2.4.1.5: dextransucrase
This is an abbreviated version!
For detailed information about dextransucrase, go to the full flat file.
Word Map on EC 2.4.1.5
-
2.4.1.5
-
streptococcus
-
mutans
-
glucosylation
-
glucans
-
leuconostoc
-
dental
-
mesenteroides
-
caries
-
udp-glucose
-
oligosaccharide
-
cariogenic
-
sobrinus
-
glucoside
-
water-insoluble
-
difficile
-
plaque
-
maltose
-
glycosyltransferases
-
serotype
-
saliva
-
tooth
-
sanguis
-
gordonii
-
fructosyltransferase
-
udp-glc
-
monoglucosylated
-
dextranase
-
tcda
-
glucansucrase
-
pellicle
-
salivarius
-
gtases
-
galactosyltransferase
-
saliva-coated
-
calnexin
-
viscosus
-
lipid-linked
-
industry
-
food industry
-
aureobasidium
-
oralis
-
pharmacology
-
pseudomembranous
-
medicine
-
3-o-glucoside
-
levansucrase
-
biotechnology
-
alpha-1,6
-
weissella
-
man9glcnac2
-
transglucosylation
-
synthesis
-
glc3man9glcnac2
-
nutrition
-
isomaltose
-
sordellii
-
holotoxins
- 2.4.1.5
- streptococcus
- mutans
-
glucosylation
- glucans
- leuconostoc
-
dental
- mesenteroides
- caries
- udp-glucose
- oligosaccharide
-
cariogenic
- sobrinus
- glucoside
-
water-insoluble
- difficile
- plaque
- maltose
- glycosyltransferases
-
serotype
- saliva
- tooth
- sanguis
- gordonii
- fructosyltransferase
- udp-glc
-
monoglucosylated
- dextranase
- tcda
- glucansucrase
- pellicle
- salivarius
- gtases
-
galactosyltransferase
-
saliva-coated
- calnexin
- viscosus
-
lipid-linked
- industry
- food industry
- aureobasidium
- oralis
- pharmacology
-
pseudomembranous
- medicine
- 3-o-glucoside
- levansucrase
- biotechnology
-
alpha-1,6
- weissella
- man9glcnac2
-
transglucosylation
- synthesis
- glc3man9glcnac2
- nutrition
- isomaltose
- sordellii
-
holotoxins
Reaction
Synonyms
B-512F dextransucrase, B-512FMC dextransucrase, Cab3, CEP, DexT, dextran-sucrase, DS, DSase, DSR, Dsr S protein, DSR-F, DSR-S, DSRB742, DSRBCB4, DSRC39-2, DsrE563, DsrP, DSRS, DSRWC, DsrX, FT045B dextransucrase, glucansucrase, glucosyltransferase, glucosyltransferase, sucrose-1,6-alpha-glucan, glycosyltransferase R, Gtf, Gtf-DSM, GTFR, More, SGE, sucrose 6-glucosyltransferase, sucrose:1, 6-alpha-D-glucan 6-alpha-glucosyltransferase, sucrose:1,6-alpha-D-glucan-6-alpha-D-glucosyltransferase, Wc392-rDSR, WcCab3-DSR
ECTree
2.4.1.5 dextransucraseAdvanced search results
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results (Substrates Products
Substrates Products on EC 2.4.1.5 - dextransucrase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
luteolin + sucrose
luteolin-3'-O-alpha-D-glucopyranoside + luteolin-4'-O-alpha-D-glucopyranoside
sucrose + 1,5-anhydro-D-fructose
alpha-D-glucopyranosyl-(1,6)-1,5-anhydro-D-fructose + alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-O-1,5-anhydro-D-fructose + alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-O-1,5-anhydro-D-fructose
sucrose + 2-chloroethanol
2-chloroethyl alpha-D-glucopyranoside + D-fructose
-
-
-
-
?
sucrose + 4-chlorobutanol
4-chlorobutyl alpha-D-glucopyranoside + D-fructose
-
-
-
-
?
sucrose + 6-chlorohexanol
6-chlorohexyl alpha-D-glucopyranoside + D-fructose
-
-
-
-
?
sucrose + alpha-butylglucopyranoside
alpha-D-glucopyranosyl-(1,6)-O-butyl-alpha-D-glucopyranoside + alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-O-butyl-alpha-D-glucopyranoside
-
-
-
-
?
sucrose + butan-1-ol
butyl alpha-D-glucopyranoside + D-fructose
-
-
-
-
?
sucrose + gentobiose
?
-
glucose transfer from donor sucrose to acceptors releasing D-fructose, acceptor specificity of wild-type and mutant enzymes, overview
-
-
?
sucrose + maltose
?
-
glucose transfer from donor sucrose to acceptors releasing D-fructose, acceptor specificity of wild-type and mutant enzymes, overview
-
-
?
sucrose + methanol
methyl alpha-D-glucopyranoside + D-fructose
-
-
-
-
?
sucrose + N-(tert-butoxycarbonyl)-L-serine methyl ester
N-tert-butoxycarbonyl-3-O-alpha-D-glucopyranosyl-L-serine methyl ester + D-fructose
-
-
-
-
?
sucrose + N-tert-butoxycarbonyl-D-serine methyl ester
N-tert-butoxycarbonyl-3-O-alpha-D-glycopyranosyl-D-serine methyl ester + D-fructose
-
-
-
-
?
sucrose + propan-1-ol
propyl alpha-D-glucopyranoside + D-fructose
-
-
-
-
?
sucrose + salicin
?
-
glucose transfer from donor sucrose to acceptors releasing D-fructose, acceptor specificity of wild-type and mutant enzymes, overview
-
-
?
sucrose + stevioside
13-O-beta-sophorosyl-19-O-beta-isomaltosyl-steviol + 13-O-(beta-(1->6) glucosyl)-beta-glucosylsophorosyl-19-O-beta-isomaltosyl-steviol + 13-O-beta-sophorosyl-19-O-beta-isomaltotriosyl-steviol
sucrose + tert-butanol
D-fructose + tert-butyl alpha-D-glucoside
-
-
-
-
?
1'-beta-D-fructofuranosyl alpha-acarbose
D-fructose + acarbose
-
-
-
-
?
1'-beta-D-fructofuranosyl alpha-acarbose
D-fructose + acarbose
-
-
-
-
?
luteolin + sucrose
luteolin-3'-O-alpha-D-glucopyranoside + luteolin-4'-O-alpha-D-glucopyranoside
-
44% conversion
luteolin-3'-O-alpha-D-glucopyranoside is the major product
-
?
luteolin + sucrose
luteolin-3'-O-alpha-D-glucopyranoside + luteolin-4'-O-alpha-D-glucopyranoside
-
44% conversion
luteolin-3'-O-alpha-D-glucopyranoside is the major product
-
?
luteolin + sucrose
luteolin-3'-O-alpha-D-glucopyranoside + luteolin-4'-O-alpha-D-glucopyranoside
-
44% conversion
luteolin-3'-O-alpha-D-glucopyranoside is the major product
-
?
sucrose
D-fructose + ?
a dextransucrase efficient in synthesizing oligosaccharides is designed. The truncation mutant DSR-S1-DELTAA (residues 1-3087 bp) by deleting the 1494 bp fragment of the C-terminal.The mutant enzyme (MW: 110 kDa) loses activity, when sucrose is used as only substrate. After adding an acceptor, DSR-S1-DELTAA is fully activated but with heavily impaired polysaccharide synthesis ability. The enzyme produces a large amount of oligosaccharides. DSR-S1-DELTAA shows transglycosylation for synthesizing more oligosaccharides of lower degree of polymerization (DP) with different acceptors, and it also improves the selection range of dextransucrase acceptor response to acceptors. The enzyme can be applied in glycodiversifcation studies
-
-
?
sucrose
D-fructose + ?
a dextransucrase efficient in synthesizing oligosaccharides is designed. The truncation mutant DSR-S1-DELTAA (residues 1-3087 bp) by deleting the 1494 bp fragment of the C-terminal.The mutant enzyme (MW: 110 kDa) loses activity, when sucrose is used as only substrate. After adding an acceptor, DSR-S1-DELTAA is fully activated but with heavily impaired polysaccharide synthesis ability. The enzyme produces a large amount of oligosaccharides. DSR-S1-DELTAA shows transglycosylation for synthesizing more oligosaccharides of lower degree of polymerization (DP) with different acceptors, and it also improves the selection range of dextransucrase acceptor response to acceptors. The enzyme can be applied in glycodiversifcation studies
-
-
?
sucrose
D-fructose + ?
dextransucrase capable of producing a dextran polysaccharide with four types of linkages, including 69% (alpha1->6), 24% (alpha1->3), 6% (alpha1->4), and 1% (alpha1->2)
-
-
?
sucrose
D-fructose + ?
dextransucrase capable of producing a dextran polysaccharide with four types of linkages, including 69% (alpha1->6), 24% (alpha1->3), 6% (alpha1->4), and 1% (alpha1->2)
-
-
?
sucrose
D-fructose + dextran
-
free and immobilized enzyme produces 5.7 mg/ml and 2.6 mg/ml of dextran in 2 l bench scale fermenter under optimum reaction conditions
-
-
?
sucrose
D-fructose + dextran
dextran that is produced by wild-type enzyme has 95% alpha(1->6) linkages in the main chains and 5% alpha(1->3) branch linkage. the dextran synthesized by mutant P473S/P856S shows almost no obvious change with comparison of the wild-type enzyme
-
-
?
sucrose
D-fructose + dextran
-
the produced dextran has a molecular size of 800-1000 kDa
-
-
?
sucrose
D-fructose + dextran
dextran that is produced by wild-type enzyme has 95% alpha(1->6) linkages in the main chains and 5% alpha(1->3) branch linkage. the dextran synthesized by mutant P473S/P856S shows almost no obvious change with comparison of the wild-type enzyme
-
-
?
sucrose
D-fructose + dextran
Leuconostoc mesenteroides IBUN 91.2.98
-
the produced dextran has a molecular size of 800-1000 kDa
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
high amounts of enzyme catalyze the hydrolysis of the D-glucose residues from the ends of the dextran chains, giving a decrease in the amount of dextran
-
r
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
native enzyme produces mainly 6-linked glucopyranosylresidues, while Escherichia coli recombinant enzyme produces a glucan consisting of 70% 6-linked glucopyranosyl residues and 15% 3,6-glucopyranosyl residues. Mutant enzyme T350K and S455K produce a glucan with 85% 6-linked glucopyranosyl residues. The mutant T350K/S455K produces adhesive, water-insoluble glucan with 77% 6-linked glucopyranosyl residues, 8% 3,6-linked glucopyranosyl residues and 4% 2,6-linked glucopyranosyl residues
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
with increasing concentrations of sucrose, from 0.1 to 4.0 M, the amount of high-molecular weight dextran decreases with a concomitant increase in low-molecular weight dextran. At 0.1 M sucrose, pH 5.5, and 28°C, 99.8% of the dextran had a MW of more than 1000000 Da and at 4.0 M sucrose, 69.9% have a MW below 100000 Da and 30.1% have a MW of more than 1000000 Da, giving a bimodal distribution. The degree of branching increased from 5% for 0.1 M sucrose to 16.6% for 4.0 M sucrose. The temperature has very little effect on the size of the dextran, which is above 1000000 Da, but it has a significant effect on the degree of branching, which is 4.8% at 4 °C and increases to 14.7% at 45°C. Both the molecular weight and the degree of branching are not significantly affected by different pH values between 4.5 and 6.0
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
dextransucrase preferentially produces an isomaltooligosaccharide series, whose concentration is always low because of the high ability of these products to be elongated and form high molecular weight dextran. In dextransucrase, the A repeats define anchoring zones for the growing chains, favoring their elongation. Based on these results, a semi-processive mechanism involving only one active site and an elongation by the non-reducing end is proposed
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
high amounts of enzyme catalyze the hydrolysis of the D-glucose residues from the ends of the dextran chains, giving a decrease in the amount of dextran
-
r
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
with increasing concentrations of sucrose, from 0.1 to 4.0 M, the amount of high-molecular weight dextran decreases with a concomitant increase in low-molecular weight dextran. At 0.1 M sucrose, pH 5.5, and 28°C, 99.8% of the dextran had a MW of more than 1000000 Da and at 4.0 M sucrose, 69.9% have a MW below 100000 Da and 30.1% have a MW of more than 1000000 Da, giving a bimodal distribution. The degree of branching increased from 5% for 0.1 M sucrose to 16.6% for 4.0 M sucrose. The temperature has very little effect on the size of the dextran, which is above 1000000 Da, but it has a significant effect on the degree of branching, which is 4.8% at 4 °C and increases to 14.7% at 45°C. Both the molecular weight and the degree of branching are not significantly affected by different pH values between 4.5 and 6.0
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
native enzyme produces mainly 6-linked glucopyranosylresidues, while Escherichia coli recombinant enzyme produces a glucan consisting of 70% 6-linked glucopyranosyl residues and 15% 3,6-glucopyranosyl residues. Mutant enzyme T350K and S455K produce a glucan with 85% 6-linked glucopyranosyl residues. The mutant T350K/S455K produces adhesive, water-insoluble glucan with 77% 6-linked glucopyranosyl residues, 8% 3,6-linked glucopyranosyl residues and 4% 2,6-linked glucopyranosyl residues
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
dextransucrase preferentially produces an isomaltooligosaccharide series, whose concentration is always low because of the high ability of these products to be elongated and form high molecular weight dextran. In dextransucrase, the A repeats define anchoring zones for the growing chains, favoring their elongation. Based on these results, a semi-processive mechanism involving only one active site and an elongation by the non-reducing end is proposed
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
participates in glucan synthesis
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
participates in glucan synthesis
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + (1,6-alpha-D-glucosyl)n
D-fructose + (1,6-alpha-D-glucosyl)n+1
-
-
-
?
sucrose + 1,5-anhydro-D-fructose
alpha-D-glucopyranosyl-(1,6)-1,5-anhydro-D-fructose + alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-O-1,5-anhydro-D-fructose + alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-O-1,5-anhydro-D-fructose
-
the amount of 1,5-anhydro-D-fructo-glucooligosaccharides produced and the average DP increases by using a high sucrose/1,5-anhydro-D-fructose molar ratio and high total sugar concentration
-
-
?
sucrose + 1,5-anhydro-D-fructose
alpha-D-glucopyranosyl-(1,6)-1,5-anhydro-D-fructose + alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-O-1,5-anhydro-D-fructose + alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-O-1,5-anhydro-D-fructose
-
the amount of 1,5-anhydro-D-fructo-glucooligosaccharides produced and the average DP increases by using a high sucrose/1,5-anhydro-D-fructose molar ratio and high total sugar concentration
-
-
?
sucrose + 3-methyl-1-butanol
D-fructose + 3-methylbutyl alpha-D-glucoside
-
-
-
-
?
sucrose + 3-methyl-1-butanol
D-fructose + 3-methylbutyl alpha-D-glucoside
-
-
-
-
?
sucrose + alpha-D-glucopyranoside
?
-
three homologous series (S1S3) of methyl alpha-D-glucooligosaccharides. Series S2 and S3 are characterized by the presence of alpha(1,2) linkages, in combination with alpha(1,6) bonds. Two parameters, sucrose to acceptor concentration ratio (S/A) and the total sugar concentration (TSC) determine the yield of methyl alpha-D-glucooligosaccharides. The maximum concentration achieved of the first acceptor product, methyl alpha-D-isomaltoside, is 65 mM using a S/A 1:4 and a TSC of 336 g/l. When increasing temperature, a shift of selectivity towards compounds containing alpha(1,2) bonds is observed. The formation of leucrose as a side process reaches values of 32 g/l at high sucrose concentrations
-
-
?
sucrose + alpha-D-glucopyranoside
?
-
three homologous series (S1S3) of methyl alpha-D-glucooligosaccharides. Series S2 and S3 are characterized by the presence of alpha(1,2) linkages, in combination with alpha(1,6) bonds. Two parameters, sucrose to acceptor concentration ratio (S/A) and the total sugar concentration (TSC) determine the yield of methyl alpha-D-glucooligosaccharides. The maximum concentration achieved of the first acceptor product, methyl alpha-D-isomaltoside, is 65 mM using a S/A 1:4 and a TSC of 336 g/l. When increasing temperature, a shift of selectivity towards compounds containing alpha(1,2) bonds is observed. The formation of leucrose as a side process reaches values of 32 g/l at high sucrose concentrations
-
-
?
sucrose + caffeic acid
D-fructose + caffeic acid-3-O-alpha-D-glucopyranoside
-
-
-
-
?
sucrose + caffeic acid
D-fructose + caffeic acid-3-O-alpha-D-glucopyranoside
-
-
-
-
?
sucrose + cellobiose
D-fructose + ?
a dextransucrase efficient in synthesizing oligosaccharides is designed. The truncation mutant DSR-S1-DELTAA (residues 1-3087 bp) by deleting the 1494 bp fragment of the C-terminal.The mutant enzyme (MW: 110 kDa) loses activity, when sucrose is used as only substrate. After adding an acceptor, DSR-S1-DELTAA is fully activated but with heavily impaired polysaccharide synthesis ability. The enzyme produces a large amount of oligosaccharides. DSR-S1-DELTAA shows transglycosylation for synthesizing more oligosaccharides of lower degree of polymerization (DP) with different acceptors, and it also improves the selection range of dextransucrase acceptor response to acceptors. The enzyme can be applied in glycodiversifcation studies
-
-
?
sucrose + cellobiose
D-fructose + ?
a dextransucrase efficient in synthesizing oligosaccharides is designed. The truncation mutant DSR-S1-DELTAA (residues 1-3087 bp) by deleting the 1494 bp fragment of the C-terminal.The mutant enzyme (MW: 110 kDa) loses activity, when sucrose is used as only substrate. After adding an acceptor, DSR-S1-DELTAA is fully activated but with heavily impaired polysaccharide synthesis ability. The enzyme produces a large amount of oligosaccharides. DSR-S1-DELTAA shows transglycosylation for synthesizing more oligosaccharides of lower degree of polymerization (DP) with different acceptors, and it also improves the selection range of dextransucrase acceptor response to acceptors. The enzyme can be applied in glycodiversifcation studies
-
-
?
sucrose + chlorogenic acid
D-fructose + chlorogenic acid-4'-O-alpha-D-glucopyranoside
-
production yield of chlorogenic acid-4'-O-alpha-D-glucopyranoside is 44.0% or 141 mM as determined by response surface methodology
-
-
?
sucrose + chlorogenic acid
D-fructose + chlorogenic acid-4'-O-alpha-D-glucopyranoside
-
production yield of chlorogenic acid-4'-O-alpha-D-glucopyranoside is 44.0% or 141 mM as determined by response surface methodology
-
-
?
sucrose + D-glucose
D-fructose + isomalto-oligosaccharide + isomaltose + leucrose
-
isomalto-oligosaccharides from DP3 to DP5 along with isomaltose 44 (DP2) and leucrose (DP2) are synthesized
-
-
?
sucrose + D-glucose
D-fructose + isomalto-oligosaccharide + isomaltose + leucrose
Weissella cibaria RBA12
-
isomalto-oligosaccharides from DP3 to DP5 along with isomaltose 44 (DP2) and leucrose (DP2) are synthesized
-
-
?
sucrose + D-glucose
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
products determined are leucrose, isomaltose, glucosyl leucroside, isomaltotriose, isomaltosyl leucroside, and isomaltotetrose
-
?
sucrose + D-glucose
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
products determined are leucrose, isomaltose, glucosyl leucroside, isomaltotriose, isomaltosyl leucroside, and isomaltotetrose
-
?
sucrose + dextran
?
-
glucose transfer reaction, determination of the dextransucrase minimal motif involved in dextran binding, strong interaction with dextran is localized between amino acids N1397 and A1527 of the C-terminal domain, GBD-7, and consists of six YG repeats, overview. The motif containing enzyme shows very high affinity for isomaltohexaose and longer dextrans and is involved in polymer formation, overview
-
-
?
sucrose + dextran
?
-
glucose transfer reaction, determination of the dextransucrase minimal motif involved in dextran binding, strong interaction with dextran is localized between amino acids N1397 and A1527 of the C-terminal domain, GBD-7, and consists of six YG repeats, overview. The motif containing enzyme shows very high affinity for isomaltohexaose and longer dextrans and is involved in polymer formation, overview
-
-
?
sucrose + dextran
?
-
dextransucrase exhibits both hydrolytic and transferase activities. It catalyses the transfer of glucosyl residues from sucrose to dextran to form complex polysaccharides
-
-
?
sucrose + dextran
?
-
dextransucrase exhibits both hydrolytic and transferase activities. It catalyses the transfer of glucosyl residues from sucrose to dextran to form complex polysaccharides
-
-
?
sucrose + dextran
D-fructose + ?
-
glucose transfer, a step in production of isomaltose, overview
-
-
?
sucrose + dextran
D-fructose + ?
-
glucose transfer, a step in production of isomaltose, overview
-
-
?
sucrose + dextran
D-fructose + ?
-
glucose transfer
-
-
?
sucrose + dextran
D-fructose + elongated dextran
-
-
-
?
sucrose + dextran
D-fructose + elongated dextran
-
-
-
?
sucrose + ethanol
D-fructose + ethyl alpha-D-glucoside
-
-
-
-
?
sucrose + hydroquinone
D-fructose + 4-hydroxyphenyl-alpha-D-glucopyranoside
-
optimum condition for 4-hydroxyphenyl-alpha-D-glucopyranoside synthesis is 450 mM hydroquinone, 215 mM sucrose, and 0.55 U/ml dextransucrase
NMR product identification, the product shows antioxidant nitrite- and diphenylpicryl-hydrazyl scavenging activity, to a higher extent than beta-arbutin
-
?
sucrose + hydroquinone
D-fructose + 4-hydroxyphenyl-alpha-D-glucopyranoside
-
optimum condition for 4-hydroxyphenyl-alpha-D-glucopyranoside synthesis is 450 mM hydroquinone, 215 mM sucrose, and 0.55 U/ml dextransucrase
NMR product identification, the product shows antioxidant nitrite- and diphenylpicryl-hydrazyl scavenging activity, to a higher extent than beta-arbutin
-
?
sucrose + isomaltohexaose
?
-
glucose transfer reaction, determination of the dextransucrase minimal motif involved in dextran binding, strong interaction with dextran is localized between amino acids N1397 and A1527 of the C-terminal domain, GBD-7, and consists of six YG repeats, overview. The motif containing enzyme shows very high affinity for isomaltohexaose and longer dextrans and is involved in polymer formation, overview
-
-
?
sucrose + isomaltohexaose
?
-
glucose transfer reaction, determination of the dextransucrase minimal motif involved in dextran binding, strong interaction with dextran is localized between amino acids N1397 and A1527 of the C-terminal domain, GBD-7, and consists of six YG repeats, overview. The motif containing enzyme shows very high affinity for isomaltohexaose and longer dextrans and is involved in polymer formation, overview
-
-
?
sucrose + isomaltose
D-fructose + isomaltotriose
-
-
-
-
?
sucrose + isomaltose
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
products determined are leucroside, glucosyl leucroside, isomaltotriose, and isomaltotetraose
-
?
sucrose + isomaltose
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
products determined are leucroside, glucosyl leucroside, isomaltotriose, and isomaltotetraose
-
?
sucrose + L-ascorbic acid
D-fructose + L-ascorbic acid 2-glucoside
recombinant glucansucrase
the glycosylated product has the potential as an antioxidant in industrial applications
-
?
sucrose + L-ascorbic acid
D-fructose + L-ascorbic acid 2-glucoside
recombinant glucansucrase
the glycosylated product has the potential as an antioxidant in industrial applications
-
?
sucrose + lactulose
D-fructose + lactulosucrose
-
-
i.e. beta-D-Gal-(1->4)-beta-D-Fru-(2->1)-alpha-D-Glu, structure determination by NMR, overview
-
?
sucrose + lactulose
D-fructose + lactulosucrose
-
-
i.e. beta-D-Gal-(1->4)-beta-D-Fru-(2->1)-alpha-D-Glu, structure determination by NMR, overview
-
?
sucrose + maltose
D-fructose + ?
a dextransucrase efficient in synthesizing oligosaccharides is designed. The truncation mutant DSR-S1-DELTAA (residues 1-3087 bp) by deleting the 1494 bp fragment of the C-terminal.The mutant enzyme (MW: 110 kDa) loses activity, when sucrose is used as only substrate. After adding an acceptor, DSR-S1-DELTAA is fully activated but with heavily impaired polysaccharide synthesis ability. The enzyme produces a large amount of oligosaccharides. DSR-S1-DELTAA shows transglycosylation for synthesizing more oligosaccharides of lower degree of polymerization (DP) with different acceptors, and it also improves the selection range of dextransucrase acceptor response to acceptors. The enzyme can be applied in glycodiversifcation studies
-
-
?
sucrose + maltose
D-fructose + ?
a dextransucrase efficient in synthesizing oligosaccharides is designed. The truncation mutant DSR-S1-DELTAA (residues 1-3087 bp) by deleting the 1494 bp fragment of the C-terminal.The mutant enzyme (MW: 110 kDa) loses activity, when sucrose is used as only substrate. After adding an acceptor, DSR-S1-DELTAA is fully activated but with heavily impaired polysaccharide synthesis ability. The enzyme produces a large amount of oligosaccharides. DSR-S1-DELTAA shows transglycosylation for synthesizing more oligosaccharides of lower degree of polymerization (DP) with different acceptors, and it also improves the selection range of dextransucrase acceptor response to acceptors. The enzyme can be applied in glycodiversifcation studies
-
-
?
sucrose + maltose
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
products determined are panose, alpha-isomaltosyl-1,6-alpha-D-glucopyranosyl-1,4-D-glucopyranose, and alpha-isomaltotriosyl-1,6-alpha-D-glucopyranosyl-1,4-D-glucopyranose
-
?
sucrose + maltose
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
products determined are panose, alpha-isomaltosyl-1,6-alpha-D-glucopyranosyl-1,4-D-glucopyranose, and alpha-isomaltotriosyl-1,6-alpha-D-glucopyranosyl-1,4-D-glucopyranose
-
?
sucrose + maltose
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
glucooligosaccarides are produced through the acceptor reaction with maltose, a homologous series of isomaltooligosac-charides with reducing end maltose units
-
?
sucrose + methanol
D-fructose + methyl alpha-D-glucoside
-
-
-
-
?
sucrose + n-propanol
D-fructose + propyl alpha-D-glucoside
-
-
-
-
?
sucrose + n-propanol
D-fructose + propyl alpha-D-glucoside
-
-
-
-
?
sucrose + raffinose
D-fructose + ?
a dextransucrase efficient in synthesizing oligosaccharides is designed. The truncation mutant DSR-S1-DELTAA (residues 1-3087 bp) by deleting the 1494 bp fragment of the C-terminal.The mutant enzyme (MW: 110 kDa) loses activity, when sucrose is used as only substrate. After adding an acceptor, DSR-S1-DELTAA is fully activated but with heavily impaired polysaccharide synthesis ability. The enzyme produces a large amount of oligosaccharides. DSR-S1-DELTAA shows transglycosylation for synthesizing more oligosaccharides of lower degree of polymerization (DP) with different acceptors, and it also improves the selection range of dextransucrase acceptor response to acceptors. The enzyme can be applied in glycodiversifcation studies
-
-
?
sucrose + raffinose
D-fructose + ?
a dextransucrase efficient in synthesizing oligosaccharides is designed. The truncation mutant DSR-S1-DELTAA (residues 1-3087 bp) by deleting the 1494 bp fragment of the C-terminal.The mutant enzyme (MW: 110 kDa) loses activity, when sucrose is used as only substrate. After adding an acceptor, DSR-S1-DELTAA is fully activated but with heavily impaired polysaccharide synthesis ability. The enzyme produces a large amount of oligosaccharides. DSR-S1-DELTAA shows transglycosylation for synthesizing more oligosaccharides of lower degree of polymerization (DP) with different acceptors, and it also improves the selection range of dextransucrase acceptor response to acceptors. The enzyme can be applied in glycodiversifcation studies
-
-
?
sucrose + stachyose tetrahydrate
D-fructose + ?
a dextransucrase efficient in synthesizing oligosaccharides is designed. The truncation mutant DSR-S1-DELTAA (residues 1-3087 bp) by deleting the 1494 bp fragment of the C-terminal.The mutant enzyme (MW: 110 kDa) loses activity, when sucrose is used as only substrate. After adding an acceptor, DSR-S1-DELTAA is fully activated but with heavily impaired polysaccharide synthesis ability. The enzyme produces a large amount of oligosaccharides. DSR-S1-DELTAA shows transglycosylation for synthesizing more oligosaccharides of lower degree of polymerization (DP) with different acceptors, and it also improves the selection range of dextransucrase acceptor response to acceptors. The enzyme can be applied in glycodiversifcation studies
-
-
?
sucrose + stachyose tetrahydrate
D-fructose + ?
a dextransucrase efficient in synthesizing oligosaccharides is designed. The truncation mutant DSR-S1-DELTAA (residues 1-3087 bp) by deleting the 1494 bp fragment of the C-terminal.The mutant enzyme (MW: 110 kDa) loses activity, when sucrose is used as only substrate. After adding an acceptor, DSR-S1-DELTAA is fully activated but with heavily impaired polysaccharide synthesis ability. The enzyme produces a large amount of oligosaccharides. DSR-S1-DELTAA shows transglycosylation for synthesizing more oligosaccharides of lower degree of polymerization (DP) with different acceptors, and it also improves the selection range of dextransucrase acceptor response to acceptors. The enzyme can be applied in glycodiversifcation studies
-
-
?
sucrose + stevioside
13-O-beta-sophorosyl-19-O-beta-isomaltosyl-steviol + 13-O-(beta-(1->6) glucosyl)-beta-glucosylsophorosyl-19-O-beta-isomaltosyl-steviol + 13-O-beta-sophorosyl-19-O-beta-isomaltotriosyl-steviol
-
-
-
-
?
sucrose + stevioside
13-O-beta-sophorosyl-19-O-beta-isomaltosyl-steviol + 13-O-(beta-(1->6) glucosyl)-beta-glucosylsophorosyl-19-O-beta-isomaltosyl-steviol + 13-O-beta-sophorosyl-19-O-beta-isomaltotriosyl-steviol
Leuconostoc mesenteroides B-512 F/KM
-
-
-
-
?
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
-
a highly processive mechanism of dextran biosynthesis, overview
-
-
?
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
-
the enzyme performs dextran synthesis from sucrose, but D-glucose and sucrose are no initiator primers. Both D-glucose and dextran are covalently attached to B-512FMC dextransucrase at the active site during polymerization. The D-glucose moieties of sucrose are added to the reducing ends of the covalently linked growing dextran chains. Asp551, Glu589, and Asp 622 at the active sites of glucansucrases participate in the polymerization of dextran and related glucans from a single active site by the addition of the D-glucose moiety of sucrose to the reducing ends of the covalently linked glucan chains in a two catalytic-site, insertion mechanism overview. In the early stages of the reaction the products are D-glucose, D-fructose, leucrose, and isomaltodextrins in low, exponentially decreasing amounts from DP 2-5, with minuscule amounts of DP 6-12, but exponentially decreasing amounts of isomaltodextrins, down to minuscule amounts of DP 20-25, overview
-
-
?
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
-
a highly processive mechanism of dextran biosynthesis, overview
-
-
?
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
-
the enzyme performs dextran synthesis from sucrose, but D-glucose and sucrose are no initiator primers. Both D-glucose and dextran are covalently attached to B-512FMC dextransucrase at the active site during polymerization. The D-glucose moieties of sucrose are added to the reducing ends of the covalently linked growing dextran chains. Asp551, Glu589, and Asp 622 at the active sites of glucansucrases participate in the polymerization of dextran and related glucans from a single active site by the addition of the D-glucose moiety of sucrose to the reducing ends of the covalently linked glucan chains in a two catalytic-site, insertion mechanism overview. In the early stages of the reaction the products are D-glucose, D-fructose, leucrose, and isomaltodextrins in low, exponentially decreasing amounts from DP 2-5, with minuscule amounts of DP 6-12, but exponentially decreasing amounts of isomaltodextrins, down to minuscule amounts of DP 20-25, overview
-
-
?
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
-
-
-
-
?
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
-
-
-
-
?
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1,6)-alpha-D-glucosyl]n
D-fructose + [(1,6)-alpha-D-glucosyl]n+1
In the presence of maltose, the most abundant reaction product is panose, i.e. MP1 or alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,4)-D-glucopyranose, with 35.3%, detailed NMR product identification and structure analysis, overview
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
structural properties of exopolysaccharides produced, overview
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
Latilactobacillus curvatus TMW 1.624
-
-
structural properties of exopolysaccharides produced, overview
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
substrate is dextran
product analysis by thin layer chromatography
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
substrate is dextran
product analysis by thin layer chromatography
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
the structure of the commercial B-512F dextran synthesized by strain B-512F dextran sucrase is composed of D-glucose residues, containing 95% alpha-(1,6) linkages in the main chains and 5% alpha-(1,3) branch linkages, the structure of the dextran synthesized by strain FT045B dextran sucrase is composed of D-glucose residues, containing 97.9% alpha-(1,6) linkages in the main chains and 2.1% alpha-(1,3) branch linkages
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
DSase-catalyzed dextran elongation
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
sucrose is the preferred donor substrate
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
the structure of the commercial B-512F dextran synthesized by strain B-512F dextran sucrase is composed of D-glucose residues, containing 95% alpha-(1,6) linkages in the main chains and 5% alpha-(1,3) branch linkages, the structure of the dextran synthesized by strain FT045B dextran sucrase is composed of D-glucose residues, containing 97.9% alpha-(1,6) linkages in the main chains and 2.1% alpha-(1,3) branch linkages
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
sucrose is the preferred donor substrate
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
the structure of the commercial B-512F dextran synthesized by strain B-512F dextran sucrase is composed of D-glucose residues, containing 95% alpha-(1,6) linkages in the main chains and 5% alpha-(1,3) branch linkages, the structure of the dextran synthesized by strain FT045B dextran sucrase is composed of D-glucose residues, containing 97.9% alpha-(1,6) linkages in the main chains and 2.1% alpha-(1,3) branch linkages
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
structural properties of exopolysaccharides produced, overview
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
Ligilactobacillus animalis TMW 1.971
-
-
structural properties of exopolysaccharides produced, overview
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
structural properties of exopolysaccharides produced, overview
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
Limosilactobacillus reuteri TMW 1.106
-
-
structural properties of exopolysaccharides produced, overview
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
JX679020
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
JX679020
best at 5% sucrose in 20 mM sodium acetate buffer
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
JX679020
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
JX679020
best at 5% sucrose in 20 mM sodium acetate buffer
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
production of dextran
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
production of dextran, optimal at 5% w/v sucrose
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
production of dextran
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
production of dextran, optimal at 5% w/v sucrose
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
substrate is dextran
product determination by NMR spectroscopy
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
substrate is dextran
the produced dextran confirmes the presence of main chain alpha-(1->6) linkages with only 3.0% of alpha-(1->3) branching, of which some are elongated
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
dextran
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
-
-
-
?
sucrose + [(1->6)-alpha-D-glucosyl]n
D-fructose + [(1->6)-alpha-D-glucosyl]n+1
substrate is dextran
product determination by NMR spectroscopy
-
?
additional information
?
-
-
glucose transfer from sucrose, synthesis of panose
-
-
?
additional information
?
-
the recombinant enzyme successfully produces a series of isomaltooligosaccharides from sucrose and maltose, on the basis of its transglycosylation activity
-
-
?
additional information
?
-
DexT catalyzes the polymerization of sucrose to dextran via a transglucosyl reaction
-
-
?
additional information
?
-
dextransucrase DSR-F from Leuconostoc citreum B/110-1-2 is a novel sucrose glucosyltransferase specific for alpha-1,6 and alpha-1,3 glucosidic bond synthesis, with alpha-1,4 branching
-
-
?
additional information
?
-
-
dextransucrase DSR-F from Leuconostoc citreum B/110-1-2 is a novel sucrose glucosyltransferase specific for alpha-1,6 and alpha-1,3 glucosidic bond synthesis, with alpha-1,4 branching
-
-
?
additional information
?
-
-
dextransucrase promotes the sucrose cleavage polymerizing the glucose into dextran chain and releasing the fructose moiety
-
-
?
additional information
?
-
structural analysis, by HPAEC-PAD, HPSEC, and 13C-NMR, of the polymer and oligodextrans produced by the B/110-1-2 dextransucrases, overview
-
-
?
additional information
?
-
-
structural analysis, by HPAEC-PAD, HPSEC, and 13C-NMR, of the polymer and oligodextrans produced by the B/110-1-2 dextransucrases, overview
-
-
?
additional information
?
-
the recombinant enzyme catalyzes oligosaccharides synthesis from sucrose as donor and maltose acceptor
-
-
?
additional information
?
-
-
the recombinant enzyme catalyzes oligosaccharides synthesis from sucrose as donor and maltose acceptor
-
-
?
additional information
?
-
dextransucrase DSR-F from Leuconostoc citreum B/110-1-2 is a novel sucrose glucosyltransferase specific for alpha-1,6 and alpha-1,3 glucosidic bond synthesis, with alpha-1,4 branching
-
-
?
additional information
?
-
-
dextransucrase DSR-F from Leuconostoc citreum B/110-1-2 is a novel sucrose glucosyltransferase specific for alpha-1,6 and alpha-1,3 glucosidic bond synthesis, with alpha-1,4 branching
-
-
?
additional information
?
-
the recombinant enzyme catalyzes oligosaccharides synthesis from sucrose as donor and maltose acceptor
-
-
?
additional information
?
-
-
the recombinant enzyme catalyzes oligosaccharides synthesis from sucrose as donor and maltose acceptor
-
-
?
additional information
?
-
structural analysis, by HPAEC-PAD, HPSEC, and 13C-NMR, of the polymer and oligodextrans produced by the B/110-1-2 dextransucrases, overview
-
-
?
additional information
?
-
the recombinant enzyme successfully produces a series of isomaltooligosaccharides from sucrose and maltose, on the basis of its transglycosylation activity
-
-
?
additional information
?
-
-
the recombinant enzyme successfully produces a series of isomaltooligosaccharides from sucrose and maltose, on the basis of its transglycosylation activity
-
-
?
additional information
?
-
DexT catalyzes the polymerization of sucrose to dextran via a transglucosyl reaction
-
-
?
additional information
?
-
-
DexT catalyzes the polymerization of sucrose to dextran via a transglucosyl reaction
-
-
?
additional information
?
-
-
dextransucrase promotes the sucrose cleavage polymerizing the glucose into dextran chain and releasing the fructose moiety
-
-
?
additional information
?
-
-
a lysine residue is present at the active site and is essential for the activity
-
-
?
additional information
?
-
-
the enzyme also catalyzes hydrolysis of D-glucose from the non-reducing ends of dextran chains and transfer of D-glucose from the non-reducing ends of dextran chains to maltose with low efficiency
-
-
?
additional information
?
-
-
the enzyme possesses enhanced levels of sucrose hydrolyzing activity
-
-
?
additional information
?
-
the enzyme catalyzes the formation of both alpha-1,6 and alpha1,2-glycosidic linkages. The catalytic domain CD1 is specific for the synthesis of alpha-1,6 glucosidic bonds and CD2 only catalyzes the formation of alpha-1,2 linkage
-
-
?
additional information
?
-
-
activity assay by measurement of release of reducing sugar from sucrose by the 3,5-dinitrosalicylic acid method
-
-
?
additional information
?
-
glucose transfer from sucrose to dextran of about 68 kDa by the recombinant enzyme expressed in Escherichia coli
-
-
?
additional information
?
-
-
glucose transfer from sucrose to dextran of about 68 kDa by the recombinant enzyme expressed in Escherichia coli
-
-
?
additional information
?
-
-
glucose transfer from sucrose to dextrans leading to polymerization with release of D-fructose, the enzyme contains an active site His residue as well as an essential lysine residue
-
-
?
additional information
?
-
-
glucose transfer from sucrose, synthesis of panose
-
-
?
additional information
?
-
-
keta-sucrose, produced by pyranose 2-oxidase, is polymerized to keto-dextran by the dextrasucrase
-
-
?
additional information
?
-
-
synthesis of a series of cellobio-oligosaccharides from cellobiose by dextransucrase performed transglycosylation, method optimization, overview
-
-
?
additional information
?
-
-
the dextransucrase DSRBCB4 synthesizes only alpha-1,6-linked dextran, the recombinantly expressed DSRBCB4 synthesizes oligosaccharides in the presence of maltose or isomaltose as an acceptor, the products including alpha-1,6-linked glucosyl residues in addition to the maltosyl or isomaltosyl residue, conserved amino acid residues in the catalytic core, D530, E568, and D641, that are critical for enzyme activity, NMR product analysis, overview
-
-
?
additional information
?
-
-
the enzyme synthesizes isomaltooligosaccharide, a promising dietary component with prebiotic effect, the long-chain IMOs are preferred to short chain ones owing to the longer persistence in the colon, optimization of synthesis of long-chain IMOs, overview
-
-
?
additional information
?
-
-
wild-type and mutant enzymes from strain Lm M286 produce a resistant glucan, based on endo-dextranase and amyloglucosidase hydrolysis. The extracellular enzymes from strain Lm M286 catalyse acceptor reactions and transfer the glucose unit from sucrose to maltose to produce glucooligosaccharides , synthesisis of a dextran-type polysaccharide, overview
-
-
?
additional information
?
-
-
dextransucrase can possibly transfer acarbose to various types of dextransucrase acceptors
-
-
?
additional information
?
-
engineered recombinant mutant enzyme DXSR, a fusion of dextransucrase and dextranase, produces linear isomalto-oligosaccharides with DP2-DP10 using sucrose as a sole substrate. DXSR gives 30fold higher production of isomalto-oligosaccharides than that of an equal activity mixture of the two enzymes such as dextranase and dextransucrase
-
-
?
additional information
?
-
-
measurement of liberation of D-fructose from sucrose
-
-
?
additional information
?
-
-
no activity with 2-propanol, MALDI-TOF-mass spectrometry and NMR, structures and HMBC correlations, product analysis
-
-
?
additional information
?
-
-
DSase can quickly proceed to elongation because the decomposition rate of the ESdex complex is very small
-
-
?
additional information
?
-
dextran product analysis by treatment with Penicillium dextranase and by thin layer chromatography, and by NMR spectroscopy
-
-
?
additional information
?
-
-
dextran product analysis by treatment with Penicillium dextranase and by thin layer chromatography, and by NMR spectroscopy
-
-
?
additional information
?
-
dextran production by dextransucrase over time at pH 7.0, 30°C, overview
-
-
?
additional information
?
-
dextran production by dextransucrase over time at pH 7.0, 30°C, overview
-
-
?
additional information
?
-
dextran production by dextransucrase over time at pH 7.0, 30°C, overview
-
-
?
additional information
?
-
-
synergistic catalytic manner of recombinant dextransucrase and Hypocrea lixii dextranase in production of isomalto-oligosaccharides, produced by sucrose conversion and dextran hydrolysis, molecular weight change of dextrans, overview. High sucrose concentrations in the dextransucrase and dextranase system lead to accumulation of oligodextrans with molecular weights below 15 kDa. Combined usage of recombinant dextransucrase and Hypocrea lixii dextranase produces isomalto-oligosaccharides with a degree of polymerization of 2-10
-
-
?
additional information
?
-
-
the enzyme also catalyzes the hydrolysis of sucrose to give D-glucose and D-fructose. Leucrose (alpha-D-Glu-(1->5)-D-Fru) formation is attributed to the minor capacity of free D-fructose to act as acceptor in the dextransucrase-catalyzed reactions, formation of leucrose by action of dextransucrase is favored at high fructose concentration. Once the availability of sucrose is very limited, lactulosucrose can then act as donor substrate
-
-
?
additional information
?
-
glucose transfer from sucrose to dextran of about 68 kDa by the recombinant enzyme expressed in Escherichia coli
-
-
?
additional information
?
-
-
glucose transfer from sucrose to dextran of about 68 kDa by the recombinant enzyme expressed in Escherichia coli
-
-
?
additional information
?
-
-
no activity with 2-propanol, MALDI-TOF-mass spectrometry and NMR, structures and HMBC correlations, product analysis
-
-
?
additional information
?
-
-
the dextransucrase DSRBCB4 synthesizes only alpha-1,6-linked dextran, the recombinantly expressed DSRBCB4 synthesizes oligosaccharides in the presence of maltose or isomaltose as an acceptor, the products including alpha-1,6-linked glucosyl residues in addition to the maltosyl or isomaltosyl residue, conserved amino acid residues in the catalytic core, D530, E568, and D641, that are critical for enzyme activity, NMR product analysis, overview
-
-
?
additional information
?
-
dextran product analysis by treatment with Penicillium dextranase and by thin layer chromatography, and by NMR spectroscopy
-
-
?
additional information
?
-
-
dextran product analysis by treatment with Penicillium dextranase and by thin layer chromatography, and by NMR spectroscopy
-
-
?
additional information
?
-
engineered recombinant mutant enzyme DXSR, a fusion of dextransucrase and dextranase, produces linear isomalto-oligosaccharides with DP2-DP10 using sucrose as a sole substrate. DXSR gives 30fold higher production of isomalto-oligosaccharides than that of an equal activity mixture of the two enzymes such as dextranase and dextransucrase
-
-
?
additional information
?
-
-
dextransucrase can possibly transfer acarbose to various types of dextransucrase acceptors
-
-
?
additional information
?
-
-
glucose transfer from sucrose to dextrans leading to polymerization with release of D-fructose, the enzyme contains an active site His residue as well as an essential lysine residue
-
-
?
additional information
?
-
-
the enzyme synthesizes isomaltooligosaccharide, a promising dietary component with prebiotic effect, the long-chain IMOs are preferred to short chain ones owing to the longer persistence in the colon, optimization of synthesis of long-chain IMOs, overview
-
-
?
additional information
?
-
-
the enzyme also catalyzes hydrolysis of D-glucose from the non-reducing ends of dextran chains and transfer of D-glucose from the non-reducing ends of dextran chains to maltose with low efficiency
-
-
?
additional information
?
-
-
synthesis of a series of cellobio-oligosaccharides from cellobiose by dextransucrase performed transglycosylation, method optimization, overview
-
-
?
additional information
?
-
-
the enzyme also catalyzes the hydrolysis of sucrose to give D-glucose and D-fructose. Leucrose (alpha-D-Glu-(1->5)-D-Fru) formation is attributed to the minor capacity of free D-fructose to act as acceptor in the dextransucrase-catalyzed reactions, formation of leucrose by action of dextransucrase is favored at high fructose concentration. Once the availability of sucrose is very limited, lactulosucrose can then act as donor substrate
-
-
?
additional information
?
-
-
wild-type and mutant enzymes from strain Lm M286 produce a resistant glucan, based on endo-dextranase and amyloglucosidase hydrolysis. The extracellular enzymes from strain Lm M286 catalyse acceptor reactions and transfer the glucose unit from sucrose to maltose to produce glucooligosaccharides , synthesisis of a dextran-type polysaccharide, overview
-
-
?
additional information
?
-
dextran production by dextransucrase over time at pH 7.0, 30°C, overview
-
-
?
additional information
?
-
dextran production by dextransucrase over time at pH 7.0, 30°C, overview
-
-
?
additional information
?
-
dextran production by dextransucrase over time at pH 7.0, 30°C, overview
-
-
?
additional information
?
-
the enzyme catalyzes the formation of both alpha-1,6 and alpha1,2-glycosidic linkages. The catalytic domain CD1 is specific for the synthesis of alpha-1,6 glucosidic bonds and CD2 only catalyzes the formation of alpha-1,2 linkage
-
-
?
additional information
?
-
-
the enzyme catalyzes the formation of both alpha-1,6 and alpha1,2-glycosidic linkages. The catalytic domain CD1 is specific for the synthesis of alpha-1,6 glucosidic bonds and CD2 only catalyzes the formation of alpha-1,2 linkage
-
-
?
additional information
?
-
-
the enzyme possesses enhanced levels of sucrose hydrolyzing activity
-
-
?
additional information
?
-
-
a lysine residue is present at the active site and is essential for the activity
-
-
?
additional information
?
-
-
triple mutation N1134S/N1135E/S1136V converts glucosyltransferase from a mainly alpha-(1,4) (about 45%, reuteran) to a mainly alpha-(1,6) (about 80%, dextran) synthesizing enzyme. Mutant enzyme P1026V/I1029V/N1134S/N1135E/S1136V synthesizes an alpha-glucan containing only a very small percentage of alpha-(1,4) glucosidic linkages (about 5%) and a further increased percentage of alpha-(1,6) glucosidic linkages (about 85%)
-
-
?
additional information
?
-
-
triple mutation N1134S/N1135E/S1136V converts glucosyltransferase from a mainly alpha-(1,4) (about 45%, reuteran) to a mainly alpha-(1,6) (about 80%, dextran) synthesizing enzyme. Mutant enzyme P1026V/I1029V/N1134S/N1135E/S1136V synthesizes an alpha-glucan containing only a very small percentage of alpha-(1,4) glucosidic linkages (about 5%) and a further increased percentage of alpha-(1,6) glucosidic linkages (about 85%)
-
-
?
additional information
?
-
-
optimization of conditions for dextransucrase activity assay
-
-
?
additional information
?
-
JX679020
no activity with raffinose
-
-
?
additional information
?
-
-
purified dextransucrase possesses an invertase-like activity
-
-
?
additional information
?
-
-
the enzyme shows hydrolytic and glucosyl transferase activities with sucrose
-
-
?
additional information
?
-
-
purified dextransucrase possesses an invertase-like activity
-
-
?
additional information
?
-
-
the enzyme shows hydrolytic and glucosyl transferase activities with sucrose
-
-
?
additional information
?
-
the recombinant DSRWC synthesizes oligosaccharides in the presence of maltose or isomaltose as an acceptor and the synthesized products include alpha-1,6-linked glucosyl residues in addition to the maltosyl or isomaltosyl residue. rDSRWC synthesizes water-soluble polymers using sucrose as substrate, and rDSRBWC synthesizes dextran and leucrose [alpha-D-glucopyranosyl-(1,5)-beta-D-fructofuranose]
-
-
?
additional information
?
-
-
the recombinant DSRWC synthesizes oligosaccharides in the presence of maltose or isomaltose as an acceptor and the synthesized products include alpha-1,6-linked glucosyl residues in addition to the maltosyl or isomaltosyl residue. rDSRWC synthesizes water-soluble polymers using sucrose as substrate, and rDSRBWC synthesizes dextran and leucrose [alpha-D-glucopyranosyl-(1,5)-beta-D-fructofuranose]
-
-
?
additional information
?
-
Cab3 dextransucrase WcCab3-DSR is used for in vitro synthesis of dextran and glucooligosaccharides, product analysis by NMR and and mass spectrometry. Glucooligosaccarides are produced through the acceptor reaction with maltose
-
-
?
additional information
?
-
-
Cab3 dextransucrase WcCab3-DSR is used for in vitro synthesis of dextran and glucooligosaccharides, product analysis by NMR and and mass spectrometry. Glucooligosaccarides are produced through the acceptor reaction with maltose
-
-
?
additional information
?
-
optimization of enzymatic dextran production in wheat bran, overview
-
-
?
additional information
?
-
-
optimization of enzymatic dextran production in wheat bran, overview
-
-
?
additional information
?
-
optimization of enzymatic dextran production in wheat bran, overview
-
-
?
additional information
?
-
-
optimization of enzymatic dextran production in wheat bran, overview
-
-
?
