
GtfML4	-	Pediococcus sp.
GtfW	-	Limosilactobacillus reuteri

General Information

General Information	Comment	Organism
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	Bacillus sp. (in: Bacteria)
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	Exiguobacterium sp.
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	Exiguobacterium sibiricum
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	Limosilactobacillus reuteri
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	Lactobacillus sp.
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	Pediococcus sp.