2.4.1.10: levansucrase
This is an abbreviated version!
For detailed information about levansucrase, go to the full flat file.
Word Map on EC 2.4.1.10
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2.4.1.10
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fructosylation
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fructooligosaccharides
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transfructosylation
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mobilis
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zymomonas
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exopolysaccharide
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erwinia
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raffinose
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prebiotics
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inulin
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levan-type
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diazotrophicus
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fructosyltransferases
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leuconostoc
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reuteri
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inulosucrase
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gluconacetobacter
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mesenteroides
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dextransucrase
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sucrose:sucrose
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synthesis
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gluconobacter
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6-kestose
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aquatilis
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rahnella
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exocellular
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invertases
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hpaec-pad
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sourdough
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amylovoran
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antitermination
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oxydans
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food industry
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agriculture
- 2.4.1.10
-
fructosylation
- fructooligosaccharides
-
transfructosylation
- mobilis
-
zymomonas
- exopolysaccharide
- erwinia
- raffinose
-
prebiotics
- inulin
-
levan-type
- diazotrophicus
- fructosyltransferases
- leuconostoc
- reuteri
- inulosucrase
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gluconacetobacter
- mesenteroides
- dextransucrase
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sucrose:sucrose
- synthesis
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gluconobacter
- 6-kestose
- aquatilis
-
rahnella
-
exocellular
- invertases
-
hpaec-pad
-
sourdough
-
amylovoran
-
antitermination
- oxydans
- food industry
- agriculture
Reaction
Synonyms
(2,6)-beta-D-fructan:D-glucose 6-fructosyltransferase, 6-SFT, 6G-FFT2, beta-2,6-fructan: D-glucose-1-fructosyltransferase, beta-2,6-fructan:D-glucose 1-fructosyltransferase, beta-2,6-fructosyltransferase, endolevanase, fructansucrase, fructosyltransferase, sucrose 6-, FTF, Lev, LEV-Y, levanase-sucrase, levansucrase, LevB1, LevB1SacB, LevJ, LEVS, LevU, Lsc, Lsc-3, Lsc2, Lsc3, LscA, LscrA, LSD, LsdA, LvnS, m1ft, M1FT protein, SacB, sucrose 6-fructosyltransferase, sucrose: 2, 6-beta-D-fructan 6-beta-Dfructosyltransferase, sucrose:2,6-beta-D-fructan:6-beta-D-fructosyltransferase, sucrose:fructan 6-fructosyltransferase, T1-LS, T2-LS, type 1 levansucrase
ECTree
2.4.1.10 levansucraseAdvanced search results
results (
results (Engineering
Engineering on EC 2.4.1.10 - levansucrase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
T14V
Y237S
K372A
-
the mutant shows reduced activity compared to the wild type enzyme
K372Y
-
the mutant shows reduced activity compared to the wild type enzyme
N251W
-
the mutant shows reduced activity compared to the wild type enzyme
N251W/K372Y
-
the mutant shows reduced activity compared to the wild type enzyme
K372A
Bacillus licheniformis RN-01
-
the mutant shows reduced activity compared to the wild type enzyme
-
K372Y
Bacillus licheniformis RN-01
-
the mutant shows reduced activity compared to the wild type enzyme
-
N251W
Bacillus licheniformis RN-01
-
the mutant shows reduced activity compared to the wild type enzyme
-
D247A
D86A
E342A
G361F
site-directed mutagenesis, less stable than the wild-type, synthesizes mainly oligosaccharides, still catalyzes the synthesis of low amounts of polymer, pH-optimum 6, affinity for sucrose is reduced, shift of reaction specificity (hydrolysis/transfer)
H243L
H331R
-
invers directed mutation of natural point mutation R331H to H331R restores the wild-type enzyme properties
I341V
N242H
the mutant shows 31fold decrease in catalytic efficiency compared to the wild type enzyme
R331H
-
natural point mutation, low polymerase activity, invers mutation H331R restores the wild-type enzyme properties
R331K
R331L
R331S
R360H
the mutant shows 5fold decrease in catalytic efficiency compared to the wild type enzyme. The mutant still can produce levan, but has 60% less transfructosylation activity
R360K
R360S
R433A
site-directed mutagenesis, synthesizes only oligosaccharides, pH-optimum 6-7, affinity for sucrose is reduced, shift of reaction specificity (hydrolysis/transfer)
S164A
Y429
site-directed mutagenesis, Y429 plays an indirect but important role in catalysis and acceptor specificity, as this is a key residue coordinating the sucrose position in the levansucrase binding pocket through a complex water network
Y429N
H243L
-
the mutant shows 2fold decrease in catalytic efficiency compared to the wild type enzyme
-
S164A
-
the mutant shows 8fold decrease in catalytic efficiency compared to the wild type enzyme
-
A154S
-
the mutant shows reduced activity compared to the wild type enzyme
E404A
the mutant exhibits a decreased thermostability compared to the wild type enzyme
E404C
the mutant exhibits a decreased thermostability compared to the wild type enzyme
E404D
the mutant exhibits a decreased thermostability compared to the wild type enzyme
E404F
the mutant exhibits an enhanced thermostability and the melting temperature of the mutant is enhanced by 1.5°C compared to the wild type enzyme
E404G
the mutant exhibits a decreased thermostability compared to the wild type enzyme
E404H
the mutant exhibits a decreased thermostability compared to the wild type enzyme
E404I
the mutant exhibits an enhanced thermostability and and the melting temperature of the mutant is enhanced by 1.5°C compared to the wild type enzyme
E404K
the mutant exhibits a decreased thermostability compared to the wild type enzyme
E404L
the melting temperature of the mutant is enhanced by 2.8°C and the half-life is increased by 12.5 and 1.3fold at 35 and 45°C, respectively, as compared to the wild type enzyme
E404M
the mutant exhibits a decreased thermostability compared to the wild type enzyme
E404N
the mutant exhibits a decreased thermostability compared to the wild type enzyme
E404P
the mutant exhibits a decreased thermostability compared to the wild type enzyme
E404Q
the mutant exhibits a decreased thermostability compared to the wild type enzyme
E404R
the mutant exhibits a decreased thermostability compared to the wild type enzyme
E404S
the mutant exhibits a decreased thermostability compared to the wild type enzyme
E404T
the mutant exhibits a decreased thermostability compared to the wild type enzyme
E404V
the mutant exhibits an enhanced thermostability and the melting temperature of the mutant is enhanced by 1.4°C compared to the wild type enzyme
E404W
the mutant exhibits an enhanced thermostability and and the melting temperature of the mutant is enhanced by 1.6°C compared to the wild type enzyme
E404Y
the mutant exhibits a decreased thermostability compared to the wild type enzyme
H327A
-
the mutant shows reduced activity compared to the wild type enzyme
H327R
-
the mutant shows reduced activity compared to the wild type enzyme
C339S
kcat/Km for hydrolysis of sucrose is 68.75fold lower than wild-type value
C395S
kcat/Km for hydrolysis of sucrose is 60fold lower than wild-type value
D135N
kcat/Km for hydrolysis of sucrose is 1257fold lower than wild-type value
D309N
site-directed mutagenesis of RDP-motif, no affection of enzyme secretion but hydrolysis activity, 13fold increase of kcat, 71fold decrease of kcat/Km, unaltered Km for sucrose
C339S
-
kcat/Km for hydrolysis of sucrose is 68.75fold lower than wild-type value
-
C395S
-
kcat/Km for hydrolysis of sucrose is 60fold lower than wild-type value
-
D135N
-
kcat/Km for hydrolysis of sucrose is 1257fold lower than wild-type value
-
D500A
D500N
D500A
D500N
D257A
D95A
E350A
E352A
K373A
the mutant shows 2fold decrease in catalytic efficiency compared to the wild type enzyme
K373R
the mutant shows 2fold decrease in catalytic efficiency compared to the wild type enzyme
L118A
N252A
N252H
the mutant shows 8fold decrease in catalytic efficiency compared to the wild type enzyme
R256A
R370A
S173A
S173G
the mutant shows 59fold decrease in catalytic efficiency compared to the wild type enzyme
S173T
the mutant shows 7fold decrease in catalytic efficiency compared to the wild type enzyme
S422A
the mutant shows 4fold decrease in catalytic efficiency compared to the wild type enzyme
W172A
W94A
Y247A
the mutant shows 2fold decrease in catalytic efficiency compared to the wild type enzyme
Y247I
the mutant shows 2fold decrease in catalytic efficiency compared to the wild type enzyme
Y247W
the mutant shows 0.2fold decrease in catalytic efficiency compared to the wild type enzyme
Y421A
Y421F
the mutant shows 33fold decrease in catalytic efficiency compared to the wild type enzyme
Y421M
the mutant shows 302fold decrease in catalytic efficiency compared to the wild type enzyme
Y421W
the mutant shows 101fold decrease in catalytic efficiency compared to the wild type enzyme
Y439A
the mutant shows 2130fold decrease in catalytic efficiency compared to the wild type enzyme
Y439F
the mutant shows 9fold decrease in catalytic efficiency compared to the wild type enzyme
Y439M
the mutant shows 131fold decrease in catalytic efficiency compared to the wild type enzyme
Y439W
the mutant shows 41fold decrease in catalytic efficiency compared to the wild type enzyme
E350A
W172A
D300A
-
the mutant shows 2fold decrease in catalytic efficiency compared to the wild type enzyme
D300N
-
the mutant shows 4fold decrease in catalytic efficiency compared to the wild type enzyme
D333A
-
the mutant shows 6fold decrease in catalytic efficiency compared to the wild type enzyme
D333N
-
the mutant shows 2fold decrease in catalytic efficiency compared to the wild type enzyme
E146Q
-
the mutant shows 2fold decrease in catalytic efficiency compared to the wild type enzyme
E236Q
-
the mutant shows 42fold decrease in catalytic efficiency compared to the wild type enzyme
H321K
-
the mutant shows 75fold decrease in catalytic efficiency compared to the wild type enzyme
H321L
-
the mutant shows 61fold decrease in catalytic efficiency compared to the wild type enzyme
H321R
-
the mutant shows 82fold decrease in catalytic efficiency compared to the wild type enzyme
H321S
-
the mutant shows 234fold decrease in catalytic efficiency compared to the wild type enzyme
Q301A
-
the mutant shows 55fold decrease in catalytic efficiency compared to the wild type enzyme
Q301E
-
the mutant shows 2fold decrease in catalytic efficiency compared to the wild type enzyme
T302P
-
the mutant shows 3fold decrease in catalytic efficiency compared to the wild type enzyme
W61A
-
the mutant shows 137fold decrease in catalytic efficiency compared to the wild type enzyme
W61N
-
the mutant shows 3708fold decrease in catalytic efficiency compared to the wild type enzyme
D219A
D225A
D225N
D300A
D31N
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D333A
D333N
D62A
E110D
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
E146Q
site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme
E211Q
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E236Q
E303A
E303Q
H113A
H113Q
H306A
H321K
H321L
H321R
H321S
L66A
P220A
Q301A
Q301E
R304A
R304C
T302M
T302P
V248A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W109A
W109F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W109R
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
W61A
W61N
W63A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W80R
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
D333N
E211Q
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
H113A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
H113Q
P220A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
D194N
D275N
-
site-directed mutagenesis, enhanced kcat and Km for sucrose, activity with sucrose similar to wild-type, reduced activity with raffinose and stachyose
D302N
-
site-directed mutagenesis, enhanced kcat and Km for sucrose, activity with sucrose similar to wild-type, reduced activity with raffinose and stachyose
D308N
E117Q
E211Q
E278D
E278H
-
site-directed mutagenesis, 210fold reduced kcat and enhanced Km for sucrose, reduced activity with sucrose and reduced activity with raffinose
H296K
H296L
H296Q
-
site-directed mutagenesis, minimal hydrolysis and transfructosylation activities, transfructosylation activity is reduced to 2.5% of the wild-type
H296R
H296S
H296W
Q339H/P340A
-
random mutagenesis, reduced activity with stachyose, slightly enhanced kcat and enhanced Km for sucrose, slightly reduced activity with sucrose
R193H
-
the mutant shows 298fold decrease in catalytic efficiency compared to the wild type enzyme
R193K
-
the mutant shows 521fold decrease in catalytic efficiency compared to the wild type enzyme
V223A
-
random mutagenesis, reduced kcat, highly enhanced Km, and reduced activity with sucrose, enhanced activity with raffinose and 3.8fold with stachyose
W118H
-
the mutant shows 521fold decrease in catalytic efficiency compared to the wild type enzyme
W118N
-
the mutant shows 521fold decrease in catalytic efficiency compared to the wild type enzyme
W47H
-
the mutant shows 695fold decrease in catalytic efficiency compared to the wild type enzyme
W47N
-
the mutant shows 72fold decrease in catalytic efficiency compared to the wild type enzyme
W80R
-
random mutagenesis, reduced kcat for sucrose, enhanced Km, reduced activity with sucrose, slightly reduced activity with raffinose
additional information
Y237S
the mutant efficiently produces a higher amount of short-chain levan-typed fructooligosaccharide than wild type with increased prebiotic activity
Y237S
-
the mutant efficiently produces a higher amount of short-chain levan-typed fructooligosaccharide than wild type with increased prebiotic activity
-
D247A
single site mutant, substitutions have little effect on the active site geometry, catalytically inactive
D86A
single site mutant, substitutions have little effect on the active site geometry, catalytically inactive
E342A
single site mutant, catalytically inactive, the E342A mutant reveals conformational flexibility of functionally relevant side chains in the vicinity of the general acid Glu342, including Arg360, a residue required for levan polymerisation
H243L
site-directed mutagenesis, less stable than the wild-type, pH-optimum 6, shift of reaction specificity (hydrolysis/transfer)
H243L
the mutant shows 2fold decrease in catalytic efficiency compared to the wild type enzyme
R331K
-
site-directed mutagenesis, loss of ability to perform the whole production of levan from sucrose, only capable to perform the first reaction step, the formation of the trisaccharide kestose, higher kcat than the wild-type for sucrose hydrolysis
R331K
mutant enzyme loses the ability to synthesize levan and is only able to produce the trisaccharide kestose
R331L
-
site-directed mutagenesis, loss of ability to perform the whole production of levan from sucrose, only capable to perform the first reaction step, the formation of the trisaccharide kestose, reduced fructosyl-enzyme intermediate formation
R331L
mutant enzyme loses the ability to synthesize levan and is only able to produce the trisaccharide kestose
R331S
-
site-directed mutagenesis, loss of ability to perform the whole production of levan from sucrose, only capable to perform the first reaction step, the formation of the trisaccharide kestose, reduced fructosyl-enzyme intermediate formation
R331S
mutant enzyme loses the ability to synthesize levan and is only able to produce the trisaccharide kestose
R360K
site-directed mutagenesis, pH-optimum 6, affinity for sucrose is reduced, shift of reaction specificity (hydrolysis/transfer)
R360K
-
the immobilized mutant enzyme shows increased activity and is improved for fructosyl-xyloside synthesis compared to the wild-type enzyme
R360K
the mutant shows 1-4fold decrease in catalytic efficiency compared to the wild type enzyme
R360S
site-directed mutagenesis, pH-optimum 6, decrease in activity, affinity for sucrose is reduced, shift of reaction specificity (hydrolysis/transfer)
R360S
the mutant shows 98-226fold decrease in catalytic efficiency compared to the wild type enzyme
S164A
site-directed mutagenesis, S164A is catalytically important, as it maintains the nucleophile in an appropriate position regarding the sucrose molecule. S164A results in a 12fold more stable and less hydrolytic enzyme than the wild-type, with a half-life of 628.0 (+51.0) min, pH-optimum 6, decrease in activity, slightly higher affinity for sucrose
S164A
the mutant shows 8fold decrease in catalytic efficiency compared to the wild type enzyme
Y429N
site-directed mutagenesis, synthesizes only oligosaccharides, pH-optimum 5-6, decrease in activity, affinity for sucrose is reduced, shift of reaction specificity (hydrolysis/transfer)
Y429N
-
the immobilized mutant enzyme shows increased activity and is improved for fructosyl-xyloside synthesis compared to the wild-type enzyme
Y429N
the mutant shows 1015fold decrease in catalytic efficiency compared to the wild type enzyme
D500A
at 45°C the mutant enzyme is inactive in absence of Ca2+, 45% of wild-type activity remains in presence of 1 mM Ca2+
D500A
at 45°C the mutant enzyme is inactive in the absence of Ca2+ ions, with 15% of wild-type activity remaining in the presence of 1 mM Ca2+. In the presence of 1 mM Ca2+ mutant enzyme displays highest activity at 40°C. In the absence of Ca2+ ions, the optimal temperature is 30°C
D500N
at 45°C the mutant enzyme is inactive in absence of Ca2+, 45% of wild-type activity remains in presence of 1 mM Ca2+
D500N
at 45°C the mutant enzyme is inactive in the absence of Ca2+ ions, with 45% of wild-type activity remaining in the presence of 1 mM Ca2+. In the presence of 1 mM Ca2+ mutant enzyme displays highest activity at 40°C. In the absence of Ca2+ ions, the optimal temperature is 30°C
D500A
-
at 45°C the mutant enzyme is inactive in absence of Ca2+, 45% of wild-type activity remains in presence of 1 mM Ca2+
-
D500A
-
at 45°C the mutant enzyme is inactive in the absence of Ca2+ ions, with 15% of wild-type activity remaining in the presence of 1 mM Ca2+. In the presence of 1 mM Ca2+ mutant enzyme displays highest activity at 40°C. In the absence of Ca2+ ions, the optimal temperature is 30°C
-
D500N
-
at 45°C the mutant enzyme is inactive in absence of Ca2+, 45% of wild-type activity remains in presence of 1 mM Ca2+
-
D500N
-
at 45°C the mutant enzyme is inactive in the absence of Ca2+ ions, with 45% of wild-type activity remaining in the presence of 1 mM Ca2+. In the presence of 1 mM Ca2+ mutant enzyme displays highest activity at 40°C. In the absence of Ca2+ ions, the optimal temperature is 30°C
-
R370A
-
site-directed mutagenesis, after a reaction time of 60 min an accumulation of neokestose (2,6-beta-Fru-betaGlc-1,2-beta-Fru, 32.7 mM) is determined, whereas after 19 h, blastose (2,6-beta-Fru-alpha,betaGlc) is the main reaction product (69.7 mM)
R370A
the mutant shows 57fold decrease in catalytic efficiency compared to the wild type enzyme
S173A
the mutant shows 19fold decrease in catalytic efficiency compared to the wild type enzyme
W172A
-
site-directed mutagenesis, 72fold increase of the KM of the wild-type
W172A
the mutant shows 69fold decrease in catalytic efficiency compared to the wild type enzyme
W94A
-
site-directed mutagenesis, 9% of the catalytic efficiency of the wild-type
W94A
the mutant shows 11fold decrease in catalytic efficiency compared to the wild type enzyme
Y421A
the mutant shows 520fold decrease in catalytic efficiency compared to the wild type enzyme
W172A
-
site-directed mutagenesis, 72fold increase of the KM of the wild-type
-
W172A
-
the mutant shows 69fold decrease in catalytic efficiency compared to the wild type enzyme
-
D219A
site-directed mutagenesis, inactive mutant
D225A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D225A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D225N
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D225N
site-directed mutagenesis, the mutant shows enhanced activity compared to the wild-type enzyme
D300A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D300A
site-directed mutagenesis, the mutant shows slightly enhanced activity compared to the wild-type enzyme
D333A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D333A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D333N
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D333N
site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme
D62A
site-directed mutagenesis, inactive mutant
E236Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E236Q
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E303A
site-directed mutagenesis, inactive mutant
E303Q
site-directed mutagenesis, inactive mutant
H113A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
H113A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
H113Q
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
H306A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H306A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H321K
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
H321K
site-directed mutagenesis, almost inactive mutant
H321L
site-directed mutagenesis, almost inactive mutant
H321L
site-directed mutagenesis, almost inactive mutant
H321R
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
H321R
site-directed mutagenesis, almost inactive mutant
H321R
site-directed mutagenesis, significantly decreased polymerizing ability compared to the wild-type
H321S
site-directed mutagenesis, almost inactive mutant
H321S
site-directed mutagenesis, almost inactive mutant
L66A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L66A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
P220A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
P220A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Q301A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Q301A
site-directed mutagenesis, significantly decreased polymerizing ability compared to the wild-type
Q301E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Q301E
site-directed mutagenesis, the mutant shows slightly enhanced activity compared to the wild-type enzyme
R304A
site-directed mutagenesis, almost inactive mutant
R304C
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
T302M
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
T302M
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
T302P
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T302P
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T302P
site-directed mutagenesis, significantly decreased polymerizing ability compared to the wild-type
W109A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
W109A
site-directed mutagenesis, almost inactive mutant
W61A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
W61N
site-directed mutagenesis, almost inactive mutant
D333N
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
D333N
-
site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme
-
H113Q
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
D194N
-
site-directed mutagenesis, 3400fold decreased kcat and 3fold increased Km for sucrose, activity with sucrose similar to wild-type, reduced activity with raffinose and stachyose
D194N
-
the mutant shows 8300fold decrease in catalytic efficiency compared to the wild type enzyme
D308N
-
site-directed mutagenesis, enhanced kcat and Km for sucrose, activity with sucrose similar to wild-type, reduced activity with raffinose and stachyose
D308N
-
the mutant shows 3fold decrease in catalytic efficiency compared to the wild type enzyme
E117Q
-
site-directed mutagenesis, slightly reduced kcat and enhanced Km for sucrose, slightly enhanced activity with sucrose, reduced activity with raffinose and stachyose
E117Q
-
the mutant shows 5fold decrease in catalytic efficiency compared to the wild type enzyme
E211Q
-
site-directed mutagenesis, highly reduced kcat and enhanced Km for sucrose, highly reduced activity with sucrose, reduced activity with raffinose, increased activity with stachyose
E211Q
-
the mutant shows 22fold decrease in catalytic efficiency compared to the wild type enzyme
E278D
-
random mutagenesis, 30fold reduced kcat and reduced Km for sucrose, slightly enhanced activity with sucrose, reduced activity with raffinose
E278D
-
transfructosylation activity of the variant decreases 15% at 15°C as compared to the wild type enzyme
E278D
-
transfructosylation activity of the variant increases 18% at 15°C as compared to the wild type enzyme
H296K
-
site-directed mutagenesis, reduced kcat and highly increased Km for sucrose, unaltered activity with sucrose, increased activity with raffinose, highly increased activity with stachyose
H296K
-
site-directed mutagenesis, minimal hydrolysis and transfructosylation activities, transfructosylation activity is reduced to 4.6% of the wild-type
H296K
-
the mutant shows 29fold decrease in catalytic efficiency compared to the wild type enzyme
H296L
-
site-directed mutagenesis, reduced kcat and highly increased Km for sucrose, unaltered activity with sucrose, increased activity with raffinose, highly increased activity with stachyose
H296L
-
site-directed mutagenesis, minimal hydrolysis and transfructosylation activities, transfructosylation activity is reduced to 1.0% of the wild-type, mediates the accumulation of low amounts of trisaccharide, but did not produce pentasaccharide
H296L
-
the mutant shows 41fold decrease in catalytic efficiency compared to the wild type enzyme
H296R
-
site-directed mutagenesis, reduced kcat and highly increased Km for sucrose, unaltered activity with sucrose, increased activity with raffinose, highly increased activity with stachyose
H296R
Q60114
no ability of the enzyme to form microfibrils and to synthesize levan at pH 6.0
H296R
-
site-directed mutagenesis, retains partial hydrolysis and transfructosylation activities, transfructosylation activity is reduced to 23.1% of the wild-type
H296R
-
the mutant shows 23fold decrease in catalytic efficiency compared to the wild type enzyme
H296S
-
site-directed mutagenesis, reduced kcat and highly increased Km for sucrose, unaltered activity with sucrose, increased activity with raffinose, highly increased activity with stachyose
H296S
-
the mutant shows 77fold decrease in catalytic efficiency compared to the wild type enzyme
H296W
-
site-directed mutagenesis, retains partial hydrolysis and transfructosylation activities, transfructosylation activity is reduced to 19.8% of the wild-type
H296W
-
the mutant shows 14fold decrease in catalytic efficiency compared to the wild type enzyme
additional information
-
allelic mutagenesis of wild-type strain, inactivation of ftf gene, no remaining levansucrase activity in the mutated strain
additional information
-
allelic mutagenesis of wild-type strain, inactivation of ftf gene, no remaining levansucrase activity in the mutated strain
-
additional information
design and evaluation of a bi-enzymatic system: combined use of levansucrase from Bacillus amyloliquefaciens and endoinulinase from Aspergillus niger in a one-step reaction for the synthesis of fructooligosaccharides (FOSs) and oligolevans using sucrose as the sole substrate, overview
additional information
-
design and evaluation of a bi-enzymatic system: combined use of levansucrase from Bacillus amyloliquefaciens and endoinulinase from Aspergillus niger in a one-step reaction for the synthesis of fructooligosaccharides (FOSs) and oligolevans using sucrose as the sole substrate, overview
-
additional information
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covalent immobilization of recombinant purified wild-type and mutant enzymes by glutaraldehyde to give cross-linked enzyme aggregates, CLEAs. Usage of 60% ammonium sulfate, 0.2% glutaraldehyde and 4 mg protein/ml. All CLEAs show higher thermal stability than corresponding soluble enzymes, but in the long term, the operational stability is affected by levan synthesis
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partially purified enzyme immobilization on Ca-alginate beads, or entrapment in agar and agarose, or crosslinking on chitosan by glutaraldehyde, activity of the immobilized enzyme is relatively lower than the activity of the free enzyme. The immobilized levansucrase shows a slight increase in activity compared with the free enzyme above 35°C. The activation energies are 6.62 and 9.27 kcal/mol for free and immobilized enzyme, respectively. The immobilized enzyme shows an increased thermal stability and reduced deactivation energy, as well as increased pH stability at acidic pH
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partially purified enzyme immobilization on Ca-alginate beads, or entrapment in agar and agarose, or crosslinking on chitosan by glutaraldehyde, activity of the immobilized enzyme is relatively lower than the activity of the free enzyme. The immobilized levansucrase shows a slight increase in activity compared with the free enzyme above 35°C. The activation energies are 6.62 and 9.27 kcal/mol for free and immobilized enzyme, respectively. The immobilized enzyme shows an increased thermal stability and reduced deactivation energy, as well as increased pH stability at acidic pH
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deletion mutant, Lactobacillus sanfranciscensis TMW 1392DELTAlev, loses the ability to hydrolyze sucrose, and does not produce fructan or 1-kestose
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Fructilactobacillus sanfranciscensis TMW 1.392
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deletion mutant, Lactobacillus sanfranciscensis TMW 1392DELTAlev, loses the ability to hydrolyze sucrose, and does not produce fructan or 1-kestose
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construction of mutants AD6, AD8, and AD9, that are unable to secrete LsdA due to nptII insertions in the type II secretion, gsp, operon. None of the mutants released extracellular LsdB, the exolavanase organized in one operon with the levansucrase LsdA
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construction of mutants AD6, AD8, and AD9, that are unable to secrete LsdA due to nptII insertions in the type II secretion, gsp, operon. None of the mutants released extracellular LsdB, the exolavanase organized in one operon with the levansucrase LsdA
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enzyme functionally expressed in Pichia pastoris and secreted into the medium shows additional sucrose-sucrose 1-fructosyltransferase activity, methanol induction
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construction of transgenic Nicotiana tabacum and Cichorium intybus plants expressing the 6-SFT gene via Agrobacterium tumefaciens infection, levansucrase activity in leaf and root extracts, levan analysis
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construction of transgenic Nicotiana plumbaginifolia plants that transiently express the functional levansucrase
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enzyme immobilization on wool, leading to higher optimal reaction temperature, low activation energy, higher Km and lower Vmax, compared to the free enzyme, with thermal stability and resistance to chemical denaturation, overview. The immobilized enzyme shows 78.12% of the free enzyme's specific activity
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formation of enzyme-polysaccharide conjugates at 4°C, variations of activity retained of the glycosylated levansucrase are affected by the carbohydrate residue, which is covalently linked to the enzyme molecule, dextran conjugates show highest, pectin conjugates lowest activity. In general, the glycosylated enzyme retains 25-57% of the original specific activity of the free enzyme
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immobilization of whole cells on Ca-alginate, and on different carriers loaf, stone, wool, ceramic by 0.1% glutaraldehyde, enzyme production in continuous fermentation at 30°C and pH 5.3, enzyme production and activities, and reaction parameters, overview
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Vmax values for sucrose splitting of mutants, structure-function analysis of enzyme mutants, overview
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Vmax values for sucrose splitting of mutants, structure-function analysis of enzyme mutants, overview
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Vmax values for sucrose splitting of mutants, structure-function analysis of enzyme mutants, overview
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The His296 mutation influences the substrate recognizing and binding, and then has an effect on sucrose hydrolysis and fructosyl-enzyme intermediate formation. Its mutations weakens the transfructosylation reaction and changes product specificities
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enhanced levan production using chitin-binding domain fused levansucrase immobilized on chitin beads
