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Information on EC 2.4.1.395 - reuteransucrase
for references in articles please use BRENDA:EC2.4.1.395
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IUBMB Comments
The glucansucrases transfer a D-glucosyl residue from sucrose to a glucan chain. They are classified based on the linkage of the transferred glucosyl residue. The enzyme, characterized from the lactic acid bacterium Limosilactobacillus reuteri strain 121, catalyses the hydrolysis of sucrose and the transfer of the D-glucose moiety to suitable acceptors (inclduing sucrose), forming the glucan reuteran, which is typical for these strains. The enzyme forms mostly α(1→4) glucosidic linkages, but also α(1→6) linkages. The presence of maltose significantly accelerate the initial rate of the reaction. See EC 2.4.1.5, dextransucrase.
The enzyme appears in viruses and cellular organisms
showSynonyms
4,6-alpha-glucanotransferase, 4,6-alpha-glucanotransferase B, 4,6-alpha-glucanotransferase II, 4,6-alpha-GTase, alpha-1,6/alpha-1,4-specific glucansucrase, DsrM mutant S622N, DsrM mutant V583P/V586I, glucansucrase/glucosyltransferase, GtfA, GtfB, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4,6-alpha-glucanotransferase
4,6-alpha-glucanotransferase B
4,6-alpha-glucanotransferase II
4,6-alpha-GTase
alpha-1,6/alpha-1,4-specific glucansucrase
DsrM mutant S622N
DsrM mutant V583P/V586I
glucansucrase/glucosyltransferase
GtfA
GtfB
GtfB-E81
GtfO
Lr121
LrN1
reuteransucrase GtfO
GtfA
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
formation of reuteran from sucrose
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
sucrose:alpha-D-glucan 4-alpha/6-alpha-D-glucosyltransferase
The glucansucrases transfer a D-glucosyl residue from sucrose to a glucan chain. They are classified based on the linkage of the transferred glucosyl residue. The enzyme, characterized from the lactic acid bacterium Limosilactobacillus reuteri strain 121, catalyses the hydrolysis of sucrose and the transfer of the D-glucose moiety to suitable acceptors (inclduing sucrose), forming the glucan reuteran, which is typical for these strains. The enzyme forms mostly alpha(1->4) glucosidic linkages, but also alpha(1->6) linkages. The presence of maltose significantly accelerate the initial rate of the reaction. See EC 2.4.1.5, dextransucrase.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
sucrose + D-fructose
leucrose + trehalulose + 4'-alpha-D-glucosyl-leucrose + 6'-alpha-D-glucosyl-leucrose + 6'-alpha-D-glucosyl-trehalulose
sucrose + isomaltose
isopanose + alpha-(1->6)-isopanose + isomaltotriose + isomaltotetraose
sucrose + maltohexaose
panose + D-glucose
-
Substrates: low activity
Products: -
Products: -
?
sucrose + maltose
alpha-D-Glcp-(1->6)-alpha-D-Glcp-(1->4)-D-Glcp + alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-D-Glcp + alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->6)-alpha-DGlcp-(1->4)-D-Glcp + alpha-D-Glcp-(1->6)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->6)-alpha-D-Glcp-(1->4)-D-Glcp
sucrose + maltose
panose + maltotriose + glucosyl-(alpha1->4)-panose + glucosyl-(alpha1->6)-(alpha1->4)-panose
-
Substrates: -
Products: -
Products: -
?
sucrose + maltotriose
maltotetraose
-
Substrates: -
Products: -
Products: -
?
sucrose + maltotriose
maltotetraose + maltopentaose
-
Substrates: -
Products: -
Products: -
?
sucrose + panose
glucosyl-(alpha1->4)-panose and glucosyl-(alpha1->6)-(alpha1->4)-panose + ?
-
Substrates: -
Products: -
Products: -
?
amylose
?
-
Substrates: amylopectin is not used as an acceptor substrate, and no non-branched (alpha1->6) linkages are introduced into it. Substrates with higher amylose content or longer outer chains in amylopectin are more suitable for the N-terminally truncated enzyme to produce a dietary fiber with high contents of (alpha1->6) linkages, that have a prebiotic potential for use in foods
Products: -
Products: -
?
amylose
?
Substrates: mutants H1056G and Q1126I show a 9% decrease and an 11% increase, respectively, in the ratio of (alpha1->6) over (alpha1->4) linkages in maltodextrin-derived products
Products: -
Products: -
?
amylose
?
Substrates: mutants H1056G and Q1126I show a 9% decrease and an 11% increase, respectively, in the ratio of (alpha1->6) over (alpha1->4) linkages in maltodextrin-derived products
Products: -
Products: -
?
amylose
?
-
Substrates: the enzyme can significantly increase the branched chains with a degree of polymerizaion below 5 and decrease the other branches in potato starch, resulting in the high ratio of short to long branch, which contributes to the irregularity of the starch structure
Products: -
Products: -
?
pea starch
reuteran
-
Substrates: structural and property characterization of low-molecular-weight short-clustered reuterans with (alpha1->6) linkages in both linear chains and branches
Products: -
Products: -
?
pea starch
reuteran
-
Substrates: structural and property characterization of low-molecular-weight short-clustered reuterans with (alpha1->6) linkages in both linear chains and branches
Products: -
Products: -
?
starch
?
-
Substrates: production of a short length of alpha-1,6 linkages. External short chains mostly comprise of 1->6 glucosyl units are newly produced in potato starch, and the alpha-1,6 linkage ratio is significantly increased from 2.9% to 36.8%
Products: -
Products: -
?
starch
?
-
Substrates: production of a short length of alpha-1,6 linkages. External short chains mostly comprise of 1->6 glucosyl units are newly produced in potato starch, and the alpha-1,6 linkage ratio is significantly increased from 2.9% to 36.8%
Products: -
Products: -
?
sucrose
?
Substrates: the enzyme synthesizes a reuteran-type branched polymer with both alpha-1,4-linkages (46%) and alpha-1,6-linkages (34%)
Products: -
Products: -
?
sucrose
?
Substrates: the enzyme synthesizes a reuteran-type branched polymer with both alpha-1,4-linkages (46%) and alpha-1,6-linkages (34%)
Products: -
Products: -
?
sucrose
highly branched soluble glucan + D-fructose + ?
-
Substrates: the enzyme produces a highly branched, soluble glucan in which the majority of the linkages are of the alpha-(1->4) glucosidic type. The glucan also contains alpha(1->6)-linked glucosyl units and 4,6-disubstituted alpha-glucosyl units at the branching points
Products: -
Products: -
?
sucrose
highly branched soluble glucan + D-fructose + ?
-
Substrates: the enzyme produces a highly branched, soluble glucan in which the majority of the linkages are of the alpha-(1->4) glucosidic type. The glucan also contains alpha(1->6)-linked glucosyl units and 4,6-disubstituted alpha-glucosyl units at the branching points
Products: -
Products: -
?
sucrose
reuteran
-
Substrates: -
Products: -
Products: -
?
sucrose + ?
reuteran
-
Substrates: the enzyme converts sucrose into alpha-D-glucans (labelled reuterans) with mainly alpha-(1->4) glucosidic linkages plus alpha-(1->6) linkages (50% and 70%, respectively)
Products: -
Products: -
?
sucrose + ?
reuteran
-
Substrates: the enzyme converts sucrose into alpha-D-glucans (labelled reuterans) with mainly alpha-(1->4) glucosidic linkages plus alpha-(1->6) linkages (50% and 70%, respectively)
Products: -
Products: -
?
sucrose + ?
reuteran
Limosilactobacillus reuteri ATCC 55730
-
Substrates: the enzyme converts sucrose into alpha-D-glucans (labelled reuterans) with mainly alpha-(1->4) glucosidic linkages plus alpha-(1->6) linkages (50% and 70%, respectively)
Products: -
Products: -
?
sucrose + ?
reuteran + leucrose + isomaltose + D-glucose
-
Substrates: -
Products: -
Products: -
?
sucrose + ?
reuteran + leucrose + isomaltose + D-glucose
-
Substrates: -
Products: -
Products: -
?
sucrose + D-fructose
leucrose + trehalulose + 4'-alpha-D-glucosyl-leucrose + 6'-alpha-D-glucosyl-leucrose + 6'-alpha-D-glucosyl-trehalulose
-
Substrates: at high sucrose concentrations the sucrose isomers leucrose and trehalulose are synthesized, using the accumulated D-fructose as acceptor. Subsequently, the enzyme continues to transfer alpha-D-Glcp units to accumulating leucrose and trehalulose, resulting in 4'- and 6'-alpha-D-glucosyl-leucrose and 6-alpha-D-glucosyl-trehalulose
Products: -
Products: -
?
sucrose + D-fructose
leucrose + trehalulose + 4'-alpha-D-glucosyl-leucrose + 6'-alpha-D-glucosyl-leucrose + 6'-alpha-D-glucosyl-trehalulose
-
Substrates: at high sucrose concentrations the sucrose isomers leucrose and trehalulose are synthesized, using the accumulated D-fructose as acceptor. Subsequently, the enzyme continues to transfer alpha-D-Glcp units to accumulating leucrose and trehalulose, resulting in 4'- and 6'-alpha-D-glucosyl-leucrose and 6-alpha-D-glucosyl-trehalulose
Products: -
Products: -
?
sucrose + isomaltose
D-fructose + isomaltose + isopanose + D-glucose
-
Substrates: -
Products: -
Products: -
?
sucrose + isomaltose
D-fructose + isomaltose + isopanose + D-glucose
Limosilactobacillus reuteri ATCC 55730
-
Substrates: -
Products: -
Products: -
?
sucrose + isomaltose
D-fructose + isopanose + ?
-
Substrates: -
Products: -
Products: -
?
sucrose + isomaltose
D-fructose + isopanose + ?
-
Substrates: -
Products: -
Products: -
?
sucrose + isomaltose
isomaltotriose + isopanose + glucosyl-(alpha1->6)-isopanose
-
Substrates: -
Products: -
Products: -
?
sucrose + isomaltose
isomaltotriose + isopanose + glucosyl-(alpha1->6)-isopanose
-
Substrates: -
Products: -
Products: -
?
sucrose + isomaltose
isomaltotriose + isopanose + glucosyl-(alpha1->6)-isopanose
Limosilactobacillus reuteri ATCC 55730
-
Substrates: -
Products: -
Products: -
?
sucrose + isomaltose
isopanose + alpha-(1->6)-isopanose + isomaltotriose
-
Substrates: -
Products: -
Products: -
?
sucrose + isomaltose
isopanose + alpha-(1->6)-isopanose + isomaltotriose
-
Substrates: -
Products: -
Products: -
?
sucrose + isomaltose
isopanose + alpha-(1->6)-isopanose + isomaltotriose
Limosilactobacillus reuteri ATCC 55730
-
Substrates: -
Products: -
Products: -
?
sucrose + isomaltose
isopanose + alpha-(1->6)-isopanose + isomaltotriose + isomaltotetraose
-
Substrates: -
Products: -
Products: -
?
sucrose + isomaltose
isopanose + alpha-(1->6)-isopanose + isomaltotriose + isomaltotetraose
-
Substrates: -
Products: -
Products: -
?
sucrose + maltopentase
panose + D-glucose
-
Substrates: low activity
Products: -
Products: -
?
sucrose + maltopentase
panose + D-glucose
-
Substrates: low activity
Products: -
Products: -
?
sucrose + maltose
alpha-D-Glcp-(1->6)-alpha-D-Glcp-(1->4)-D-Glcp + alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-D-Glcp + alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->6)-alpha-DGlcp-(1->4)-D-Glcp + alpha-D-Glcp-(1->6)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->6)-alpha-D-Glcp-(1->4)-D-Glcp
-
Substrates: -
Products: -
Products: -
?
sucrose + maltose
alpha-D-Glcp-(1->6)-alpha-D-Glcp-(1->4)-D-Glcp + alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->4)-D-Glcp + alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->6)-alpha-DGlcp-(1->4)-D-Glcp + alpha-D-Glcp-(1->6)-alpha-D-Glcp-(1->4)-alpha-D-Glcp-(1->6)-alpha-D-Glcp-(1->4)-D-Glcp
Limosilactobacillus reuteri SK24.003
-
Substrates: -
Products: -
Products: -
?
sucrose + maltose
D-fructose + maltose + panose + D-glucose + maltotriose
-
Substrates: -
Products: -
Products: -
?
sucrose + maltose
D-fructose + maltose + panose + D-glucose + maltotriose
Limosilactobacillus reuteri ATCC 55730
-
Substrates: -
Products: -
Products: -
?
sucrose + maltose
D-fructose + panose + ?
-
Substrates: -
Products: -
Products: -
?
sucrose + maltose
D-fructose + panose + ?
-
Substrates: -
Products: -
Products: -
?
sucrose + maltose
panose + D-glucose
-
Substrates: low activity
Products: -
Products: -
?
sucrose + maltose
panose + D-glucose
-
Substrates: low activity
Products: -
Products: -
?
sucrose + maltose
panose + maltotriose
-
Substrates: -
Products: -
Products: -
?
sucrose + maltose
panose + maltotriose
-
Substrates: -
Products: -
Products: -
?
sucrose + maltose
panose + maltotriose
Limosilactobacillus reuteri ATCC 55730
-
Substrates: -
Products: -
Products: -
?
sucrose + maltose
panose + maltotriose + glucosyl-(alpha1->4)-panose + maltotetraose
-
Substrates: -
Products: -
Products: -
?
sucrose + maltose
panose + maltotriose + glucosyl-(alpha1->4)-panose + maltotetraose
-
Substrates: -
Products: -
Products: -
?
sucrose + maltose
panose + maltotriose + glucosyl-(alpha1->4)-panose + maltotetraose
Limosilactobacillus reuteri ATCC 55730
-
Substrates: -
Products: -
Products: -
?
sucrose + maltotetraose
panose + D-glucose
-
Substrates: low activity
Products: -
Products: -
?
sucrose + maltotetraose
panose + D-glucose
-
Substrates: low activity
Products: -
Products: -
?
sucrose + maltotriose
panose + D-glucose
-
Substrates: low activity
Products: -
Products: -
?
sucrose + maltotriose
panose + D-glucose
-
Substrates: low activity
Products: -
Products: -
?
sucrose + sucrose
reuteran
-
Substrates: the enzyme transfers glucose residues from donor sucrose to acceptor sucrose and to the growing glucan chain attached to a sucrose. The enzyme mainly produces linear oligosaccharides with alternating (1->6)/(1->4) linkages; no branched oligosaccharides are formed
Products: -
Products: -
?
sucrose + sucrose
reuteran
-
Substrates: the enzyme transfers glucose residues from donor sucrose to acceptor sucrose and to the growing glucan chain attached to a sucrose. The enzyme mainly produces linear oligosaccharides with alternating (1->6)/(1->4) linkages; no branched oligosaccharides are formed
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme favours hydrolysis at low sucrose concentrations and polymerization at high sucrose concentrations
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme also hydrolyzes sucrose to D-fructose and D-glucose
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme shows a hydrolysis:transglycosylation ratio of 43:57
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme shows a hydrolysis:transglycosylation ratio of 9:91
Products: -
Products: -
-
additional information
?
-
-
Substrates: only hydrolysis occurs at sucrose concentrations below 10 mM. More than 50% of sucrose is hydrolyzed into D-glucose and D-fructose
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme also hydrolyzes sucrose to D-glucose and D-fructose
Products: -
Products: -
-
additional information
?
-
-
Substrates: total and hydrolysis activities are determined by measuring the amount of fructose and glucose released, respectively. The transferase activity (also known as transglycosylation activity) is calculated by subtracting the hydrolysis activity from the total activity. GtfO produces a reuteran with 21% (alpha1->6) and 79% (alpha1->4) linkages, NMR spectroscopy analysis, overview
Products: -
Products: -
-
additional information
?
-
Substrates: total and hydrolysis activities are determined by measuring the amount of fructose and glucose released, respectively. The transferase activity (also known as transglycosylation activity) is calculated by subtracting the hydrolysis activity from the total activity. GtfO produces a reuteran with 21% (alpha1->6) and 79% (alpha1->4) linkages, NMR spectroscopy analysis, overview
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme favours hydrolysis at low sucrose concentrations and polymerization at high sucrose concentrations
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme also hydrolyzes sucrose to D-fructose and D-glucose
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme shows a hydrolysis:transglycosylation ratio of 43:57
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme also hydrolyzes sucrose to D-glucose and D-fructose
Products: -
Products: -
-
additional information
?
-
Limosilactobacillus reuteri ATCC 55730
-
Substrates: the enzyme also hydrolyzes sucrose to D-fructose and D-glucose
Products: -
Products: -
-
additional information
?
-
Limosilactobacillus reuteri ATCC 55730
-
Substrates: the enzyme shows a hydrolysis:transglycosylation ratio of 43:57
Products: -
Products: -
-
additional information
?
-
Limosilactobacillus reuteri ATCC 55730
-
Substrates: only hydrolysis occurs at sucrose concentrations below 10 mM. More than 50% of sucrose is hydrolyzed into D-glucose and D-fructose
Products: -
Products: -
-
additional information
?
-
Limosilactobacillus reuteri ATCC 55730
Substrates: total and hydrolysis activities are determined by measuring the amount of fructose and glucose released, respectively. The transferase activity (also known as transglycosylation activity) is calculated by subtracting the hydrolysis activity from the total activity. GtfO produces a reuteran with 21% (alpha1->6) and 79% (alpha1->4) linkages, NMR spectroscopy analysis, overview
Products: -
Products: -
-
additional information
?
-
Limosilactobacillus reuteri ATCC 55730
-
Substrates: total and hydrolysis activities are determined by measuring the amount of fructose and glucose released, respectively. The transferase activity (also known as transglycosylation activity) is calculated by subtracting the hydrolysis activity from the total activity. GtfO produces a reuteran with 21% (alpha1->6) and 79% (alpha1->4) linkages, NMR spectroscopy analysis, overview
Products: -
Products: -
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
sucrose
?
Substrates: the enzyme synthesizes a reuteran-type branched polymer with both alpha-1,4-linkages (46%) and alpha-1,6-linkages (34%)
Products: -
Products: -
?
sucrose
?
Substrates: the enzyme synthesizes a reuteran-type branched polymer with both alpha-1,4-linkages (46%) and alpha-1,6-linkages (34%)
Products: -
Products: -
?
sucrose
highly branched soluble glucan + D-fructose + ?
-
Substrates: the enzyme produces a highly branched, soluble glucan in which the majority of the linkages are of the alpha-(1->4) glucosidic type. The glucan also contains alpha(1->6)-linked glucosyl units and 4,6-disubstituted alpha-glucosyl units at the branching points
Products: -
Products: -
?
sucrose
highly branched soluble glucan + D-fructose + ?
-
Substrates: the enzyme produces a highly branched, soluble glucan in which the majority of the linkages are of the alpha-(1->4) glucosidic type. The glucan also contains alpha(1->6)-linked glucosyl units and 4,6-disubstituted alpha-glucosyl units at the branching points
Products: -
Products: -
?
sucrose
reuteran
-
Substrates: -
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
K+
-
K+ has stimulating effects on the enzyme activities (158% transferase activity and 122% hydrolysis activity at 1 mM)
Mg2+
-
Mg2+ has stimulating effects on the enzyme activities (151% transferase activity and 109% hydrolysis activity at 1 mM)
Na+
-
Na+ has stimulating effect on the transferase activity of the enzyme (121% activity at 1 mM)
Ca2+
-
Ca2+ has the most stimulating effect, with hydrolysis and transferase activities increasing 2 and 8fold, respectively. 1 mM Ca2+ is used in assay conditions
Ca2+
-
1 mM used in assay conditions
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Cu2+
-
Cu2+ significantly inhibits both enzyme activities, but especially the transferase activity (complete inhibition at 1 mM)
EDTA
-
EDTA inhibits transferase activity completely, but hydrolysis remains almost unaffected (89% residual activity at 1 mM)
Fe2+
-
Fe2+ significantly inhibits both enzyme activities, but especially the transferase activity (complete inhibition at 1 mM)
Fe3+
-
Fe3+ significantly inhibits both enzyme activities, but especially the transferase activity (complete inhibition at 1 mM)
Hg2+
-
Hg2+ significantly inhibits both enzyme activities, but especially the transferase activity (complete inhibition at 1 mM)
Zn2+
-
Zn2+ significantly inhibits both enzyme activities, but especially the transferase activity (complete inhibition at 1 mM)
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.8
sucrose
-
His6-tagged enzyme, hydrolysis activity, at pH 4.7 and 50°C
0.9
sucrose
-
His6-tagged enzyme, total activity, at pH 4.7 and 50°C
0.9
sucrose
-
total activity, wild type enzyme, at pH 4.7 and 50°C
1
sucrose
-
hydrolysis activity, wild type enzyme, at pH 4.7 and 50°C
1.1
sucrose
-
total activity, mutant enzyme A1066N, at pH 4.7 and 50°C
1.1
sucrose
-
total activity, mutant enzyme P1026V/I1029V/A1066N, at pH 4.7 and 50°C
1.1
sucrose
-
hydrolysis activity, mutant enzyme A1066N, at pH 4.7 and 50°C
1.1
sucrose
-
hydrolysis activity, mutant enzyme H1065S/A1066S, at pH 4.7 and 50°C
1.2
sucrose
-
total activity, mutant enzyme P1026V/I1029V, at pH 4.7 and 50°C
1.2
sucrose
-
total activity, mutant enzyme H1065S/A1066S, at pH 4.7 and 50°C
1.2
sucrose
-
hydrolysis activity, mutant enzyme P1026V/I1029V/A1066N, at pH 4.7 and 50°C
1.3
sucrose
-
hydrolysis activity, mutant enzyme I1029V, at pH 4.7 and 50°C
1.4
sucrose
-
total activity, mutant enzyme I1029V, at pH 4.7 and 50°C
1.4
sucrose
-
hydrolysis activity, mutant enzyme P1026V/I1029V, at pH 4.7 and 50°C
1.6
sucrose
-
hydrolysis activity, mutant enzyme P1026V, at pH 4.7 and 50°C
1.8
sucrose
-
total activity, mutant enzyme P1026V, at pH 4.7 and 50°C
2.2
sucrose
-
hydrolysis activity, mutant enzyme P1026V/I1029V/A1066N/N1134S/N1135E/S1136V, at pH 4.7 and 50°C
2.3
sucrose
-
hydrolysis activity, mutant enzyme P1026V/I1029V/N1134S/N1135E/S1136V, at pH 4.7 and 50°C
2.6
sucrose
-
hydrolysis activity, mutant enzyme N1134S/N1135E/S1136V, at pH 4.7 and 50°C
2.8
sucrose
-
hydrolysis activity, mutant enzyme A1066N/N1134S/N1135E/S1136V, at pH 4.7 and 50°C
3.3
sucrose
-
transferase activity, mutant enzyme A1066N, at pH 4.7 and 50°C
4.1
sucrose
-
total activity, mutant enzyme P1026V/I1029V/A1066N/N1134S/N1135E/S1136V, at pH 4.7 and 50°C
4.6
sucrose
-
His6-tagged enzyme, tranferase activity, at pH 4.7 and 50°C
4.8
sucrose
-
total activity, mutant enzyme P1026V/I1029V/N1134S/N1135E/S1136V, at pH 4.7 and 50°C
4.8
sucrose
-
transferase activity, wild type enzyme, at pH 4.7 and 50°C
5.1
sucrose
-
transferase activity, mutant enzyme P1026V/I1029V/A1066N, at pH 4.7 and 50°C
7.9
sucrose
-
total activity, mutant enzyme A1066N/N1134S/N1135E/S1136V, at pH 4.7 and 50°C
8.3
sucrose
-
transferase activity, mutant enzyme P1026V, at pH 4.7 and 50°C
8.5
sucrose
-
total activity, mutant enzyme N1134S/N1135E/S1136V, at pH 4.7 and 50°C
8.5
sucrose
-
transferase activity, mutant enzyme I1029V, at pH 4.7 and 50°C
9
sucrose
-
transferase activity, mutant enzyme P1026V/I1029V, at pH 4.7 and 50°C
33.1
sucrose
-
transferase activity, mutant enzyme P1026V/I1029V/A1066N/N1134S/N1135E/S1136V, at pH 4.7 and 50°C
36.7
sucrose
-
transferase activity, mutant enzyme P1026V/I1029V/N1134S/N1135E/S1136V, at pH 4.7 and 50°C
224.9
sucrose
-
transferase activity, mutant enzyme A1066N/N1134S/N1135E/S1136V, at pH 4.7 and 50°C
540.9
sucrose
-
transferase activity, mutant enzyme N1134S/N1135E/S1136V, at pH 4.7 and 50°C
additional information
amylose
Km: 2.58 mg/ml, pH 5.0, 40°C, wild-type enzyme
additional information
amylose
Km: 4.21 mg/ml, pH 5.0, 40°C, mutant enzyme H1056G
additional information
amylose
Km: 1.75 mg/ml, pH 5.0, 40°C, mutant enzyme Q1126I
additional information
amylose
Km: 2.7 mg/ml, pH 5.0, 40°C, mutant enzyme I1020M
additional information
amylose
Km: 1.08 mg/ml, pH 5.0, 40°C, mutant enzyme S1057P
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
36.8
sucrose
-
His6-tagged enzyme, tranferase activity, at pH 4.7 and 50°C
66.2
sucrose
-
His6-tagged enzyme, hydrolysis activity, at pH 4.7 and 50°C
83.1
sucrose
-
His6-tagged enzyme, total activity, at pH 4.7 and 50°C
293
sucrose
-
His6-tagged enzyme, with maltose as cosubstrate, total activity, at pH 4.7 and 50°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
amylose
-
kcat/Km: 2.25 mg/min*ml, pH 6.0, 40°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
56.6
sucrose
-
hydrolysis activity, mutant enzyme H1065S/A1066S, at pH 4.7 and 50°C
76.2
sucrose
-
hydrolysis activity, mutant enzyme P1026V/I1029V, at pH 4.7 and 50°C
95.7
sucrose
-
hydrolysis activity, mutant enzyme P1026V/I1029V/A1066N, at pH 4.7 and 50°C
103.4
sucrose
-
hydrolysis activity, mutant enzyme A1066N, at pH 4.7 and 50°C
105.6
sucrose
-
hydrolysis activity, mutant enzyme I1029V, at pH 4.7 and 50°C
106.9
sucrose
-
hydrolysis activity, wild type enzyme, at pH 4.7 and 50°C
111
sucrose
-
His6-tagged enzyme, hydrolysis activity, at pH 4.7 and 50°C
144.9
sucrose
-
hydrolysis activity, mutant enzyme P1026V, at pH 4.7 and 50°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Limosilactobacillus reuteri ATCC 55730
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
the enzyme belongs to the GH70 family glucansucrases. Depending on their synthesized alpha-glucan products, glucansucrases are mainly divided into dextransucrase (EC 2.4.1.5), reuteransucrase (EC 2.4.1.395), mutansucrase (EC 2.4.1.125), and alternansucrase (EC 2.4.1.140). According to their N-terminally truncated crystal structures, the polypeptide chains of glucansucrases employ a U-shaped fold composed of five structural domains (A, B, C, IV, and V). Only 11 residues of the N-terminally truncated Gtf-DSM (EC 2.4.1.5) are different from those of N-terminally truncated GtfO (EC 2.4.1.395). Sequence and domain comparisons of Gtf-DSM and GtfO, overview
evolution
Limosilactobacillus reuteri ATCC 55730
-
the enzyme belongs to the GH70 family glucansucrases. Depending on their synthesized alpha-glucan products, glucansucrases are mainly divided into dextransucrase (EC 2.4.1.5), reuteransucrase (EC 2.4.1.395), mutansucrase (EC 2.4.1.125), and alternansucrase (EC 2.4.1.140). According to their N-terminally truncated crystal structures, the polypeptide chains of glucansucrases employ a U-shaped fold composed of five structural domains (A, B, C, IV, and V). Only 11 residues of the N-terminally truncated Gtf-DSM (EC 2.4.1.5) are different from those of N-terminally truncated GtfO (EC 2.4.1.395). Sequence and domain comparisons of Gtf-DSM and GtfO, overview
-
malfunction
combined mutations of three continuous residues N1134, N1135, and S1136, following transition-state stabilizer D1133, in Limosilactobacillus reuteri 121 GtfA transforms the major linkage from (alpha1-4) to (alpha1-6) linkages
malfunction
Limosilactobacillus reuteri ATCC 55730
-
combined mutations of three continuous residues N1134, N1135, and S1136, following transition-state stabilizer D1133, in Limosilactobacillus reuteri 121 GtfA transforms the major linkage from (alpha1-4) to (alpha1-6) linkages
-
metabolism
-
the enzyme modifies starch by cleaving (alpha1->4) linkages and introducing non-branched (alpha1->6) linkages to produce functional starch derivatives
metabolism
-
the enzyme modifies starch by cleaving (alpha1->4) linkages and introducing non-branched (alpha1->6) linkages to produce functional starch derivatives
-
physiological function
reuteransucrase GtfO from Limosilactobacillus reuteri strain ATCC 55730 synthesizes a reuteran composed of 21% (alpha1-6) and 79% (alpha1-4) linkages
physiological function
Limosilactobacillus reuteri ATCC 55730
-
reuteransucrase GtfO from Limosilactobacillus reuteri strain ATCC 55730 synthesizes a reuteran composed of 21% (alpha1-6) and 79% (alpha1-4) linkages
-
additional information
-
linkage specificity differences between Gtf-DSM and reuteransucrase GtfO (EC 2.4.1.395), determined by the distinct micro-physicochemical environments, are formed by the concerted action of a series of residues not only from the acceptor binding subsites +1 and +2 but also from domains IV and V, linkage specificity comparison, overview
additional information
linkage specificity differences between Gtf-DSM and reuteransucrase GtfO (EC 2.4.1.395), determined by the distinct micro-physicochemical environments, are formed by the concerted action of a series of residues not only from the acceptor binding subsites +1 and +2 but also from domains IV and V, linkage specificity comparison, overview
additional information
Limosilactobacillus reuteri ATCC 55730
-
linkage specificity differences between Gtf-DSM and reuteransucrase GtfO (EC 2.4.1.395), determined by the distinct micro-physicochemical environments, are formed by the concerted action of a series of residues not only from the acceptor binding subsites +1 and +2 but also from domains IV and V, linkage specificity comparison, overview
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Q4JCS4_LIMRT
1781
0
196912
TrEMBL
Mitochondrion (Reliability: 3)
Q5SBM0_LIMRT
1619
0
179412
TrEMBL
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
-
x * 197170, N-terminal deletion mutant, calculated from amino acid sequence
?
-
x * 194000, full-length enzyme, calculated from amino acid sequence
?
x * 99000, SDS-PAGE, N-terminally truncated wild-type enzyme
?
Limosilactobacillus reuteri ATCC 55730
-
x * 197170, N-terminal deletion mutant, calculated from amino acid sequence
-
?
Limosilactobacillus reuteri ATCC 55730
-
x * 194000, full-length enzyme, calculated from amino acid sequence
-
monomer
1 * 117900, enzyme fragment comprising residues 745-1763 and including the catalytic domain, calculated from amino acid sequence
monomer
-
1 * 117900, enzyme fragment comprising residues 745-1763 and including the catalytic domain, calculated from amino acid sequence
-
additional information
-
the enzyme contains five structural domains, A, B, C, IV, and V. Domain A harbors a circularly permutated (beta/alpha)8 barrel catalytic core compared to that of GH13 family enzymes. The circularly permutated (beta/alpha) domain A contains four conserved sequence motifs (I, II, III, and IV) with a catalytic triad (the nucleophile Asp1025, acid/base catalyst Glu1063, and transition-state-stabilizer Asp1136, Gtf180 numbering). Domain B possesses several amino acids forming the substrate or acceptor binding subsites involved in the glucansucrase product specificity
additional information
the enzyme contains five structural domains, A, B, C, IV, and V. Domain A harbors a circularly permutated (beta/alpha)8 barrel catalytic core compared to that of GH13 family enzymes. The circularly permutated (beta/alpha) domain A contains four conserved sequence motifs (I, II, III, and IV) with a catalytic triad (the nucleophile Asp1025, acid/base catalyst Glu1063, and transition-state-stabilizer Asp1136, Gtf180 numbering). Domain B possesses several amino acids forming the substrate or acceptor binding subsites involved in the glucansucrase product specificity
additional information
Limosilactobacillus reuteri ATCC 55730
-
the enzyme contains five structural domains, A, B, C, IV, and V. Domain A harbors a circularly permutated (beta/alpha)8 barrel catalytic core compared to that of GH13 family enzymes. The circularly permutated (beta/alpha) domain A contains four conserved sequence motifs (I, II, III, and IV) with a catalytic triad (the nucleophile Asp1025, acid/base catalyst Glu1063, and transition-state-stabilizer Asp1136, Gtf180 numbering). Domain B possesses several amino acids forming the substrate or acceptor binding subsites involved in the glucansucrase product specificity
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A1066N
-
the mutant displays similar kinetic parameters as wild type enzyme
A1066N/N1134S/N1135E/S1136V
-
the mutant shows no transferase activity at low sucrose concentrations
A977D
A977Q/G1087N
-
the mutant shows increased activity compared to the wild type enzyme
A977Q/V1083D
-
the mutant shows increased activity compared to the wild type enzyme
A977Q/V1083D/G1087N
-
the mutant shows increased activity compared to the wild type enzyme
D1024N
-
the mutant shows a 1000fold reduction of total enzyme activity compared to the wild type enzyme
D1133N
-
the mutation results in a 300fold reduced total activity compared to the wild type enzyme
E1061Q
-
the mutant shows a 1000fold reduction of total enzyme activity compared to the wild type enzyme
G1086Q
the mutant synthesizes alpha-glucan products with 70% (alpha1->3) and 30% alpha(1->6) linkages (but no (alpha1->4) linkages) from sucrose
G1087K
site-directed mutagenesis, the mutant shows altered linkage specificity compared to wild-type enzyme
G758V
G758V/H765Q/Y768D
G758V/H765Q/Y768D/N889S
H1056G
the mutant enzyme shows a decreased total activity and is more hydrolytic than the wild-type enzyme
H1065S/A1066S
-
the mutant lacks transferase activity .The hydrolytic activity of this mutant is 2fold lower than in wild type, whereas the affinity for sucrose in the hydrolysis reaction is 2fold higher compared to wild type
H765Q
I1020M
the total activity and hydrolytic activity of the mutant are similar to those of the N-terminally truncated wild-type enzyme
I1029V
-
the mutant displays 1.5-2fold higher activities than wild type in all three reactions catalyzed
K1086Q
L937I
L937I/A977D
the mutant synthesizes alpha-glucan products with 64% (alpha1->3) and 36% alpha(1->6) linkages (but no (alpha1->4) linkages) from sucrose
L937I/A977D/V1083D/K1086Q/G1087K
N1134A
-
the mutant shows 2fold increased activity compared to the wild type enzyme
N1134D
-
the mutant shows 2fold increased activity compared to the wild type enzyme
N1134E
-
the mutant shows increased activity compared to the wild type enzyme
N1134G
-
the mutant shows decreased activity compared to the wild type enzyme
N1134H
-
the mutant shows decreased activity compared to the wild type enzyme
N1134Q
-
the mutant shows decreased activity compared to the wild type enzyme
N1134S
N1134S/N1135E
-
the mutant synthesized more alpha-(1->6) glucosidic linkages in their polymers, as previously observed for the enzyme triple mutant N1134S/N1135E/S1136V
N1134S/N1135E/S1136V
N1134S/S1136V
-
the mutant synthesized more alpha-(1->6) glucosidic linkages in their polymers, as previously observed for the enzyme triple mutant N1134S/N1135E/S1136V
N1134Y
-
the mutant shows increased activity compared to the wild type enzyme
N889S
P1026V
-
the mutant displays 1.5-2fold higher activities than wild type in all three reactions catalyzed
P1026V/I1029V
-
the mutant displays 1.5-2fold higher activities than wild type in all three reactions catalyzed
P1026V/I1029V/A1066N
-
the mutations result in higher activities in all reactions, whereas affinities for the substrate sucrose are comparable to wild type levels in all reactions
P1026V/I1029V/A1066N/N1134S/N1135E/S1136V
-
the mutant displays similar kinetic parameters as wild type enzyme
P1026V/I1029V/N1134S/N1135E/S1136V
-
the mutations result in synthesis of an alpha-glucan containing a very small percentage of R-(1->4) glucosidic linkages (about 5%) and an increased percentage of alpha-(1->6) glucosidic linkages (about 85%)
Q1126I
compared to wild-type enzyme, the mutant enzyme has considerably improved catalytic efficiencies. The mutant shows an 11% increase in catalytic efficiency, in the ratio of (alpha1->6) over (alpha1->4) linkages in maltodextrin-derived products
S1057P
compared to wild-type enzyme, the mutant enzyme has considerably improved catalytic efficiencies. The mutant shows a 9% decrease in catalytic efficiency, in the ratio of (alpha1->6) over (alpha1->4) linkages in maltodextrin-derived products
S1062N
-
the mutant maintains enzyme activity but increases the proportion of alpha-(1->4) linkages
S1135N/A1137S
-
the mutant produces reuteran with a higher proportion of alpha-(1->4) linkages (39%) when compared to the wild type (14%). The mutant yields the same total activity but a lower ratio of transferase activity to hydrolysis activity compared to the wild type enzyme
V1024P/V1027I
-
the mutant produces reuteran with a higher proportion of alpha-(1->4) linkages (25%) when compared to the wild type (14%). The mutant yields the same total activity but a lower ratio of transferase activity to hydrolysis activity compared to the wild type enzyme
V1024P/V1027I/S1135N/A1137S
-
the mutant produces reuteran with a higher proportion of alpha-(1->4) linkages (51%) when compared to the wild type (14%). The mutant shows a significant decreased total activity and relative transferase activity compared to the wild type enzyme
V1083D
V1083D/K1086Q/G1087K
the mutant synthesizes alpha-glucan products with 63% (alpha1->3) and 37% alpha(1->6) linkages (but no (alpha1->4) linkages) from sucrose
Y768D
A977Q/G1087N
-
the mutant shows increased activity compared to the wild type enzyme
-
A977Q/V1083D
-
the mutant shows increased activity compared to the wild type enzyme
-
A977Q/V1083D/G1087N
-
the mutant shows increased activity compared to the wild type enzyme
-
D1024N
-
the mutant shows a 1000fold reduction of total enzyme activity compared to the wild type enzyme
-
D1133N
-
the mutation results in a 300fold reduced total activity compared to the wild type enzyme
-
E1061Q
-
the mutant shows a 1000fold reduction of total enzyme activity compared to the wild type enzyme
-
H1065S/A1066S
-
the mutant lacks transferase activity .The hydrolytic activity of this mutant is 2fold lower than in wild type, whereas the affinity for sucrose in the hydrolysis reaction is 2fold higher compared to wild type
-
N1134G
-
the mutant shows decreased activity compared to the wild type enzyme
-
N1134Q
-
the mutant shows decreased activity compared to the wild type enzyme
-
N1134S
-
the mutation greatly influences the hydrolysis :transglycosylation ratio and expands the range of glucan and glucooligosaccharide products synthesized from sucrose
-
N1134S/N1135E
-
the mutant synthesized more alpha-(1->6) glucosidic linkages in their polymers, as previously observed for the enzyme triple mutant N1134S/N1135E/S1136V
-
N1134S/N1135E/S1136V
-
the mutations convert the enzyme from a mainly alpha-(1->4) (about 45%, reuteran) to a mainly alpha-(1->6) (about 80%, dextran) synthesizing enzyme. The mutant shows no transferase activity at low sucrose concentrations
-
N1134S/S1136V
-
the mutant synthesized more alpha-(1->6) glucosidic linkages in their polymers, as previously observed for the enzyme triple mutant N1134S/N1135E/S1136V
-
P1026V/I1029V/N1134S/N1135E/S1136V
-
the mutations result in synthesis of an alpha-glucan containing a very small percentage of R-(1->4) glucosidic linkages (about 5%) and an increased percentage of alpha-(1->6) glucosidic linkages (about 85%)
-
S1057P
-
compared to wild-type enzyme, the mutant enzyme has considerably improved catalytic efficiencies. The mutant shows a 9% decrease in catalytic efficiency, in the ratio of (alpha1->6) over (alpha1->4) linkages in maltodextrin-derived products
-
A977D
Limosilactobacillus reuteri ATCC 55730
-
the mutant synthesizes alpha-glucan products with 67% (alpha1->3) and 33% alpha(1->6) linkages (but no (alpha1->4) linkages) from sucrose
-
A977Q/G1087N
Limosilactobacillus reuteri ATCC 55730
-
the mutant shows increased activity compared to the wild type enzyme
-
A977Q/V1083D
Limosilactobacillus reuteri ATCC 55730
-
the mutant shows increased activity compared to the wild type enzyme
-
A977Q/V1083D/G1087N
Limosilactobacillus reuteri ATCC 55730
-
the mutant shows increased activity compared to the wild type enzyme
-
G1086Q
Limosilactobacillus reuteri ATCC 55730
-
the mutant synthesizes alpha-glucan products with 70% (alpha1->3) and 30% alpha(1->6) linkages (but no (alpha1->4) linkages) from sucrose
-
G758V
Limosilactobacillus reuteri ATCC 55730
-
site-directed mutagenesis, the mutant shows altered linkage specificity compared to wild-type enzyme
-
H765Q
Limosilactobacillus reuteri ATCC 55730
-
site-directed mutagenesis, the mutant shows altered linkage specificity compared to wild-type enzyme
-
K1086Q
Limosilactobacillus reuteri ATCC 55730
-
the mutant synthesizes alpha-glucan products with 67% (alpha1->3) and 33% alpha(1->6) linkages (but no (alpha1->4) linkages) from sucrose
-
L937I
Limosilactobacillus reuteri ATCC 55730
-
the mutant synthesizes alpha-glucan products with 64% (alpha1->3) and 36% alpha(1->6) linkages (but no (alpha1->4) linkages) from sucrose
-
N889S
Limosilactobacillus reuteri ATCC 55730
-
site-directed mutagenesis, the mutant shows altered linkage specificity compared to wild-type enzyme
-
V1083D
Limosilactobacillus reuteri ATCC 55730
-
the mutant synthesizes alpha-glucan products with 67% (alpha1->3) and 33% alpha(1->6) linkages (but no (alpha1->4) linkages) from sucrose
-
Y768D
Limosilactobacillus reuteri ATCC 55730
-
site-directed mutagenesis, the mutant shows altered linkage specificity compared to wild-type enzyme
-
S1062N
Limosilactobacillus reuteri TMW1.656
-
the mutant maintains enzyme activity but increases the proportion of alpha-(1->4) linkages
-
S1135N/A1137S
Limosilactobacillus reuteri TMW1.656
-
the mutant produces reuteran with a higher proportion of alpha-(1->4) linkages (39%) when compared to the wild type (14%). The mutant yields the same total activity but a lower ratio of transferase activity to hydrolysis activity compared to the wild type enzyme
-
V1024P/V1027I
Limosilactobacillus reuteri TMW1.656
-
the mutant produces reuteran with a higher proportion of alpha-(1->4) linkages (25%) when compared to the wild type (14%). The mutant yields the same total activity but a lower ratio of transferase activity to hydrolysis activity compared to the wild type enzyme
-
V1024P/V1027I/S1135N/A1137S
Limosilactobacillus reuteri TMW1.656
-
the mutant produces reuteran with a higher proportion of alpha-(1->4) linkages (51%) when compared to the wild type (14%). The mutant shows a significant decreased total activity and relative transferase activity compared to the wild type enzyme
-
S622N
-
the mutant has low reuteransucrase activity and an unaltered proportion of alpha-(1->4) linkages
V583P/V586I
-
the mutant has reuteransucrase activity but does not increase the proportion of alpha-(1->4) linkages
S622N
-
the mutant has low reuteransucrase activity and an unaltered proportion of alpha-(1->4) linkages
-
V583P/V586I
-
the mutant has reuteransucrase activity but does not increase the proportion of alpha-(1->4) linkages
-
additional information
A977D
the mutant synthesizes alpha-glucan products with 67% (alpha1->3) and 33% alpha(1->6) linkages (but no (alpha1->4) linkages) from sucrose
A977D
site-directed mutagenesis, the mutant shows altered linkage specificity compared to wild-type enzyme
G758V
the mutant synthesizes reuteran with 77% (alpha1->4) and 23% alpha(1->6) linkages from sucrose
G758V
site-directed mutagenesis, the mutant shows altered linkage specificity compared to wild-type enzyme
G758V/H765Q/Y768D
the mutant synthesizes reuteran with 75% (alpha1->4) and 25% alpha(1->6) linkages from sucrose
G758V/H765Q/Y768D
site-directed mutagenesis, the mutant shows altered linkage specificity compared to wild-type enzyme
G758V/H765Q/Y768D/N889S
the mutant synthesizes reuteran with 77% (alpha1->4) and 23% alpha(1->6) linkages from sucrose
G758V/H765Q/Y768D/N889S
site-directed mutagenesis, the mutant shows altered linkage specificity compared to wild-type enzyme
H765Q
the mutant synthesizes reuteran with 78% (alpha1->4) and 22% alpha(1->6) linkages from sucrose
H765Q
site-directed mutagenesis, the mutant shows altered linkage specificity compared to wild-type enzyme
K1086Q
the mutant synthesizes alpha-glucan products with 67% (alpha1->3) and 33% alpha(1->6) linkages (but no (alpha1->4) linkages) from sucrose
K1086Q
site-directed mutagenesis, the mutant shows altered linkage specificity compared to wild-type enzyme
L937I
the mutant synthesizes alpha-glucan products with 64% (alpha1->3) and 36% alpha(1->6) linkages (but no (alpha1->4) linkages) from sucrose
L937I
site-directed mutagenesis, the mutant shows altered linkage specificity compared to wild-type enzyme
L937I/A977D/V1083D/K1086Q/G1087K
the mutant synthesizes alpha-glucan products with 53% (alpha1->3) and 47% alpha(1->6) linkages (but no (alpha1->4) linkages) from sucrose
L937I/A977D/V1083D/K1086Q/G1087K
site-directed mutagenesis, the mutant shows altered linkage specificity compared to wild-type enzyme
N1134S
-
the mutation greatly influences the hydrolysis :transglycosylation ratio and expands the range of glucan and glucooligosaccharide products synthesized from sucrose
N1134S
-
the mutant shows 2fold increased activity compared to the wild type enzyme
N1134S/N1135E/S1136V
-
the mutations convert the enzyme from a mainly alpha-(1->4) (about 45%, reuteran) to a mainly alpha-(1->6) (about 80%, dextran) synthesizing enzyme. The mutant shows no transferase activity at low sucrose concentrations
N1134S/N1135E/S1136V
-
the mutations convert the enzyme from a mainly reuteran [about 45%, alpha-(1->4)] into a mainly dextran [about 80%, alpha-(1->6)] synthesizing enzyme. The mutant shows increased activity compared to the wild type enzyme
N889S
the mutant synthesizes reuteran with 80% (alpha1->4) and 20% alpha(1->6) linkages from sucrose
N889S
site-directed mutagenesis, the mutant shows altered linkage specificity compared to wild-type enzyme
V1083D
the mutant synthesizes alpha-glucan products with 67% (alpha1->3) and 33% alpha(1->6) linkages (but no (alpha1->4) linkages) from sucrose
V1083D
site-directed mutagenesis, the mutant shows altered linkage specificity compared to wild-type enzyme
Y768D
the mutant synthesizes reuteran with 79% (alpha1->4) and 21% alpha(1->6) linkages from sucrose
Y768D
site-directed mutagenesis, the mutant shows altered linkage specificity compared to wild-type enzyme
additional information
-
deletion of the complete N-terminal variable domain of the enzyme (GTFA-DELTAN) has little effect on reuteran characteristics (size, distribution of glycosidic linkages), but the initial transferase activity of the mutant enzyme increases drastically. Sequential C-terminal deletions (up to six YG repeats) in GTFA-DELTAN also has little effect on reuteran characteristics. However, enzyme kinetics drastically change. Deletion of 7, 8 or 11 YG repeats results in dramatic loss of total enzyme activity (43, 63 and 1000fold-reduced specific activities, respectively)
additional information
-
9 residues in the reuteransucrase GtfO are transformed into the residues of corresponding sites in the dextransucrase Gtf-DSM (EC 2.4.1.5) to construct nine single-point mutants and five multiple-point mutants. The combinatorial mutations in Gtf-DSM (EC 2.4.1.5) at the acceptor binding subsites +1 and +2 nearly converts the linkage specificity of enzyme Gtf-DSM to that of GtfO. All of the individual or combinatorial mutations in four residues from domains IV and V of Gtf-DSM significantly alter the linkage specificity of Gtf-DSM. All GtfO mutants do not form (alpha1->4) linkages, but do form (alpha1->3) linkages, in contrast to the wild-type, linkage specificities, overview
additional information
9 residues in the reuteransucrase GtfO are transformed into the residues of corresponding sites in the dextransucrase Gtf-DSM (EC 2.4.1.5) to construct nine single-point mutants and five multiple-point mutants. The combinatorial mutations in Gtf-DSM (EC 2.4.1.5) at the acceptor binding subsites +1 and +2 nearly converts the linkage specificity of enzyme Gtf-DSM to that of GtfO. All of the individual or combinatorial mutations in four residues from domains IV and V of Gtf-DSM significantly alter the linkage specificity of Gtf-DSM. All GtfO mutants do not form (alpha1->4) linkages, but do form (alpha1->3) linkages, in contrast to the wild-type, linkage specificities, overview
additional information
-
deletion of the complete N-terminal variable domain of the enzyme (GTFA-DELTAN) has little effect on reuteran characteristics (size, distribution of glycosidic linkages), but the initial transferase activity of the mutant enzyme increases drastically. Sequential C-terminal deletions (up to six YG repeats) in GTFA-DELTAN also has little effect on reuteran characteristics. However, enzyme kinetics drastically change. Deletion of 7, 8 or 11 YG repeats results in dramatic loss of total enzyme activity (43, 63 and 1000fold-reduced specific activities, respectively)
-
additional information
Limosilactobacillus reuteri ATCC 55730
-
9 residues in the reuteransucrase GtfO are transformed into the residues of corresponding sites in the dextransucrase Gtf-DSM (EC 2.4.1.5) to construct nine single-point mutants and five multiple-point mutants. The combinatorial mutations in Gtf-DSM (EC 2.4.1.5) at the acceptor binding subsites +1 and +2 nearly converts the linkage specificity of enzyme Gtf-DSM to that of GtfO. All of the individual or combinatorial mutations in four residues from domains IV and V of Gtf-DSM significantly alter the linkage specificity of Gtf-DSM. All GtfO mutants do not form (alpha1->4) linkages, but do form (alpha1->3) linkages, in contrast to the wild-type, linkage specificities, overview
-
additional information
-
replacement of loops at the entrance of the active pocket of Streptococcus thermophilus 4,6-alpha-glucanotransferase changes its catalytic activity and product specificity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography and Resource-Q column chromatography
-
recombinant expression of N-terminally truncated and C-terminally His-tagged wild-type enzyme GtfO and mutants from Escherichia coli strain BL21(DE3) by nickel affiinity chromatography and dialysis
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 Star (DE3) cells
expressed in Escherichia coli BL21(DE3) cells
gene IV41_GL001464, recombinant expression of N-terminally truncated and C-terminally His-tagged enzyme GtfO in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
expressed in Escherichia coli BL21 Star (DE3) cells
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
food industry
food industry
-
the enzyme activity enhances wheat bread volume and texture
food industry
Limosilactobacillus reuteri TMW1.656
-
the enzyme activity enhances wheat bread volume and texture
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kralj, S.; van Geel-Schutten, I.G.; Faber, E.J.; van der Maarel, M.J.; Dijkhuizen, L.
Rational transformation of Lactobacillus reuteri 121 reuteransucrase into a dextransucrase
Biochemistry
44
9206-9216
2005
Limosilactobacillus reuteri, Limosilactobacillus reuteri 121
brenda
Chen, Z.; Tian, Y.; Zhang, W.; Guang, C.; Meng, X.; Mu, W.
Novel dextransucrase Gtf-DSM, highly similar in sequence to reuteransucrase GtfO, displays unique product specificity
J. Agric. Food Chem.
67
12806-12815
2019
Limosilactobacillus reuteri, Limosilactobacillus reuteri 121, Limosilactobacillus reuteri ATCC 55730
brenda
Pijning, T.; Vuji?i?-agar, A.; Kralj, S.; Dijkhuizen, L.; Dijkstra, B.W.
Structure of the alpha-1,6/alpha-1,4-specific glucansucrase GTFA from Lactobacillus reuteri 121
Acta Crystallogr. Sect. F
68
1448-1454
2012
Limosilactobacillus reuteri (Q5SBL9), Limosilactobacillus reuteri 121 (Q5SBL9)
brenda
Kralj, S.; Van Geel-Schutten, G.; Rahaoui, H.; Leer, R.; Faber, E.; Van der Maarel, M.; Dijkhuizen, L.
Molecular characterization of a novel glucosyltransferase from Lactobacillus reuteri strain 121 synthesizing a unique, highly branched glucan with alpha(1->4) and alpha(1->6) glucosidic bonds
Appl. Environ. Microbiol.
68
4283-4291
2002
Limosilactobacillus reuteri, Limosilactobacillus reuteri 121
brenda
Kralj, S.; Stripling, E.; Sanders, P.; van Geel-Schutten, G.H.; Dijkhuizen, L.
Highly hydrolytic reuteransucrase from probiotic Lactobacillus reuteri strain ATCC 55730
Appl. Environ. Microbiol.
71
3942-3950
2005
Limosilactobacillus reuteri, Limosilactobacillus reuteri ATCC 55730
brenda
Meng, X.; Dobruchowska, J.M.; Gerwig, G.J.; Kamerling, J.P.; Dijkhuizen, L.
Synthesis of oligo- and polysaccharides by Lactobacillus reuteri 121 reuteransucrase at high concentrations of sucrose
Carbohydr. Res.
414
85-92
2015
Limosilactobacillus reuteri, Limosilactobacillus reuteri 121
brenda
Kralj, S.; Eeuwema, W.; Eckhardt, T.H.; Dijkhuizen, L.
Role of asparagine 1134 in glucosidic bond and transglycosylation specificity of reuteransucrase from Lactobacillus reuteri 121
FEBS J.
273
3735-3742
2006
Limosilactobacillus reuteri, Limosilactobacillus reuteri 121
brenda
Kralj, S.; van Leeuwen, S.S.; Valk, V.; Eeuwema, W.; Kamerling, J.P.; Dijkhuizen, L.
Hybrid reuteransucrase enzymes reveal regions important for glucosidic linkage specificity and the transglucosylation/hydrolysis ratio
FEBS J.
275
6002-6010
2008
Limosilactobacillus reuteri, Limosilactobacillus reuteri 121, Limosilactobacillus reuteri ATCC 55730
brenda
Yang, Y.; Ma, Y.; Hu, X.; Cui, S.W.; Zhang, T.; Miao, M.
Reuteransucrase-catalytic kinetic modeling and functional characteristics for novel prebiotic gluco-oligomers
Food Funct.
11
7037-7047
2020
Limosilactobacillus reuteri, Limosilactobacillus reuteri SK24.003
brenda
Dobruchowska, J.M.; Meng, X.; Leemhuis, H.; Gerwig, G.J.; Dijkhuizen, L.; Kamerling, J.P.
Gluco-oligomers initially formed by the reuteransucrase enzyme of Lactobacillus reuteri 121 incubated with sucrose and malto-oligosaccharides
Glycobiology
23
1084-1096
2013
Limosilactobacillus reuteri, Limosilactobacillus reuteri 121
brenda
Hassanein, W.; Ispirli, H.; Dertli, E.; Yilmaz, M.
Structural characterization of potato starch modified by a 4,6-alpha-glucanotransferase B from Lactobacillus reuteri E81
Int. J. Biol. Macromol.
242
124988
2023
Limosilactobacillus reuteri
brenda
Li, X.; Jiang, T.; Wang, Y.; Dong, J.; Jin, Z.; Bai, Y.
Exploring the roles of amylopectin in starch modification with Limosilactobacillus reuteri 121 4,6-alpha-glucanotransferase via developed methods
Int. J. Biol. Macromol.
243
125040
2023
Limosilactobacillus reuteri, Limosilactobacillus reuteri 121
brenda
Chen, X.Y.; Levy, C.; Gaenzle, M.G.
Structure-function relationships of bacterial and enzymatically produced reuterans and dextran in sourdough bread baking application
Int. J. Food Microbiol.
239
95-102
2016
Limosilactobacillus reuteri, Limosilactobacillus reuteri TMW1.656
brenda
Chen, Z.; Ni, D.; Cheng, M.; Zhu, Y.; Mu, W.
Comparative study of physicochemical properties of dextran and reuteran synthesised by two glucansucrases that are highly similar in amino acid sequence
Int. J. Food Sci. Technol.
56
6674-6684
2021
Limosilactobacillus reuteri, Limosilactobacillus reuteri ATCC 55730
-
brenda
Chen, X.Y.; Gaenzle, M.G.
Site directed mutagenesis of dextransucrase DsrM from Weissella cibaria Transformation to a reuteransucrase
J. Agric. Food Chem.
64
6848-6855
2016
Weissella cibaria, Limosilactobacillus reuteri, Limosilactobacillus reuteri TMW1.656, Weissella cibaria 10M
brenda
Chen, Z.; Chen, J.; Huang, Z.; Ni, D.; Tian, Y.; Mu, W.
Mutations in the different residues between dextransucrase Gtf-DSM and reuteransucrase GtfO for the investigation of linkage specificity determinants
J. Agric. Food Chem.
70
12107-12116
2022
Limosilactobacillus reuteri, Limosilactobacillus reuteri (Q4JCS4), Limosilactobacillus reuteri ATCC 55730 (Q4JCS4), Limosilactobacillus reuteri ATCC 55730
brenda
Jiang, Y.; Li, X.; Pijning, T.; Bai, Y.; Dijkhuizen, L.
Mutations in amino acid residues of Limosilactobacillus reuteri 121 GtfB 4,6-alpha-glucanotransferase that affect reaction and product specificity
J. Agric. Food Chem.
70
1952-1961
2022
Limosilactobacillus reuteri (Q5SBM0), Limosilactobacillus reuteri 121 (Q5SBM0)
brenda
Kralj, S.; van Geel-Schutten, G.H.; van der Maarel, M.J.E.C.; Dijkhuizen, L.
Biochemical and molecular characterization of Lactobacillus reuteri 121 reuteransucrase
Microbiology
150
2099-2112
2004
Limosilactobacillus reuteri, Limosilactobacillus reuteri 121
brenda
Meng, X.; Pijning, T.; Dobruchowska, J.M.; Yin, H.; Gerwig, G.J.; Dijkhuizen, L.
Structural determinants of alternating (alpha1->4) and (alpha1->6) linkage specificity in reuteransucrase of Lactobacillus reuteri
Sci. Rep.
6
35261
2016
Limosilactobacillus reuteri, Limosilactobacillus reuteri 121, Limosilactobacillus reuteri ATCC 55730
brenda
Dong, J.; Wang, Y.; Fan, R.; Zhang, B.; Li, X.; Jin, Z.; Bai, Y.
Structural and property characterization of low-molecular-weight novel reuterans synthesized from pea starch by Limosilactobacillus reuteri N1 GtfB with 4,6-alpha-glucanotransferase II activity
Int. J. Biol. Macromol.
281
136396
2024
Limosilactobacillus reuteri, Limosilactobacillus reuteri N1
brenda
Li, D.; Xu, W.; Mu, S.; Gao, X.; Ma, F.; Duan, C.; Li, X.
Replacement of loops at the entrance of the active pocket of Streptococcus thermophilus 4,6-alpha-glucanotransferase changes its catalytic activity and product specificity
J. Agric. Food Chem.
72
12607-12617
2024
Streptococcus thermophilus
brenda
EXTERNAL LINKS (specific for EC-Number 2.4.1.395)
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