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Information on EC 2.4.1.140 - alternansucrase
for references in articles please use BRENDA:EC2.4.1.140
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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 by which they attach the transferred residue. In some cases, in which the enzyme forms more than one linkage type, classification relies on the relative proportion of the linkages that are generated. This enzyme forms both α(1→3) and α(1→6) linkages in approximately equal amounts by alternating the linkage type. cf. EC 2.4.1.125, sucrose—1,6-α-glucan 3(6)-α-glucosyltransferase.
The enzyme appears in viruses and cellular organisms
- 2.4.1.140
- leuconostoc
- mesenteroides
- lactobacillus
- dextrans
-
glucosylated
- dextransucrase
-
prebiotic
- citreum
- gluco-oligosaccharides
-
reuteransucrase
-
reuteran
-
glucosyltransferases
- weissella
- confusa
- levansucrase
- cibaria
- alpha-d-glucans
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glucan-binding
- downei
-
homopolysaccharide
- fructansucrase
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transglucosylation
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alpha-1,6
- synthesis
- drug development
Reaction Schemes
showSynonyms
glucansucrase, alternansucrase, lcalt, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ALT
alternansucrase
ASR
glucansucrase
glucosyltransferase, sucrose-1,6(3)-alpha-glucan 6(3)-alpha-
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-
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Lcalt
sucrose:1,6-, 1,3-alpha-D-glucan 3-alpha- and 6-alpha-D-glucosyltransferase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Transfers alternately an alpha-D-glucosyl residue from sucrose to the 6-position and the 3-position of the non-reducing terminal residue of an alpha-D-glucan, thus producing a glucan having alternating alpha-(1->6)- and alpha-(1->3)-linkages
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
sucrose:(1->6)[(1->3)]-alpha-D-glucan 6(3)-alpha-D-glucosyltransferase
The glucansucrases transfer a D-glucosyl residue from sucrose to a glucan chain. They are classified based on the linkage by which they attach the transferred residue. In some cases, in which the enzyme forms more than one linkage type, classification relies on the relative proportion of the linkages that are generated. This enzyme forms both alpha(1->3) and alpha(1->6) linkages in approximately equal amounts by alternating the linkage type. cf. EC 2.4.1.125, sucrose---1,6-alpha-glucan 3(6)-alpha-glucosyltransferase.
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CAS REGISTRY NUMBER
COMMENTARY
100630-46-4
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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 + butyl alpha-D-glucopyranoside
?
-
Substrates: -
Products: -
Products: -
?
sucrose + leucrose
?
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Substrates: regioselectivity of alternansucrase differs from dextransucrase. Alternansucrase shows greater ability to use leucrose as an acceptor, alternansucrase continues to transfer glucosyl units to leucrose, resulting in some unusual glucosyl-fructose oligosaccharides
Products: -
Products: -
?
sucrose + luteolin
luteolin-3'-O-alpha-D-glucopyranoside + luteolin-4'-O-alpha-D-glucopyranoside
sucrose + methyl alpha-D-allo-pyranoside
methyl alpha-D-glucopyranosyl-(1,6)-alpha-D-allopyranoside + alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-alpha-D-allopyranoside + beta-D-fructofuranose
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Substrates: -
Products: the product methyl alpha-D-glucopyranosyl-(1,6)-alpha-D-allopyranoside is subsequently glucosylated at position 6 to give rise to the trisaccharide methyl alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-alpha-D-allopyranoside. Higher DP products are observed
Products: the product methyl alpha-D-glucopyranosyl-(1,6)-alpha-D-allopyranoside is subsequently glucosylated at position 6 to give rise to the trisaccharide methyl alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-alpha-D-allopyranoside. Higher DP products are observed
?
sucrose + methyl alpha-D-galactopyranoside
methyl alpha-D-glucopyranosyl-(1,3)-alpha-D-galactopyranoside + methyl alpha-D-glucopyranosyl-(1,4)-alpha-D-galactopyranoside + beta-D-fructofuranose
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Substrates: -
Products: two initial products methyl alpha-D-glucopyranosyl-(1,3)-alpha-D-galactopyranoside and methyl alpha-D-glucopyranosyl-(1,4)-alpha-D-galactopyranoside, in a 2.5:1 molar ratio
Products: two initial products methyl alpha-D-glucopyranosyl-(1,3)-alpha-D-galactopyranoside and methyl alpha-D-glucopyranosyl-(1,4)-alpha-D-galactopyranoside, in a 2.5:1 molar ratio
?
sucrose + methyl alpha-D-galactopyranoside
methyl alpha-D-glucopyranosyl-(1,4)-alpha-D-galactopyranoside + methyl alpha-D-glucopyranosyl-(1,3)-alpha-D-galactopyranoside + beta-D-fructofuranose
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Substrates: -
Products: production of methyl alpha-D-glucopyranosyl-(1, 4)-alpha-D-galactopyranoside and methyl alpha-D-glucopyranosyl-(1,3)-alpha-D-galactopyranoside in the ratio 2.5:1
Products: production of methyl alpha-D-glucopyranosyl-(1, 4)-alpha-D-galactopyranoside and methyl alpha-D-glucopyranosyl-(1,3)-alpha-D-galactopyranoside in the ratio 2.5:1
?
sucrose + methyl alpha-D-mannopyranoside
methyl alpha-D-glucopyranosyl-(1,6)-alpha-D-mannopyranoside + methyl-3,6-di-O-alpha-D-glucopyranosyl-alpha-D-mannopyranoside + beta-D-fructofuranose
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Substrates: -
Products: the major initial acceptor product is methyl alpha-D-glucopyranosyl-(1,6)-alpha-D-mannopyranoside, but several minor products are also isolated and characterized, including a 3,6-di-O-substituted mannopyranoside
Products: the major initial acceptor product is methyl alpha-D-glucopyranosyl-(1,6)-alpha-D-mannopyranoside, but several minor products are also isolated and characterized, including a 3,6-di-O-substituted mannopyranoside
?
sucrose + methyl beta-D-galactopyranoside
?
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Substrates: poor substrate
Products: -
Products: -
?
sucrose + methyl beta-D-mannopyranoside
?
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Substrates: poor substrate
Products: -
Products: -
?
sucrose + methyl-beta-D-glucopyranoside
methyl beta-isomaltoside + methyl beta-isomaltotrioside + methyl alpha-D-glucopyranosyl-(1,3)-alpha-D-glucopyranosyl-(1,6)-beta-D-glucopyranoside + beta-D-fructofuranose
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Substrates: -
Products: the initial product arising is methyl beta-isomaltoside, which is subsequently glucosylated to yield methyl beta-isomaltotrioside and methyl alpha-D-glucopyranosyl-(1,3)-alpha-D-glucopyranosyl-(1,6)-beta-D-glucopyranoside
Products: the initial product arising is methyl beta-isomaltoside, which is subsequently glucosylated to yield methyl beta-isomaltotrioside and methyl alpha-D-glucopyranosyl-(1,3)-alpha-D-glucopyranosyl-(1,6)-beta-D-glucopyranoside
?
sucrose + n sucrose
?
Substrates: the enzyme catalyzes the synthesis of both high- and low-molar-mass alternans. The amount of high-molar-mass polymer decreases from 31.5% for the wild-type enzyme to 20.4%, 18.8%, and 18.3%, respectively, for the Q700A and Y717A mutants and the Q700A/Y717A double mutant
Products: -
Products: -
?
sucrose + octyl-alpha-D-glucopyranoside
?
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Substrates: -
Products: -
Products: -
?
stevioside + sucrose
?
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Substrates: transglucosylation
Products: the product is composed of mono-, di-, and triglucosylated stevioside and their isomers
Products: the product is composed of mono-, di-, and triglucosylated stevioside and their isomers
?
stevioside + sucrose
?
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Substrates: transglucosylation
Products: the product is composed of mono-, di-, and triglucosylated stevioside and their isomers
Products: the product is composed of mono-, di-, and triglucosylated stevioside and their isomers
?
sucrose + alpha-D-glucan
alternating-1,6-1,3-alpha-D-glucan
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Substrates: -
Products: -
Products: -
?
sucrose + alpha-D-glucan
alternating-1,6-1,3-alpha-D-glucan
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Substrates: -
Products: -
Products: -
?
sucrose + alpha-D-glucan
alternating-1,6-1,3-alpha-D-glucan
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Substrates: -
Products: -
Products: -
?
sucrose + alpha-D-glucan
alternating-1,6-1,3-alpha-D-glucan
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Substrates: -
Products: -
Products: -
?
sucrose + alpha-D-glucan
alternating-1,6-1,3-alpha-D-glucan
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Substrates: -
Products: the product is an insoluble D-glucan that consists of 76 mol% 1,3-alpha-linked glucose and 24 mol% 1,6-alpha-linked glucose
Products: the product is an insoluble D-glucan that consists of 76 mol% 1,3-alpha-linked glucose and 24 mol% 1,6-alpha-linked glucose
?
sucrose + alpha-D-glucan
alternating-1,6-1,3-alpha-D-glucan
-
Substrates: -
Products: glucan consists of 49.1 mol% 1,6-alpha-linked glucose and 33.9 mol% 1,3-alpha-linked glucose with 13.6 mol% terminal glucose and 3.3 mol% 1,3,6-alpha-branched glucose
Products: glucan consists of 49.1 mol% 1,6-alpha-linked glucose and 33.9 mol% 1,3-alpha-linked glucose with 13.6 mol% terminal glucose and 3.3 mol% 1,3,6-alpha-branched glucose
?
sucrose + alpha-D-glucopyranosyl-(1,4)-L-glucose
?
-
Substrates: -
Products: -
Products: -
?
sucrose + alpha-D-glucopyranosyl-(1,4)-L-glucose
?
-
Substrates: -
Products: -
Products: -
?
sucrose + cellobiose
oligosaccharides
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Substrates: -
Products: alpha-D-glucopyranosyl-(1,2)-(beta-D-glucopyranosyl-(1,4))-D-glucopyranose + alpha-D-glucopyranosyl-(1,6)-beta-D-glucopyranosyl-(1,4)-D-glucopyranose, the last compound in turn can be glycosylated leading to the synthesis of a tetrasaccharide with an additional alpha-(1,6)-linkage at the non-reducing end
Products: alpha-D-glucopyranosyl-(1,2)-(beta-D-glucopyranosyl-(1,4))-D-glucopyranose + alpha-D-glucopyranosyl-(1,6)-beta-D-glucopyranosyl-(1,4)-D-glucopyranose, the last compound in turn can be glycosylated leading to the synthesis of a tetrasaccharide with an additional alpha-(1,6)-linkage at the non-reducing end
?
sucrose + cellobiose
oligosaccharides
-
Substrates: -
Products: alpha-D-glucopyranosyl-(1,2)-(beta-D-glucopyranosyl-(1,4))-D-glucopyranose + alpha-D-glucopyranosyl-(1,6)-beta-D-glucopyranosyl-(1,4)-D-glucopyranose, the last compound in turn can be glycosylated leading to the synthesis of a tetrasaccharide with an additional alpha-(1,6)-linkage at the non-reducing end
Products: alpha-D-glucopyranosyl-(1,2)-(beta-D-glucopyranosyl-(1,4))-D-glucopyranose + alpha-D-glucopyranosyl-(1,6)-beta-D-glucopyranosyl-(1,4)-D-glucopyranose, the last compound in turn can be glycosylated leading to the synthesis of a tetrasaccharide with an additional alpha-(1,6)-linkage at the non-reducing end
?
sucrose + D-tagatose
alpha-D-glucopyranosyl-(1,1)-beta-D-tagatopyranose
-
Substrates: -
Products: -
Products: -
?
sucrose + D-tagatose
alpha-D-glucopyranosyl-(1,1)-beta-D-tagatopyranose
-
Substrates: -
Products: -
Products: -
?
sucrose + gentiobiose
?
-
Substrates: gentiobiose is better as an acceptor than isomaltose, acceptor products from gentiobiose, form in good yields (nearly 90% in unoptimized reactions). The initial product is a single trisaccharide, alpha-D-Glcp-(1-6)-beta-D-Glcp-(1-6)-D-Glc. Two tetrasaccharides are formed in approximately equal quantities: alpha-D-Glcp-(1-3)-alpha-D-Glcp-(1-6)-beta-D-Glcp-(1-6)-D-Glc and alpha-D-Glcp-(1-6)-alpha-D-Glcp-(1-6)-beta-D-Glcp-(1-6)-D-Glc. One pentasaccharide is isolated from the reaction mixture, alpha-D-Glcp-(1-6)-alpha-D-Glcp-(1-3)-alpha-D-Glcp-(1-6)-beta-D-Glcp-(1-6)-D-Glc
Products: -
Products: -
?
sucrose + gentiobiose
?
-
Substrates: gentiobiose is better as an acceptor than isomaltose, acceptor products from gentiobiose, form in good yields (nearly 90% in unoptimized reactions). The initial product is a single trisaccharide, alpha-D-Glcp-(1-6)-beta-D-Glcp-(1-6)-D-Glc. Two tetrasaccharides are formed in approximately equal quantities: alpha-D-Glcp-(1-3)-alpha-D-Glcp-(1-6)-beta-D-Glcp-(1-6)-D-Glc and alpha-D-Glcp-(1-6)-alpha-D-Glcp-(1-6)-beta-D-Glcp-(1-6)-D-Glc. One pentasaccharide is isolated from the reaction mixture, alpha-D-Glcp-(1-6)-alpha-D-Glcp-(1-3)-alpha-D-Glcp-(1-6)-beta-D-Glcp-(1-6)-D-Glc
Products: -
Products: -
?
sucrose + isomaltose
oligoalternan
-
Substrates: -
Products: -
Products: -
?
sucrose + L-glucose
alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,4)-L-glucose
-
Substrates: -
Products: -
Products: -
?
sucrose + L-glucose
alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,4)-L-glucose
-
Substrates: -
Products: -
Products: -
?
sucrose + luteolin
luteolin-3'-O-alpha-D-glucopyranoside + luteolin-4'-O-alpha-D-glucopyranoside
-
Substrates: 8% conversion
Products: -
Products: -
?
sucrose + luteolin
luteolin-3'-O-alpha-D-glucopyranoside + luteolin-4'-O-alpha-D-glucopyranoside
-
Substrates: 8% conversion
Products: -
Products: -
?
sucrose + luteolin
luteolin-3'-O-alpha-D-glucopyranoside + luteolin-4'-O-alpha-D-glucopyranoside
-
Substrates: 8% conversion
Products: -
Products: -
?
sucrose + maltose
?
Substrates: maltose undergoes alpha-1,6 glucosylation alone to give the oligodextran of DP3 (OD3 panose, alpha-D-Glcp-(1->6)-alpha-D-Glcp-(1->4)-D-Glc), which can be further elongated at either the O6 or the O3 position of the nonreducing unit to give the structures OD4 (alpha-D-Glcp-(1->6)-alpha-D-Glcp-(1->6)-alpha-D-Glcp-(1->4)-D-Glc) and OA4 (alpha-D-Glcp-(1->3)-alpha-D-Glcp-(1->6)-alpha-D-Glcp-(1->4)-D-Glc), respectively. The oligosaccharide OA4 is quick to appear at the beginning of the reaction (1 min) and accumulates at a much higher level than OD4, indicating that panose is preferentially elongated with an alpha-1,3 linkage. A very small peak of OD5 originating from OD4 only appears toward the end of the reaction (after about 30 min) and is not elongated further (no OD6 is found). As soon as the OA4 starts to accumulate, it is efficiently converts to OA5 (alpha-D-Glcp-(1->6)-alpha-D-Glcp-(1->3)-alpha-D-Glcp-(1->6)-alpha-D-Glcp-(1->4)-D-Glc). The OA5 itself can act as an acceptor for the formation of two OA6s (alpha-D-Glcp-(1->6)-alpha-D-Glcp-(1->6)-alpha-D-Glcp-(1->3)-alpha-D-Glcp-(1->6)-alpha-D-Glcp-(1->4)-DGlc and alpha-D-Glcp-(1->3)-alpha-D-Glcp-(1->6)-alpha-D-Glcp-(1->3)-alpha-D-Glcp-(1->6)-alpha-D-Glcp-(1->4)-D-Glc)
Products: -
Products: -
?
sucrose + maltose
?
Substrates: the wild-type enzyme strictly synthesized alpha-(1,6) linkage on the maltose acceptor. Formation of alpha-(1,2), alpha-(1,3), alpha-(1,4), and alpha-(1,6) linkages are detected from products of the W675A mutant
Products: -
Products: -
?
sucrose + maltose
?
Leuconostoc citreum ABK-1
Substrates: the wild-type enzyme strictly synthesized alpha-(1,6) linkage on the maltose acceptor. Formation of alpha-(1,2), alpha-(1,3), alpha-(1,4), and alpha-(1,6) linkages are detected from products of the W675A mutant
Products: -
Products: -
?
sucrose + maltose
?
Leuconostoc citreum NRRL B-1355
Substrates: maltose undergoes alpha-1,6 glucosylation alone to give the oligodextran of DP3 (OD3 panose, alpha-D-Glcp-(1->6)-alpha-D-Glcp-(1->4)-D-Glc), which can be further elongated at either the O6 or the O3 position of the nonreducing unit to give the structures OD4 (alpha-D-Glcp-(1->6)-alpha-D-Glcp-(1->6)-alpha-D-Glcp-(1->4)-D-Glc) and OA4 (alpha-D-Glcp-(1->3)-alpha-D-Glcp-(1->6)-alpha-D-Glcp-(1->4)-D-Glc), respectively. The oligosaccharide OA4 is quick to appear at the beginning of the reaction (1 min) and accumulates at a much higher level than OD4, indicating that panose is preferentially elongated with an alpha-1,3 linkage. A very small peak of OD5 originating from OD4 only appears toward the end of the reaction (after about 30 min) and is not elongated further (no OD6 is found). As soon as the OA4 starts to accumulate, it is efficiently converts to OA5 (alpha-D-Glcp-(1->6)-alpha-D-Glcp-(1->3)-alpha-D-Glcp-(1->6)-alpha-D-Glcp-(1->4)-D-Glc). The OA5 itself can act as an acceptor for the formation of two OA6s (alpha-D-Glcp-(1->6)-alpha-D-Glcp-(1->6)-alpha-D-Glcp-(1->3)-alpha-D-Glcp-(1->6)-alpha-D-Glcp-(1->4)-DGlc and alpha-D-Glcp-(1->3)-alpha-D-Glcp-(1->6)-alpha-D-Glcp-(1->3)-alpha-D-Glcp-(1->6)-alpha-D-Glcp-(1->4)-D-Glc)
Products: -
Products: -
?
sucrose + maltose
?
-
Substrates: alternansucrase acceptor products from maltose do not contain dextran-type linkage sequences. Instead, the product series is comprised of an alternan-type linkage sequence, with some pairs of consecutive alpha-(1,6) linkages in the evennumbered members of the series. The distribution and sequence of linkages is apparently kinetically controlled. Branch formation is not detected below DP 8. Alternansucrase forms alpha-(1,3) linkages only when the acceptor is a-(1,6)-linked, thereby prohibiting the formation of sequences of alpha-(1,3) linkages. Furthermore, the enzyme appears not to make products containing more than two sequential alpha-(1,6) linkages, thereby prohibiting the formation of dextran-like linkage sequences
Products: -
Products: -
?
sucrose + maltose
?
-
Substrates: alternansucrase acceptor products from maltose do not contain dextran-type linkage sequences. Instead, the product series is comprised of an alternan-type linkage sequence, with some pairs of consecutive alpha-(1,6) linkages in the evennumbered members of the series. The distribution and sequence of linkages is apparently kinetically controlled. Branch formation is not detected below DP 8. Alternansucrase forms alpha-(1,3) linkages only when the acceptor is a-(1,6)-linked, thereby prohibiting the formation of sequences of alpha-(1,3) linkages. Furthermore, the enzyme appears not to make products containing more than two sequential alpha-(1,6) linkages, thereby prohibiting the formation of dextran-like linkage sequences
Products: -
Products: -
?
sucrose + maltose
oligoalternan
-
Substrates: -
Products: panose is the first acceptor product
Products: panose is the first acceptor product
?
sucrose + maltose
oligoalternan
-
Substrates: -
Products: panose is the first acceptor product
Products: panose is the first acceptor product
?
sucrose + maltose
oligoalternan
-
Substrates: -
Products: -
Products: -
?
sucrose + methyl-alpha-D-glucoside
oligoalternan
-
Substrates: -
Products: -
Products: -
?
sucrose + methyl-alpha-D-glucoside
oligoalternan
-
Substrates: -
Products: -
Products: -
?
sucrose + myricetin
?
-
Substrates: 49% conversion
Products: -
Products: -
?
sucrose + myricetin
?
-
Substrates: 49% conversion
Products: -
Products: -
?
sucrose + n sucrose
alpha-(1,3/1,6)-linked glucan
Substrates: -
Products: -
Products: -
?
sucrose + n sucrose
alpha-(1,3/1,6)-linked glucan
Leuconostoc citreum ABK-1
Substrates: -
Products: -
Products: -
?
sucrose + quercetin
?
-
Substrates: 4% conversion
Products: -
Products: -
?
sucrose + quercetin
?
-
Substrates: 4% conversion
Products: -
Products: -
?
sucrose + raffinose
?
-
Substrates: the alternansucrase-catalyzed acceptor reaction with raffinose gives a gravimetric yield of alternan of 9.5% relative to the weight of sucrose, indicating that 20% of the glucosyl units are incorporated into alternan, and 80% into oligosaccharide acceptor products. The main products are the tetrasaccharides alpha-D-Glcp-(1-3)-alpha-D-Galp-(1-6)-alpha-D-Glcp-(1-2)-beta-D-Fruf and alpha-D-Glcp-(1-4)-alpha-D-Galp-(1-6)-alpha-D-Glcp-(1-2)-beta-D-Fruf in ratios ranging from 4:1 to 9:1, along with lesser amounts of alpha-D-Glcp-(1-6)-alpha-D-Galp-(1-6)-alpha-D-Glcp-(1-2)-beta-D-Fruf. Pentasaccharides, hexasaccharides and higher oligosaccharides are also produced
Products: -
Products: -
?
sucrose + raffinose
?
-
Substrates: the alternansucrase-catalyzed acceptor reaction with raffinose gives a gravimetric yield of alternan of 9.5% relative to the weight of sucrose, indicating that 20% of the glucosyl units are incorporated into alternan, and 80% into oligosaccharide acceptor products. The main products are the tetrasaccharides alpha-D-Glcp-(1-3)-alpha-D-Galp-(1-6)-alpha-D-Glcp-(1-2)-beta-D-Fruf and alpha-D-Glcp-(1-4)-alpha-D-Galp-(1-6)-alpha-D-Glcp-(1-2)-beta-D-Fruf in ratios ranging from 4:1 to 9:1, along with lesser amounts of alpha-D-Glcp-(1-6)-alpha-D-Galp-(1-6)-alpha-D-Glcp-(1-2)-beta-D-Fruf. Pentasaccharides, hexasaccharides and higher oligosaccharides are also produced
Products: -
Products: -
?
additional information
?
-
-
Substrates: LC/MS product analysis
Products: -
Products: -
?
additional information
?
-
Substrates: product analysis, determination of alternan nanoparticle size distribution by dynamic light scattering
Products: -
Products: -
?
additional information
?
-
-
Substrates: product analysis, determination of alternan nanoparticle size distribution by dynamic light scattering
Products: -
Products: -
?
additional information
?
-
Substrates: for the docking calculations, a model of the ASRDELTA2 glucosyl-enzyme intermediate is constructed based on the high resolution structure of the GH13 covalent intermediate (PDB ID 1S46). Maltose is the best known acceptor for ASR
Products: -
Products: -
?
additional information
?
-
Substrates: alternansucrase enzyme from Leuconostoc citreum SK24.002 is used to produce di-glycosyl-stevioside through acceptor reaction. Identification of the di-glycosyl-stevioside structure as 13-([alpha-D-glucopyranosyl-(1->3)-alpha-D-glucopyranosyl-(1->6)-beta-D glucopyranosyl-(1->2)-beta-D-glucopyranosyl]oxy)kaur-16-en-19-oic acid beta-D glucopyranosyl ester, method optimization and evaluation, overview
Products: -
Products: -
?
additional information
?
-
Leuconostoc citreum ABK-1
Substrates: product analysis, determination of alternan nanoparticle size distribution by dynamic light scattering
Products: -
Products: -
?
additional information
?
-
Leuconostoc citreum NRRL B-1355
Substrates: for the docking calculations, a model of the ASRDELTA2 glucosyl-enzyme intermediate is constructed based on the high resolution structure of the GH13 covalent intermediate (PDB ID 1S46). Maltose is the best known acceptor for ASR
Products: -
Products: -
?
additional information
?
-
-
Substrates: LC/MS product analysis
Products: -
Products: -
?
additional information
?
-
Substrates: alternansucrase enzyme from Leuconostoc citreum SK24.002 is used to produce di-glycosyl-stevioside through acceptor reaction. Identification of the di-glycosyl-stevioside structure as 13-([alpha-D-glucopyranosyl-(1->3)-alpha-D-glucopyranosyl-(1->6)-beta-D glucopyranosyl-(1->2)-beta-D-glucopyranosyl]oxy)kaur-16-en-19-oic acid beta-D glucopyranosyl ester, method optimization and evaluation, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: methyl D-allopyrano-sides are glucosylated primarily at position 6, yielding methyl alpha-D-glucopyranosyl-(1,6)-D-allopyranosides. The latter subsequently gave rise to methyl alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-D-allopyranosides. The methyl alpha-D-hexopyranosides are better acceptors than the corresponding beta-glycosides
Products: -
Products: -
?
additional information
?
-
-
Substrates: non-digestible isomaltooligosaccharides are synthesized by combining dextransucrase from Leuconostoc mesenteroides B512F/KM and alternansucrase from Leuconostoc mesenteroides NRRL 1355CF10/KM using sucrose as substrate and maltose as acceptor
Products: -
Products: -
-
additional information
?
-
Leuconostoc mesenteroides B512F/KM
-
Substrates: non-digestible isomaltooligosaccharides are synthesized by combining dextransucrase from Leuconostoc mesenteroides B512F/KM and alternansucrase from Leuconostoc mesenteroides NRRL 1355CF10/KM using sucrose as substrate and maltose as acceptor
Products: -
Products: -
-
additional information
?
-
Leuconostoc mesenteroides NRRL 1355CF10/KM
-
Substrates: non-digestible isomaltooligosaccharides are synthesized by combining dextransucrase from Leuconostoc mesenteroides B512F/KM and alternansucrase from Leuconostoc mesenteroides NRRL 1355CF10/KM using sucrose as substrate and maltose as acceptor
Products: -
Products: -
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
additional information
Ca2+
a calcium ion is present at the interface between domain A and B in interaction with Glu589, Asp595 (motif V), Asp1173 (motif I), and Asn639 (motif II) forming the binding site
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
below a sodium phosphate buffer concentration of 50 mM the activity is reduced by 75%
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Dental Caries
Crystal Structure of Glucansucrase from the Dental Caries Pathogen Streptococcus mutans.
Dental Caries
Crystallization and preliminary X-ray analysis of a glucansucrase from the dental caries pathogen Streptococcus mutans.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kinetic study conducted with ASR C-APY-del shows that both high molar mass and low molar mass alternan populations are formed in the early stage of the reaction, suggesting that ASR follows a semiprocessive mechanism of polymerization
-
14.7
sucrose
pH 4.0, 40°C, transglycosylation, mutant enzyme W675Y
18
sucrose
pH 4.0, 40°C, transglycosylation, mutant enzyme W675F
33.4
sucrose
pH 4.0, 40°C, transglycosylation, wild-type enzyme
79
sucrose
pH 4.0, 40°C, transglycosylation, mutant enzyme W675I
90.9
sucrose
pH 4.0, 40°C, transglycosylation, mutant enzyme W675N
92.7
sucrose
pH 4.0, 40°C, transglycosylation, mutant enzyme W675L
106
sucrose
pH 4.0, 40°C, transglycosylation, mutant enzyme W675A
160.6
sucrose
pH 4.0, 40°C, transglycosylation, mutant enzyme W675S
185.1
sucrose
pH 4.0, 40°C, transglycosylation, mutant enzyme W675H
226.9
sucrose
pH 4.0, 40°C, transglycosylation, mutant enzyme W675D
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.6
sucrose
pH 4.0, 40°C, transglycosylation, mutant enzyme W675H
1.7
sucrose
pH 4.0, 40°C, transglycosylation, mutant enzyme W675D
4.1
sucrose
pH 4.0, 40°C, transglycosylation, mutant enzyme W675N
5
sucrose
pH 4.0, 40°C, transglycosylation, mutant enzyme W675I
9
sucrose
pH 4.0, 40°C, transglycosylation, mutant enzyme W675S
9.2
sucrose
pH 4.0, 40°C, transglycosylation, mutant enzyme W675L
9.9
sucrose
pH 4.0, 40°C, transglycosylation, mutant enzyme W675A
47.1
sucrose
pH 4.0, 40°C, transglycosylation, mutant enzyme W675F
91.1
sucrose
pH 4.0, 40°C, transglycosylation, mutant enzyme W675Y
815.6
sucrose
pH 4.0, 40°C, transglycosylation, wild-type enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
sucrose
pH 4.0, 40°C, transglycosylation, mutant enzyme W675H
0.01
sucrose
pH 4.0, 40°C, transglycosylation, mutant enzyme W675D
0.05
sucrose
pH 4.0, 40°C, transglycosylation, mutant enzyme W675N
0.09
sucrose
pH 4.0, 40°C, transglycosylation, mutant enzyme W675A
0.1
sucrose
pH 4.0, 40°C, transglycosylation, mutant enzyme W675L
0.1
sucrose
pH 4.0, 40°C, transglycosylation, mutant enzyme W675I
0.1
sucrose
pH 4.0, 40°C, transglycosylation, mutant enzyme W675S
2.6
sucrose
pH 4.0, 40°C, transglycosylation, mutant enzyme W675F
6.2
sucrose
pH 4.0, 40°C, transglycosylation, mutant enzyme W675Y
24.4
sucrose
pH 4.0, 40°C, transglycosylation, wild-type enzyme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 7.2
-
pH 4.0: about 75% of maximal activity, pH 7.2: about 60% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 50
-
30°C: about 65% of maximal activity, 50°C: about 55% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Leuconostoc citreum ABK-1
constitutive mutants are obtained after chemical mutagenesis by ethyl methane sulfonate
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the concentration of the enzyme in the particulate fraction suggests that it is associated primarily with the cell wall or membrane
-
brenda
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
physiological function
additional information
evolution
the enzyme belongs to the CAZy glycoside hydrolase family 70 (GH70)
evolution
the enzyme belongs to the glycoside hydrolase family 70 (GH70)
evolution
Leuconostoc citreum ABK-1
-
the enzyme belongs to the CAZy glycoside hydrolase family 70 (GH70)
-
evolution
Leuconostoc citreum NRRL B-1355
-
the enzyme belongs to the glycoside hydrolase family 70 (GH70)
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physiological function
alternansucrase catalyses the sequential transfer of glucose residues from sucrose onto another sucrose molecule to form a long chain polymer, known as alternan. The insoluble polymer alternan has alternating alpha-1,6 and alpha-1,3 glycosidic linkages as has been judged by using 13C NMR spectroscopy and methylation analysis, partially hydrolysed product analysis, and enzymatic analysis
physiological function
alternansucrase (ASR) is an alpha-transglucosylase capable of catalyzing high and low molar mass alternan, an alpha-glucan comprising alternating alpha-1,3 and alpha-1,6 linkages in its linear chain. ASR also catalyzes transglucosylation from sucrose to many different types of sugar acceptors: methyl-alpha-D-glucoside, maltose, maltodextrin, maltitol, isomaltooligosaccharides, cellobiose, melibiose, raffinose, gentiobiose, and lactose, and produces glucosylated products showing interesting prebiotic properties
physiological function
Leuconostoc citreum ABK-1
-
alternansucrase catalyses the sequential transfer of glucose residues from sucrose onto another sucrose molecule to form a long chain polymer, known as alternan. The insoluble polymer alternan has alternating alpha-1,6 and alpha-1,3 glycosidic linkages as has been judged by using 13C NMR spectroscopy and methylation analysis, partially hydrolysed product analysis, and enzymatic analysis
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physiological function
Leuconostoc citreum NRRL B-1355
-
alternansucrase (ASR) is an alpha-transglucosylase capable of catalyzing high and low molar mass alternan, an alpha-glucan comprising alternating alpha-1,3 and alpha-1,6 linkages in its linear chain. ASR also catalyzes transglucosylation from sucrose to many different types of sugar acceptors: methyl-alpha-D-glucoside, maltose, maltodextrin, maltitol, isomaltooligosaccharides, cellobiose, melibiose, raffinose, gentiobiose, and lactose, and produces glucosylated products showing interesting prebiotic properties
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additional information
analysis of structural determinants involved in the linkage specificity of alternansucrase (ASR), overview. ASR displays two different acceptor subsites in the prolongation of its subsites -1 and +1. The first one is defined by Trp675, a residue of subsite +2, and orients acceptor binding exclusively toward alpha-1,6 linkage synthesis. The second binding site comprises Asp772 and Trp543, two residues defining the +2' and +3' subsites, respectively, which are critical for alpha-1,3 linkage formation. It is proposed that the interplay between these two acceptor sites controls alternance. The enzyme is predicted to adopt the same fold as the other glucansucrases and the same alpha-retaining mechanism involving the contribution of Asp635, Glu673, and Asp767. These amino acids play the role of, respectively, the nucleophile, acid/base catalyst, and transition state stabilizer (TSS) implicated in the formation of the beta-D-glucosyl-enzyme intermediate. Kinetic study conducted with ASR C-APY-del shows that both high molar mass and low molar mass alternan populations are formed in the early stage of the reaction, suggesting that ASR follows a semiprocessive mechanism of polymerization. Three-dimensional structure analysis, overview
additional information
catalytic mechanism of di-glycosyl-stevioside synthesis, overview
additional information
-
catalytic mechanism of di-glycosyl-stevioside synthesis, overview
-
additional information
Leuconostoc citreum NRRL B-1355
-
analysis of structural determinants involved in the linkage specificity of alternansucrase (ASR), overview. ASR displays two different acceptor subsites in the prolongation of its subsites -1 and +1. The first one is defined by Trp675, a residue of subsite +2, and orients acceptor binding exclusively toward alpha-1,6 linkage synthesis. The second binding site comprises Asp772 and Trp543, two residues defining the +2' and +3' subsites, respectively, which are critical for alpha-1,3 linkage formation. It is proposed that the interplay between these two acceptor sites controls alternance. The enzyme is predicted to adopt the same fold as the other glucansucrases and the same alpha-retaining mechanism involving the contribution of Asp635, Glu673, and Asp767. These amino acids play the role of, respectively, the nucleophile, acid/base catalyst, and transition state stabilizer (TSS) implicated in the formation of the beta-D-glucosyl-enzyme intermediate. Kinetic study conducted with ASR C-APY-del shows that both high molar mass and low molar mass alternan populations are formed in the early stage of the reaction, suggesting that ASR follows a semiprocessive mechanism of polymerization. Three-dimensional structure analysis, 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). D3JC18_LEUCI
176
0
20211
TrEMBL
Secretory Pathway (Reliability: 4)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the catalytic domain A of ASRDELTA2 is formed by a (beta/alpha)8 barrel
additional information
Leuconostoc citreum NRRL B-1355
-
the catalytic domain A of ASRDELTA2 is formed by a (beta/alpha)8 barrel
-
additional information
-
cultures of strains B-1355 and R15 have a principal alternansucrase band of 204000 Da. These strains also produce minor alternansucrase bands. Cultures of strains R1579, R1622 and R1535 produce principal alternansucrase activity bands of 191000 Da, 161000 Da and 150000 Da, respectively and numerous minor bands
additional information
-
cultures of strains B-1355 and R15 have a principal alternansucrase band of 204000 Da. These strains also produce minor alternansucrase bands. Cultures of strains R1579, R1622 and R1535 produce principal alternansucrase activity bands of 191000 Da, 161000 Da and 150000 Da, respectively and numerous minor bands
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant truncated mutant ASRDELTA2 (ASR (Met1-Ala2057)), sitting drop vapour diffusion method, mixing of 200 nl of 8 mg/ml protein in 30 mM MES buffer, pH 6.5, 100 mM NaCl, 0.05 g/l CaCl2, and 10 mM isomaltohexaose, with 200 nl of reservoir solution containing 17% w/v PEG 3350, and NaNO3 0.5 M, 3 months, at 12°C, X-ray diffraction structure determination and analysis at 2.8 A resolution
3D structures of the enzyme in complex with different sugars (isomaltose, isomaltotriose, isomaltononaose, panose, and oligoalternan) bound either in domain A (SBS-A1) or in domain V (sugar-binding pocket V-B)
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
W675A
formation of alpha-(1,2), alpha-(1,3), alpha-(1,4), and alpha-(1,6) linkages are detected from products of the W675A mutant in the reaction with sucrose and maltose. Kojibiose, nigerose, maltose, and isomaltose are formed. kcat/Km for sucrose is 0.36% as compared to wild-type enzyme
W675D
kcat/Km for sucrose is 0.04% as compared to wild-type enzyme
W675F
in the maltose-acceptor reaction the oligosaccharide pattern of the mutant enzyme corresponds with that of the wild-type enzyme. Specific activity is reduced by 80%. kcat/Km for sucrose is 10.6% as compared to wild-type enzyme
W675H
kcat/Km for sucrose is 0.04% as compared to wild-type enzyme
W675I
kcat/Km for sucrose is 0.4% as compared to wild-type enzyme
W675L
kcat/Km for sucrose is 0.4% as compared to wild-type enzyme
W675N
kcat/Km for sucrose is 0.2% as compared to wild-type enzyme
W675S
kcat/Km for sucrose is 0.4% as compared to wild-type enzyme
W675Y
in the maltose-acceptor reaction the oligosaccharide pattern of the mutant enzyme corresponds with that of the wild-type enzyme. Specific activity is reduced by 60%. kcat/Km for sucrose is 25% as compared to wild-type enzyme
W675A
Leuconostoc citreum ABK-1
-
formation of alpha-(1,2), alpha-(1,3), alpha-(1,4), and alpha-(1,6) linkages are detected from products of the W675A mutant in the reaction with sucrose and maltose. Kojibiose, nigerose, maltose, and isomaltose are formed. kcat/Km for sucrose is 0.36% as compared to wild-type enzyme
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W675F
Leuconostoc citreum ABK-1
-
in the maltose-acceptor reaction the oligosaccharide pattern of the mutant enzyme corresponds with that of the wild-type enzyme. Specific activity is reduced by 80%. kcat/Km for sucrose is 10.6% as compared to wild-type enzyme
-
W675Y
Leuconostoc citreum ABK-1
-
in the maltose-acceptor reaction the oligosaccharide pattern of the mutant enzyme corresponds with that of the wild-type enzyme. Specific activity is reduced by 60%. kcat/Km for sucrose is 25% as compared to wild-type enzyme
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Q700A
the amount of high-molar-mass polymer decreases from 31.5% for the wild-type enzyme to 20.4% for the Q700A mutant
Q700A/Y717A
the amount of high-molar-mass polymer decreases from 31.5% for the wild-type enzyme to 18.3% for the Q700A mutant
Y717A
additional information
Y717A
the amount of high-molar-mass polymer decreases from 31.5% for the wild-type enzyme to 18.8% for the Q700A mutant
Y717A
the mutant produces less than 3% of high-molar-mass alternan
additional information
generation of a truncated version of alternansucrase, mutant ASRDELTA2 (ASR (Met1-Ala2057)), three-dimensional structure determination and analysis. Unusual repeated sequences named APY repeats are identified at the C-terminal end of the protein. Their deletion in the mutant ASR C-APY-del (Met1-Gly1425) does not impact the product profile but significantly increases the enzyme half-life time at 50°C by 5fold compared to the full-length ASR. Generation of several truncated forms: ASRDELTA2, ASRDELTA3, ASRDELTA4, and ASRDELTA5, which are deleted, respectively, of the signal peptide (Met1-His38), one predicted disordered region (Met1-Asp78), two predicted disordered regions (Met1-Pro152), and the entire domain V (Met1-Ser398 and Gln1305-Gly1425). Domain organization of ASR truncated mutants, catalytic sites and domain properties of wild-type and mutant enzymes, detailed overview
additional information
Leuconostoc citreum NRRL B-1355
-
generation of a truncated version of alternansucrase, mutant ASRDELTA2 (ASR (Met1-Ala2057)), three-dimensional structure determination and analysis. Unusual repeated sequences named APY repeats are identified at the C-terminal end of the protein. Their deletion in the mutant ASR C-APY-del (Met1-Gly1425) does not impact the product profile but significantly increases the enzyme half-life time at 50°C by 5fold compared to the full-length ASR. Generation of several truncated forms: ASRDELTA2, ASRDELTA3, ASRDELTA4, and ASRDELTA5, which are deleted, respectively, of the signal peptide (Met1-His38), one predicted disordered region (Met1-Asp78), two predicted disordered regions (Met1-Pro152), and the entire domain V (Met1-Ser398 and Gln1305-Gly1425). Domain organization of ASR truncated mutants, catalytic sites and domain properties of wild-type and mutant enzymes, detailed overview
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
rcombinant enzyme from Escherichia coli strain BL21(DE3) by anion exchange chromatography, hydrophobic interaction chromatography, and dialysis
recombinant wild-type enzyme and truncated mutants from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration, followed by ultrafiltration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Solanum tuberosum. The Asr transcript levels correlated well with alternan accumulation in tuber juices
-
gene asr, recombinant expression of wild-type enzyme and truncated mutants in Escherichia coli strain BL21(DE3)
gene Lcalt, rcombinant expression in Escherichia coli strain BL21(DE3)
recombinant expression of the large alternansucrase (2057 amino acids) is hindered in Escherichia coli due to poor enzyme solubility and protein degradation. A truncated variant deleted of the APY repeats but harboring four C-terminal CW-like repeats display a high specific activity and the same specificity of product synthesis as the native enzyme. It is more soluble and suffers less degradation than full length alternansucrase
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
food industry
pharmacology
synthesis
additional information
drug development
-
formation of oligosaccharides by alternansucrase may serve as prebiotics
drug development
-
formation of oligosaccharides by alternansucrase may serve as prebiotics
-
food industry
-
non-digestible isomaltooligosaccharides (NDIMOS) are synthesized by combining dextransucrase from Leuconostoc mesenteroides B512F/KM and alternansucrase from Leuconostoc mesenteroides NRRL 1355CF10/KM using sucrose as substrate and maltose as acceptor. The optimal conditions for NDIMOS synthesis are 1 U/ml dextransucrase, 1 U/ml alternansucrase, and 400 mM maltose in 2 M sucrose at 45°C. NDIMOS show prebiotic effects by proliferating Bifidobacteria in the pure culture as well as in the mixed culture with Salmonella typhimurium. Thus, NDIMOS have several potential applications in the food and pharmaceutical industries
food industry
Leuconostoc mesenteroides NRRL 1355CF10/KM
-
non-digestible isomaltooligosaccharides (NDIMOS) are synthesized by combining dextransucrase from Leuconostoc mesenteroides B512F/KM and alternansucrase from Leuconostoc mesenteroides NRRL 1355CF10/KM using sucrose as substrate and maltose as acceptor. The optimal conditions for NDIMOS synthesis are 1 U/ml dextransucrase, 1 U/ml alternansucrase, and 400 mM maltose in 2 M sucrose at 45°C. NDIMOS show prebiotic effects by proliferating Bifidobacteria in the pure culture as well as in the mixed culture with Salmonella typhimurium. Thus, NDIMOS have several potential applications in the food and pharmaceutical industries
-
food industry
Leuconostoc mesenteroides B512F/KM
-
non-digestible isomaltooligosaccharides (NDIMOS) are synthesized by combining dextransucrase from Leuconostoc mesenteroides B512F/KM and alternansucrase from Leuconostoc mesenteroides NRRL 1355CF10/KM using sucrose as substrate and maltose as acceptor. The optimal conditions for NDIMOS synthesis are 1 U/ml dextransucrase, 1 U/ml alternansucrase, and 400 mM maltose in 2 M sucrose at 45°C. NDIMOS show prebiotic effects by proliferating Bifidobacteria in the pure culture as well as in the mixed culture with Salmonella typhimurium. Thus, NDIMOS have several potential applications in the food and pharmaceutical industries
-
pharmacology
-
non-digestible isomaltooligosaccharides (NDIMOS) are synthesized by combining dextransucrase from Leuconostoc mesenteroides B512F/KM and alternansucrase from Leuconostoc mesenteroides NRRL 1355CF10/KM using sucrose as substrate and maltose as acceptor. The optimal conditions for NDIMOS synthesis are 1 U/ml dextransucrase, 1 U/ml alternansucrase, and 400 mM maltose in 2 M sucrose at 45°C. NDIMOS show prebiotic effects by proliferating Bifidobacteria in the pure culture as well as in the mixed culture with Salmonella typhimurium. Thus, NDIMOS have several potential applications in the food and pharmaceutical industries
pharmacology
Leuconostoc mesenteroides NRRL 1355CF10/KM
-
non-digestible isomaltooligosaccharides (NDIMOS) are synthesized by combining dextransucrase from Leuconostoc mesenteroides B512F/KM and alternansucrase from Leuconostoc mesenteroides NRRL 1355CF10/KM using sucrose as substrate and maltose as acceptor. The optimal conditions for NDIMOS synthesis are 1 U/ml dextransucrase, 1 U/ml alternansucrase, and 400 mM maltose in 2 M sucrose at 45°C. NDIMOS show prebiotic effects by proliferating Bifidobacteria in the pure culture as well as in the mixed culture with Salmonella typhimurium. Thus, NDIMOS have several potential applications in the food and pharmaceutical industries
-
pharmacology
Leuconostoc mesenteroides B512F/KM
-
non-digestible isomaltooligosaccharides (NDIMOS) are synthesized by combining dextransucrase from Leuconostoc mesenteroides B512F/KM and alternansucrase from Leuconostoc mesenteroides NRRL 1355CF10/KM using sucrose as substrate and maltose as acceptor. The optimal conditions for NDIMOS synthesis are 1 U/ml dextransucrase, 1 U/ml alternansucrase, and 400 mM maltose in 2 M sucrose at 45°C. NDIMOS show prebiotic effects by proliferating Bifidobacteria in the pure culture as well as in the mixed culture with Salmonella typhimurium. Thus, NDIMOS have several potential applications in the food and pharmaceutical industries
-
synthesis
-
modification of bacterial cellulose using sucrose, dextransucrase from Leuconostoc mesenteroides B-742CMB and alternansucrase from Leuconostoc B-1355C. This modification method produces a new bacterial cellulose that has a unique structure and probably new property
synthesis
alternan polymer is more water soluble and less viscous than dextrans, making it a good substitute for Arabic gum. Nanoparticles and films have been obtained with alternan produced by Leuconostoc citreum ABK-1 alternansucrase, thereby opening up other potential applications in nanotechnology
synthesis
alternansucrase enzyme from Leuconostoc citreum SK24.002 is used to produce di-glycosyl-stevioside through acceptor reaction, optimized method, overview
synthesis
-
alternansucrase enzyme from Leuconostoc citreum SK24.002 is used to produce di-glycosyl-stevioside through acceptor reaction, optimized method, overview
-
synthesis
Leuconostoc citreum NRRL B-1355
-
alternan polymer is more water soluble and less viscous than dextrans, making it a good substitute for Arabic gum. Nanoparticles and films have been obtained with alternan produced by Leuconostoc citreum ABK-1 alternansucrase, thereby opening up other potential applications in nanotechnology
-
additional information
-
the enzyme is utilised in the biotransformation of stevioside to fully or partially remove the bitter taste of the stevioside, 13-O-beta-sophorosyl-19-O-beta-D-glucosyl-steviol, a non-cariogenic and low-calorigenic diterpenoid glycoside with a bitter taste and a bad aftertaste, from the leaves of Stevia rebaudiana, commercially used as a low calorie and a non-cariogenic sweetener. Effects of reaction condition and enzyme concentration on biotransformation, overview
additional information
-
the enzyme is utilised in the biotransformation of stevioside to fully or partially remove the bitter taste of the stevioside, 13-O-beta-sophorosyl-19-O-beta-D-glucosyl-steviol, a non-cariogenic and low-calorigenic diterpenoid glycoside with a bitter taste and a bad aftertaste, from the leaves of Stevia rebaudiana, commercially used as a low calorie and a non-cariogenic sweetener. Effects of reaction condition and enzyme concentration on biotransformation, overview
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cote, G.L.; Robyt, J.F.
Isolation and partial characterization of an extracellular glucansucrase from Leuconostoc mesenteroides NRRL B-1355 that synthesizes an alternating (1-6),(1-3)-alpha-D-glucan
Carbohydr. Res.
101
57-74
1982
Leuconostoc mesenteroides, Leuconostoc mesenteroides NRRL B-1355
brenda
Lopez-Munguia, A.; Pelenc, V.; Remaud, M.; Biton, J.; Michel, J.M.; Lang, C.; Paul, F.; Monsan, P.
Production and purification of alternansucrase, a glucosyltransferase from Leuconostoc mesenteroides NRRL B-1355, for the synthesis of oligoalternan
Enzyme Microb. Technol.
15
77-85
1993
Leuconostoc mesenteroides, Leuconostoc mesenteroides NRRL B-1355
-
brenda
Mukasa, H.; Shimamura, A.; Tsumori, H.
Purification and characterization of cell-associated glucosyltransferase synthesizing insoluble glucan from Streptococcus mutans serotype c
J. Gen. Microbiol.
135
2055-2063
1989
Streptococcus mutans
brenda
Tsumori, H.; Shimamura, A.; Mukasa, H.
Purification and properties of extracellular glucosyltransferase synthesizing 1,6-, 1,3-alpha-D-glucan from Streptococcus mutans serotype a
J. Gen. Microbiol.
131
3347-3353
1985
Streptococcus mutans
brenda
Arguello-Morales, M.A.; Remaud-Simeon, M.; Pizzut, S.; Sarcabal, P.; Willemot, R.M.; Monsan, P.
Sequence analysis of the gene encoding alternansucrase, a sucrose glucosyltransferase from Leuconostoc mesenteroides NRRL B-1355
FEMS Microbiol. Lett.
182
81-85
2000
Leuconostoc mesenteroides, Leuconostoc mesenteroides NRRL B-1355
brenda
Zahnley, J.C.; Smith, M.R.
Cellular association of glucosyltransferases in Leuconostoc mesenteroides and effects of detergent on cell association
Appl. Biochem. Biotechnol.
87
57-70
2000
Leuconostoc mesenteroides
brenda
Smith, M.R.; Zahnley, J.C.
Leuconostoc mesenteroides B-1355 mutants producing alternansucrases exhibiting decreases in apparent molecular mass
Appl. Environ. Microbiol.
63
581-586
1997
Leuconostoc mesenteroides, Leuconostoc mesenteroides NRRL B-1355
brenda
Kim, D.; Kim, Y.M.; Park, M.R.; Park, D.H.
Modification of Acetobacter xylinum bacterial cellulose using dextransucrase and alternansucrase
J. Microbiol. Biotechnol.
9
704-708
1999
Leuconostoc mesenteroides
-
brenda
Richard, G.; Morel, S.; Willemot, R.M.; Monsan, P.; Remaud-Simeon, M.
Glucosylation of alpha-butyl- and alpha-octyl-D-glucopyranosides by dextransucrase and alternansucrase from Leuconostoc mesenteroides
Carbohydr. Res.
338
855-864
2003
Leuconostoc mesenteroides
brenda
Arguello Morales, M.A.; Remaud-Simeon, M.; Willemot, R.M.; Vignon, M.R.; Monsan, P.
Novel oligosaccharides synthesized from sucrose donor and cellobiose acceptor by alternansucrase
Carbohydr. Res.
331
403-411
2001
Leuconostoc mesenteroides, Leuconostoc mesenteroides NRRL B-23192
brenda
Cote, G.L.; Dunlap, C.A.
Alternansucrase acceptor reactions with methyl hexopyranosides
Carbohydr. Res.
338
1961-1967
2003
Leuconostoc mesenteroides
brenda
Cote, G.L.; Dunlap, C.A.; Appell, M.; Momany, F.A.
Alternansucrase acceptor reactions with D-tagatose and L-glucose
Carbohydr. Res.
340
257-262
2005
Leuconostoc mesenteroides, Leuconostoc mesenteroides NRRL B-21297
brenda
Kok-Jacon, G.A.; Vincken, J.P.; Suurs, L.C.; Wang, D.; Liu, S.; Visser, R.G.
Expression of alternansucrase in potato plants
Biotechnol. Lett.
29
1135-1142
2007
Leuconostoc mesenteroides, Leuconostoc mesenteroides NRRL B-1355
brenda
Cote, G.L.; Sheng, S.
Penta-, hexa-, and heptasaccharide acceptor products of alternansucrase
Carbohydr. Res.
341
2066-2072
2006
Leuconostoc mesenteroides, Leuconostoc mesenteroides NRRL B-21297
brenda
Bertrand, A.; Morel, S.; Lefoulon, F.; Rolland, Y.; Monsan, P.; Remaud-Simeon, M.
Leuconostoc mesenteroides glucansucrase synthesis of flavonoid glucosides by acceptor reactions in aqueous-organic solvents
Carbohydr. Res.
341
855-863
2006
Leuconostoc mesenteroides, Leuconostoc mesenteroides NRRL B-23192
brenda
Joucla, G.; Pizzut, S.; Monsan, P.; Remaud-Simeon, M.
Construction of a fully active truncated alternansucrase partially deleted of its carboxy-terminal domain
FEBS Lett.
580
763-768
2006
Leuconostoc mesenteroides (Q9RE05)
brenda
Iliev, I.; Vassileva, T.; Ignatova, C.; Ivanova, I.; Haertle, T.; Monsan, P.; Chobert, J.M.
Gluco-oligosaccharides synthesized by glucosyltransferases from constitutive mutants of Leuconostoc mesenteroides strain Lm 28
J. Appl. Microbiol.
104
243-250
2008
Leuconostoc mesenteroides
brenda
Colte, G.; Sheng, S.; Dunlap, C.
Alternansucrase acceptor products
Biocatal. Biotransform.
26
161-168
2008
Leuconostoc mesenteroides
-
brenda
Cote, G.L.
Acceptor products of alternansucrase with gentiobiose. Production of novel oligosaccharides for food and feed and elimination of bitterness
Carbohydr. Res.
344
187-190
2009
Leuconostoc mesenteroides, Leuconostoc mesenteroides NRRL B-21297
brenda
Cote, G.L.; Dunlap, C.A.; Vermillion, K.E.
Glucosylation of raffinose via alternansucrase acceptor reactions
Carbohydr. Res.
344
1951-1959
2009
Leuconostoc mesenteroides, Leuconostoc mesenteroides NRRL B-21297
brenda
Bounaix, M.S.; Gabriel, V.; Robert, H.; Morel, S.; Remaud-Simeon, M.; Gabriel, B.; Fontagne-Faucher, C.
Characterization of glucan-producing Leuconostoc strains isolated from sourdough
Int. J. Food Microbiol.
144
1-9
2010
Leuconostoc citreum (D3JC18), Leuconostoc citreum (D3JBW0), Leuconostoc citreum (D3JC16), Leuconostoc citreum, Leuconostoc citreum B2 (D3JC16), Leuconostoc citreum C-11 (D3JC18), Leuconostoc citreum E16 (D3JBW0), Leuconostoc mesenteroides, Leuconostoc mesenteroides G15
brenda
Hernandez-Hernandez, O.; Cote, G.L.; Kolida, S.; Rastall, R.A.; Sanz, M.L.
In vitro fermentation of alternansucrase raffinose-derived oligosaccharides by human gut bacteria
J. Agric. Food Chem.
59
10901-10906
2011
Leuconostoc mesenteroides, Leuconostoc mesenteroides NRRL B-21297
brenda
Musa, A.; Miao, M.; Zhang, T.; Jiang, B.
Biotransformation of stevioside by Leuconostoc citreum SK24.002 alternansucrase acceptor reaction
Food Chem.
146
23-29
2014
Leuconostoc citreum, Leuconostoc citreum SK24.002
brenda
Molina, M.; Moulis, C.; Monties, N.; Pizzut-Serin, S.; Guieysse, D.; Morel, S.; Cioci, G.; Remaud-Simeon, M.
Deciphering an undecided enzyme investigations of the structural determinants involved in the linkage specificity of alternansucrase
ACS Catal.
9
2222-2237
2019
Leuconostoc citreum (D3JC16), Leuconostoc citreum NRRL B-1355 (D3JC16)
-
brenda
Musa, A.; Jiang, B.; Ma, H.; Gasmalla, M.A.A.; Abdalhai, M.H.; Al-alfarga, A.
Di-glycosyl-stevioside production via Leuconostoc citreum sk24.002 alternansucrase enzymatic reaction and structural characterization
J. Food Meas. Charact.
13
1159-1165
2019
Leuconostoc citreum (D3JC16), Leuconostoc citreum SK24.002 (D3JC16)
-
brenda
Wangpaiboon, K.; Padungros, P.; Nakapong, S.; Charoenwongpaiboon, T.; Rejzek, M.; Field, R.A.; Pichyangkura, R.
An alpha-1,6-and alpha-1,3-linked glucan produced by Leuconostoc citreum ABK-1 alternansucrase with nanoparticle and film-forming properties
Sci. Rep.
8
8340
2018
Leuconostoc citreum (D3JC16), Leuconostoc citreum, Leuconostoc citreum ABK-1 (D3JC16)
brenda
Nguyen, T.T.H.; Lee, D.G.; Apu, M.A.I.; Jung, J.H.; Kim, M.K.; Lim, S.; Chung, B.; Pal, K.; Kim, D.
The bifidogenic effects and dental plaque deformation of non-digestible isomaltooligosaccharides synthesized by dextransucrase and alternansucrase
Enzyme Microb. Technol.
153
109955
2022
Leuconostoc mesenteroides, Leuconostoc mesenteroides NRRL 1355CF10/KM
brenda
Wangpaiboon, K.; Sitthiyotha, T.; Chunsrivirot, S.; Charoenwongpaiboon, T.; Pichyangkura, R.
Unravelling regioselectivity of Leuconostoc citreum ABK-1 alternansucrase by acceptor site engineering
Int. J. Mol. Sci.
22
3229
2021
Leuconostoc citreum (A0A088FXI5), Leuconostoc citreum ABK-1 (A0A088FXI5)
brenda
Molina, M.; Moulis, C.; Monties, N.; Guieysse, D.; Morel, S.; Cioci, G.; Remaud-Simeon, M.
A specific oligosaccharide-binding site in the alternansucrase catalytic domain mediates alternan elongation
J. Biol. Chem.
295
9474-9489
2020
Leuconostoc mesenteroides (Q9RE05)
brenda
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