2.4.1.9: inulosucrase
This is an abbreviated version!
For detailed information about inulosucrase, go to the full flat file.
Word Map on EC 2.4.1.9
-
2.4.1.9
-
farnesyltransferase
-
farnesylation
-
prenylation
-
geranylgeranylation
-
isoprenoids
-
fructooligosaccharides
-
ggtase-i
-
prenyltransferases
-
peptidomimetic
-
h-ras
-
inulin
-
transfructosylation
-
levan
-
ca1a2x
-
15-carbon
-
tipifarnib
-
levansucrase
-
rhob
-
p21ras
-
geranylgeranyltransferase-i
-
reuteri
-
ggtis
-
inulin-type
-
fructosyltransferases
-
1-kestose
-
cvim
-
fructansucrases
-
biotechnology
-
citreum
-
lonafarnib
- 2.4.1.9
-
farnesyltransferase
-
farnesylation
-
prenylation
-
geranylgeranylation
-
isoprenoids
- fructooligosaccharides
- ggtase-i
- prenyltransferases
-
peptidomimetic
- h-ras
- inulin
-
transfructosylation
- levan
-
ca1a2x
-
15-carbon
- tipifarnib
- levansucrase
- rhob
-
p21ras
-
geranylgeranyltransferase-i
- reuteri
-
ggtis
-
inulin-type
- fructosyltransferases
- 1-kestose
- cvim
- fructansucrases
- biotechnology
- citreum
- lonafarnib
Reaction
Synonyms
Ffase, fructansucrase, fructosyltransferase, fructosyltransferase, sucrose 1-, FTase, FTF, GH68 fructansucrase, HugO, INU, InuJ, IS, ISase, IslA, More, sucrose 1-fructosyltransferase, sucrose: 2,1-beta-D-fructan 1-beta-D-fructosyltransferase, sucrose:2,1-beta-D-fructan1-beta-D-fructosyltransferase
ECTree
2.4.1.9 inulosucraseAdvanced search results
results (
results (Engineering
Engineering on EC 2.4.1.9 - inulosucrase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
N301A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
N301S
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
N305A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
N305S
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
N301A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
N301S
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
N305A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
N305S
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
S425A
A417N
site-directed mutagenesis, unaltered activity compared to the wild-type enzyme
A425P
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
A425P/A538S/N543S/D548R/W551T
site-directed mutagenesis, the mutant shows 65% reduced activity compared to the wild-type enzyme
A489G
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
A538S
site-directed mutagenesis, the mutation, located behind the general acid/base, increases the enzyme activity two to threefold
D272N
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
D424N
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
D479A
-
the mutant shows 80% of wild type transglycosylation activity. For hydrolytic activity, the catalytic turnover rate (kcat) of the mutant is slightly lower than that of the wild type enzyme
D520A
D520N
D548R
site-directed mutagenesis, increased activity compared to the wild-type enzyme
D689A
-
for hydrolytic activity, the catalytic turnover rate (kcat) of the mutant is slightly lower than that of the wild type enzyme
E523Q
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
G416E
site-directed mutagenesis, the mutation at the rim of the active site pocket in loop 415-423, increases the hydrolytic activity twofold, without significantly changing the transglycosylation activity
K415R
site-directed mutagenesis, unaltered activity compared to the wild-type enzyme
N365K
site-directed mutagenesis, slightly increased activity compared to the wild-type enzyme
N414A
-
the mutation does not affect fructooligosaccharide production but causes the production of shorter oligosaccharides compared to the wild type
N543A
-
the mutant shows 67% of wild type transglycosylation activity. For hydrolytic activity, the catalytic turnover rate (kcat) of the mutant is slightly lower than that of the wild type enzyme
N543S
N555A
-
the mutant shows 75% of wild type transglycosylation activity. For hydrolytic activity, the catalytic turnover rate (kcat) of the mutant is slightly lower than that of the wild type enzyme
N561A
-
the mutant enzyme incompletely hydrolyzes sucrose at 50°C though equivalent initial enzymatic activity is used
P516L
site-directed mutagenesis, unaltered activity compared to the wild-type enzyme
R423H
R423K
R483A
-
the mutant shows 73% of wild type transglycosylation activity. For hydrolytic activity, the catalytic turnover rate (kcat) of the mutant is slightly lower than that of the wild type enzyme
S442N
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
T366L
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
T366L/A425P/N365K
site-directed mutagenesis, the mutant shows 47% reduced activity compared to the wild-type enzyme
T413K
site-directed mutagenesis, slightly increased activity compared to the wild-type enzyme
T413K/K415R/G416E/A425P/S442N/W486L/P516L
site-directed mutagenesis, the mutant synthesizes 1-kestose only, but at low efficiency, it shows 94% reduced activity compared to the wild-type enzyme
W271N
W340N
W486L
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
W551A
-
the mutant shows 58% of wild type transglycosylation activity. For hydrolytic activity, the catalytic turnover rate (kcat) of the mutant is slightly lower than that of the wild type enzyme. The mutant enzyme incompletely hydrolyzes sucrose at 50°C though equivalent initial enzymatic activity is used
W551T
site-directed mutagenesis, slightly increased activity compared to the wild-type enzyme
A425P
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
-
D272N
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
-
D424N
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
-
D479A
-
the mutant shows 80% of wild type transglycosylation activity. For hydrolytic activity, the catalytic turnover rate (kcat) of the mutant is slightly lower than that of the wild type enzyme
-
D520A
D520N
D689A
-
for hydrolytic activity, the catalytic turnover rate (kcat) of the mutant is slightly lower than that of the wild type enzyme
-
E523Q
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
-
G416E
-
site-directed mutagenesis, the mutation at the rim of the active site pocket in loop 415-423, increases the hydrolytic activity twofold, without significantly changing the transglycosylation activity
-
K415R
-
site-directed mutagenesis, unaltered activity compared to the wild-type enzyme
-
N543A
-
the mutant shows 67% of wild type transglycosylation activity. For hydrolytic activity, the catalytic turnover rate (kcat) of the mutant is slightly lower than that of the wild type enzyme
-
R423H
R423K
R483A
-
the mutant shows 73% of wild type transglycosylation activity. For hydrolytic activity, the catalytic turnover rate (kcat) of the mutant is slightly lower than that of the wild type enzyme
-
T413K
-
site-directed mutagenesis, slightly increased activity compared to the wild-type enzyme
-
W271N
-
altered fructooligosaccharide product pattern from sucrose, synthesizing a much lower amount of oligosaccharide and significantly more polymer than wild-type enzyme. KM-value for sucrose is 15.6fold higher than wild-type value. Vmax is 16.9fold lower than wild-type value
-
W340N
W551A
-
the mutant shows 58% of wild type transglycosylation activity. For hydrolytic activity, the catalytic turnover rate (kcat) of the mutant is slightly lower than that of the wild type enzyme. The mutant enzyme incompletely hydrolyzes sucrose at 50°C though equivalent initial enzymatic activity is used
-
additional information
S425A
-
the mutant displays complex kinetic behavior in which the transfructosylation rate is described by first-order kinetics, while sucrose hydrolysis follows Michaelis-Menten behavior, the hydrolytic activity of S425A is reduced to about 52% of the converted sucrose
D520A
site-directed mutagenesis, reduced activity in absence of Ca2+ at 30°C, reduction in affinity for Ca2+ at higher temperatures, overview
D520A
the mutation causes a strong reduction of activity compared to the wild type enzyme
D520N
site-directed mutagenesis, mutant enzyme is nearly inactive in presence of 1 mM Ca2+ and completely inactive in absence of Ca2+
D520N
the mutation causes a strong reduction of activity compared to the wild type enzyme
N543S
site-directed mutagenesis, slightly increased activity compared to the wild-type enzyme
N543S
site-directed mutagenesis, the mutation, located adjacent to the +1/+2 subsite residue R544, results in synthesis of a reduced variety of fructooligosaccharides compared to the wild-type enzyme
R423K
-
altered fructooligosaccharide product pattern from sucrose, synthesizing a much lower amount of oligosaccharide and significantly more polymer than wild-type enzyme. KM-value for sucrose is 3.3fold higher than wild-type value. Vmax is 28.8fold lower than wild-type value
W271N
-
altered fructooligosaccharide product pattern from sucrose, synthesizing a much lower amount of oligosaccharide and significantly more polymer than wild-type enzyme. KM-value for sucrose is 15.6fold higher than wild-type value. Vmax is 16.9fold lower than wild-type value
W271N
the mutant shows 5.3% of wild type activity. The mutant synthesizes very similar amounts of fructooligosaccarides up to DP 6, but clearly less of DP 7-9
W340N
the mutant shows 0.5% of wild type activity and only synthesizes small amounts of kestose and nystose
D520A
-
the mutation causes a strong reduction of activity compared to the wild type enzyme
-
D520A
-
site-directed mutagenesis, reduced activity in absence of Ca2+ at 30°C, reduction in affinity for Ca2+ at higher temperatures, overview
-
D520N
-
the mutation causes a strong reduction of activity compared to the wild type enzyme
-
D520N
-
site-directed mutagenesis, mutant enzyme is nearly inactive in presence of 1 mM Ca2+ and completely inactive in absence of Ca2+
-
R423K
-
altered fructooligosaccharide product pattern from sucrose, synthesizing a much lower amount of oligosaccharide and significantly more polymer than wild-type enzyme. KM-value for sucrose is 3.3fold higher than wild-type value. Vmax is 28.8fold lower than wild-type value
-
W340N
-
the mutant shows 0.5% of wild type activity and only synthesizes small amounts of kestose and nystose
-
additional information
construction of an enzyme mutant lacking the cell-anchoring motif
additional information
-
construction of an enzyme mutant lacking the cell-anchoring motif
additional information
-
establishing of an enzymatic synthesis process of a series of raffinose-derived oligosaccharides or raffinosyl oligofructosides (RFOS) with degree of polymerization from 4 to 8 developed in presence of raffinose and involving a transfructosylation reaction catalyzed by an inulosucrase from Lactobacillus gasseri DSM 20604, method development, overview. The main synthesized RFOS consist of beta-2,1-linked fructose unit(s) to raffinose: alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranosyl-(1<->2)-beta-D-fructofuranosyl-((1<-2)-beta-D-fructofuranoside)n (where n refers to the number of transferred fructose moieties), structure analysis by NMR spectroscopy
additional information
-
establishing of an enzymatic synthesis process of a series of raffinose-derived oligosaccharides or raffinosyl oligofructosides (RFOS) with degree of polymerization from 4 to 8 developed in presence of raffinose and involving a transfructosylation reaction catalyzed by an inulosucrase from Lactobacillus gasseri DSM 20604, method development, overview. The main synthesized RFOS consist of beta-2,1-linked fructose unit(s) to raffinose: alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranosyl-(1<->2)-beta-D-fructofuranosyl-((1<-2)-beta-D-fructofuranoside)n (where n refers to the number of transferred fructose moieties), structure analysis by NMR spectroscopy
-
additional information
-
construction of an enzyme mutant lacking the cell-anchoring motif
-
additional information
-
deletion of residues 301-303 reduces the enzyme activity
additional information
-
deletion of residues 301-303 reduces the enzyme activity
-
additional information
-
when the C-terminal domain is deleted the resulting enzyme is more active and more hydrolytic than the wild-type enzyme but is more sensitive to inactivation at 40°C
additional information
truncated version IslA2 of 102000 Da lacks C-terminal region, kinetic parameters and stability are similar to wild-type. Truncated version IslA3 of 80000 Da lacks both transition region and C-terminal region, protein is not attached to the cell surface such as wild-type. truncated version IslA4 of 64000 Da lacks part of the N-terminal region and both transition region and C-terminal region and show decrease in stability but increase in kcat value
additional information
-
IslA4 is a truncated form of inulosucrase that contains only the catalytic domain, this truncated form is more hydrolytic than the wild type enzyme and produces both high-molecular-weight inulin and fructooligosaccharides
additional information
-
construction of the truncated enzyme mutant IslA4 that can synthesize high molecular weight inulin from sucrose, with a residual sucrose hydrolytic activity, and a product specificity similar to the multidomain wild-type enzyme. High sucrose concentrations shift the specificity of the reaction towards fructooligosaccharides (FOS) synthesis, which almost eliminates inulin synthesis and leads to a considerable reduction in sucrose hydrolysis. Reactions with low IslA4 activity and a high sucrose activity allow for high levels of FOS synthesis, where 70% sucrose is used for transfer reactions, with 65% corresponding to transfructosylation for the synthesis of FOS, quantitative product analysis, overview
additional information
-
truncated version IslA2 of 102000 Da lacks C-terminal region, kinetic parameters and stability are similar to wild-type. Truncated version IslA3 of 80000 Da lacks both transition region and C-terminal region, protein is not attached to the cell surface such as wild-type. truncated version IslA4 of 64000 Da lacks part of the N-terminal region and both transition region and C-terminal region and show decrease in stability but increase in kcat value
-
additional information
-
in an enzyme disruption mutant,inactivation of inulosucrase slows the formation of cell aggregates. Both glucosyltransferase and inulosucrase contribute to biofilm formation. Ecological performance of the inulosucrase mutant, but not of the glucosyltransferase or fructosyltransferase mutant, is reduced in the gastrointestinal tract of ex-Lactobacillus-free mice when in competition with the parental strain
additional information
-
inactivation of inulosucrase gene is without effect on growth of cells and mutants reach similar cell counts when maltose is offered as substrate. Mutants show impaired growth in media containing sucrose as sole carbon source, form less lactate and ethanol and tolerate lower lactate levels comapred to wild-type. The inulosucrase inactivation mutant constitutively overexpresses glucosyltransferase
additional information
construction of 15 single and four multiple inulosucrase mutants that of residues conserved in inulosucrase enzymes, most of the inulosucrase mutants behave similarly to the wild-type enzyme. But some inulosucrase variants show higher transglycosylation specificity, higher catalytic rates, and different fructooligosaccharide size distributions, without changing the beta(2-1) linkage type in the product
additional information
-
construction of 15 single and four multiple inulosucrase mutants that of residues conserved in inulosucrase enzymes, most of the inulosucrase mutants behave similarly to the wild-type enzyme. But some inulosucrase variants show higher transglycosylation specificity, higher catalytic rates, and different fructooligosaccharide size distributions, without changing the beta(2-1) linkage type in the product
-
additional information
Limosilactobacillus reuteri TMW1.106
-
in an enzyme disruption mutant,inactivation of inulosucrase slows the formation of cell aggregates. Both glucosyltransferase and inulosucrase contribute to biofilm formation. Ecological performance of the inulosucrase mutant, but not of the glucosyltransferase or fructosyltransferase mutant, is reduced in the gastrointestinal tract of ex-Lactobacillus-free mice when in competition with the parental strain
-
