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Information on EC 2.4.1.9 - inulosucrase
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2.4.1.9 inulosucraseIUBMB Comments
Converts sucrose into inulin and D-glucose. Some other sugars can act as D-fructosyl acceptors.
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Word Map
- 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
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
ftase, inulosucrase, isase, sucrose 1-fructosyltransferase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
fructansucrase
fructosyltransferase
fructosyltransferase, sucrose 1-
-
-
-
-
FTase
FTF
GH68 fructansucrase
HugO
INU
InuJ
IS
ISase
IslA
sucrose 1-fructosyltransferase
-
-
-
-
sucrose: 2,1-beta-D-fructan 1-beta-D-fructosyltransferase
sucrose:2,1-beta-D-fructan1-beta-D-fructosyltransferase
additional information
sucrose: 2,1-beta-D-fructan 1-beta-D-fructosyltransferase
-
-
sucrose: 2,1-beta-D-fructan 1-beta-D-fructosyltransferase
-
-
sucrose: 2,1-beta-D-fructan 1-beta-D-fructosyltransferase
-
additional information
-
enzyme belongs to the family 68 of glucoside hydrolases
additional information
enzyme belongs to the family 68 of glucoside hydrolases
additional information
-
enzyme belongs to the family 68 of glucoside hydrolases
-
additional information
enzyme belongs to the family 68 of glucoside hydrolases
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sucrose + [(beta-D-Fruf-(2->1))n]-alpha-D-Glup = alpha-D-glucose + [(beta-D-Fruf-(2->1))n+1]-alpha-D-Glup
sucrose + [(beta-D-Fruf-(2->1))n]-alpha-D-Glup = alpha-D-glucose + [(beta-D-Fruf-(2->1))n+1]-alpha-D-Glup
-
-
-
-
sucrose + [(beta-D-Fruf-(2->1))n]-alpha-D-Glup = alpha-D-glucose + [(beta-D-Fruf-(2->1))n+1]-alpha-D-Glup
catalytic triad formed by essential residues D272, D424, and E523
-
sucrose + [(beta-D-Fruf-(2->1))n]-alpha-D-Glup = alpha-D-glucose + [(beta-D-Fruf-(2->1))n+1]-alpha-D-Glup
catalytic triad formed by essential residues D272, D424, and E523
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
fructosyl group transfer
-
-
-
-
hexosyl group transfer
-
-
-
-
hydrolysis
transglycosylation
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
sucrose:(2->1)-beta-D-fructan 1-beta-D-fructosyltransferase
Converts sucrose into inulin and D-glucose. Some other sugars can act as D-fructosyl acceptors.
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CAS REGISTRY NUMBER
COMMENTARY
9030-16-4
-
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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
sucrose + sucrose
alpha-D-glucose + medium chain fructooligosaccharides (DP 2-20)
with 300 g/l sucrose, 128.4 g/l of fructooligosaccharide is produced with 85.6% conversion yield. From 400 g/l sucrose, 152.6 g/l of fructooligosaccharides is produced with 76.3% conversion yield
-
-
?
sucrose + [(beta-D-Fruf-(2-1))n]-alpha-D-Glup
alpha-D-glucose + [(beta-D-Fruf-(2-1))n+1]-alpha-D-Glup
3 sucrose + sucrose
3 alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
-
-
-
?
3 sucrose + sucrose
3 alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
enzyme produces a diverse range of fructooligosaccharide molecules and a minor amount of inulin polymer [with beta(21) linkages]
-
-
?
3 sucrose + sucrose
3 alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
enzyme produces a diverse range of fructooligosaccharide molecules and a minor amount of inulin polymer [with beta(21) linkages]
-
-
?
raffinose + [(2->1)-beta-D-fructosyl]n
glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
-
?
raffinose + [(2->1)-beta-D-fructosyl]n
glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
FTase possesses only transfructosylating activity, acts on sucrose by cleaving the beta-1,2 linkage and transferring the fructosyl group to an acceptor molecule such as sucrose and fructooligosaccharides, releasing D-glucose
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
FTase possesses only transfructosylating activity, acts on sucrose by cleaving the beta-1,2 linkage and transferring the fructosyl group to an acceptor molecule such as sucrose and fructooligosaccharides, releasing D-glucose
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
FTase possesses only transfructosylating activity, acts on sucrose by cleaving the beta-1,2 linkage and transferring the fructosyl group to an acceptor molecule such as sucrose and fructooligosaccharides, releasing D-glucose
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
FTase possesses only transfructosylating activity, acts on sucrose by cleaving the beta-1,2 linkage and transferring the fructosyl group to an acceptor molecule such as sucrose and fructooligosaccharides, releasing D-glucose
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
FTase possesses only transfructosylating activity, acts on sucrose by cleaving the beta-1,2 linkage and transferring the fructosyl group to an acceptor molecule such as sucrose and fructooligosaccharides, releasing D-glucose
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
FTase possesses only transfructosylating activity, acts on sucrose by cleaving the beta-1,2 linkage and transferring the fructosyl group to an acceptor molecule such as sucrose and fructooligosaccharides, releasing D-glucose
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
FTase possesses only transfructosylating activity, acts on sucrose by cleaving the beta-1,2 linkage and transferring the fructosyl group to an acceptor molecule such as sucrose and fructooligosaccharides, releasing D-glucose
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
FTase possesses only transfructosylating activity, acts on sucrose by cleaving the beta-1,2 linkage and transferring the fructosyl group to an acceptor molecule such as sucrose and fructooligosaccharides, releasing D-glucose
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
-
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
transferase activity
i.e. inulin, determination of inulin product chain length, overview
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
-
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
transferase activity
i.e. inulin, determination of inulin product chain length, overview
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
-
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
transferase activity
i.e. inulin
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
transferase activity
i.e. inulin
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
transferase activity
i.e. inulin
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
-
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
transferase activity
i.e. inulin
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
-
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
transferase activity
i.e. inulin
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
transferase activity
i.e. inulin
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
transferase activity
i.e. inulin
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
FTase possesses only transfructosylating activity, acts on sucrose by cleaving the beta-1,2 linkage and transferring the fructosyl group to an acceptor molecule such as sucrose and fructooligosaccharides, releasing D-glucose
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
FTase possesses only transfructosylating activity, acts on sucrose by cleaving the beta-1,2 linkage and transferring the fructosyl group to an acceptor molecule such as sucrose and fructooligosaccharides, releasing D-glucose
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
FTase possesses only transfructosylating activity, acts on sucrose by cleaving the beta-1,2 linkage and transferring the fructosyl group to an acceptor molecule such as sucrose and fructooligosaccharides, releasing D-glucose
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
FTase possesses only transfructosylating activity, acts on sucrose by cleaving the beta-1,2 linkage and transferring the fructosyl group to an acceptor molecule such as sucrose and fructooligosaccharides, releasing D-glucose
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
FTase possesses only transfructosylating activity, acts on sucrose by cleaving the beta-1,2 linkage and transferring the fructosyl group to an acceptor molecule such as sucrose and fructooligosaccharides, releasing D-glucose
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
FTase possesses only transfructosylating activity, acts on sucrose by cleaving the beta-1,2 linkage and transferring the fructosyl group to an acceptor molecule such as sucrose and fructooligosaccharides, releasing D-glucose
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
D-glucose + (2,1-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
D-glucose + (2,1-beta-D-fructosyl)n+1
-
-
-
?
sucrose + H2O
alpha-D-glucose + beta-D-fructose
-
hydrolytic activity. Transglycosylation activity is higher in the whole concentration range tested and completely dominating at higher sucrose concentrations
-
-
?
sucrose + H2O
alpha-D-glucose + beta-D-fructose
-
-
-
?
sucrose + H2O
alpha-D-glucose + beta-D-fructose
hydrolytic activity, ratio of transglycosylation to hydrolysis activities is almost 1:1 at 37°C but increases about 26fold at 55°C
-
-
?
sucrose + H2O
alpha-D-glucose + beta-D-fructose
hydrolytic activity, ratio of transglycosylation to hydrolysis activities is almost 1:1 at 37°C but increases about 26fold at 55°C
-
-
?
sucrose + H2O
alpha-D-glucose + beta-D-fructose
-
hydrolytic activity
-
-
?
sucrose + H2O
alpha-D-glucose + beta-D-fructose
-
hydrolytic activity
-
-
?
sucrose + H2O
alpha-D-glucose + beta-D-fructose
-
hydrolytic activity
-
-
?
sucrose + H2O
alpha-D-glucose + beta-D-fructose
hydrolytic activity
-
-
?
sucrose + H2O
alpha-D-glucose + beta-D-fructose
-
hydrolytic activity
-
-
?
sucrose + H2O
alpha-D-glucose + beta-D-fructose
-
hydrolytic activity
-
-
?
sucrose + H2O
alpha-D-glucose + beta-D-fructose
hydrolytic activity
-
-
?
sucrose + H2O
D-fructose + D-glucose
at sucrose concentrations lower than 200 mM (at 37°C), hydrolysis is the main enzyme activity. At higher sucrose concentrations, transglycosylation increases gradually, reaching 90% or more of total enzyme activity at 1.7 M sucrose
-
-
?
sucrose + H2O
D-fructose + D-glucose
at sucrose concentrations lower than 200 mM (at 37°C), hydrolysis is the main enzyme activity. At higher sucrose concentrations, transglycosylation increases gradually, reaching 90% or more of total enzyme activity at 1.7 M sucrose
-
-
?
sucrose + raffinose
?
synthesizes fructosylraffinose (most likely GalGF2) and a range of larger oligomers (up to GalGF6), and some polymeric material
-
-
?
sucrose + raffinose
?
synthesizes fructosylraffinose (most likely GalGF2) and a range of larger oligomers (up to GalGF6), and some polymeric material
-
-
?
sucrose + raffinose
glucose + 1-kestose
-
-
i.e. beta-D-fructofuranosyl-(2->1)-beta-D-fructofuranosyl-(2->1)-alpha-D-glucopyranoside
-
?
sucrose + raffinose
glucose + 1-kestose
-
-
i.e. beta-D-fructofuranosyl-(2->1)-beta-D-fructofuranosyl-(2->1)-alpha-D-glucopyranoside
-
?
sucrose + sucrose
1-kestose + nystose + fructooligosaccharides
-
-
-
-
?
sucrose + sucrose
1-kestose + nystose + fructooligosaccharides
-
-
-
-
?
sucrose + sucrose
alpha-D-glucose + inulin nanoparticles
-
-
-
-
?
sucrose + sucrose
alpha-D-glucose + inulin nanoparticles
-
-
-
-
?
sucrose + sucrose
alpha-D-glucose + inulin-type fructan
-
-
-
?
sucrose + sucrose
alpha-D-glucose + inulin-type fructan
-
-
-
-
?
sucrose + sucrose
alpha-D-glucose + inulin-type fructan
-
-
-
?
sucrose + sucrose
alpha-D-glucose + inulin-type fructan
-
-
-
-
?
sucrose + sucrose
alpha-D-glucose + inulin-type fructan
-
-
-
?
sucrose + sucrose
alpha-D-glucose + inulin-type fructan
-
-
-
?
sucrose + sucrose
alpha-D-glucose + inulin-type fructan
-
-
-
?
sucrose + sucrose
alpha-D-glucose + inulin-type fructan
-
-
-
?
sucrose + sucrose
alpha-D-glucose + inulin-type fructan
-
-
-
-
?
sucrose + sucrose
alpha-D-glucose + inulin-type fructan
Limosilactobacillus reuteri TMW1.106
-
-
-
?
sucrose + sucrose
alpha-D-glucose + inulin-type fructan
-
-
-
?
sucrose + sucrose
alpha-D-glucose + inulin-type fructan
-
-
-
?
sucrose + sucrose
alpha-D-glucose + inulin-type fructan
-
-
-
?
sucrose + sucrose
alpha-D-glucose + inulin-type fructan
-
-
-
?
sucrose + sucrose
alpha-D-glucose + inulin-type fructan polymer
-
-
-
-
?
sucrose + sucrose
alpha-D-glucose + inulin-type fructan polymer
-
-
-
-
?
sucrose + sucrose
alpha-D-glucose + inulin-type fructooligosaccharides
-
-
-
?
sucrose + sucrose
alpha-D-glucose + inulin-type fructooligosaccharides
-
-
-
?
sucrose + sucrose
alpha-D-glucose + inulin-type oligosaccharide + inulin
-
-
-
?
sucrose + sucrose
alpha-D-glucose + inulin-type oligosaccharide + inulin
-
-
-
?
sucrose + sucrose
alpha-D-glucose + inulin-type oligosaccharide + inulin
-
-
-
?
sucrose + sucrose
alpha-D-glucose + inulin-type oligosaccharide + inulin
-
-
-
?
sucrose + sucrose
alpha-D-glucose + inulin-type oligosaccharide + inulin
-
-
-
-
?
sucrose + sucrose
alpha-D-glucose + inulin-type oligosaccharide + inulin
-
-
-
-
?
sucrose + sucrose
alpha-D-glucose + inulin-type oligosaccharide + inulin
-
-
-
?
sucrose + sucrose
alpha-D-glucose + inulin-type oligosaccharide + inulin
-
-
-
-
?
sucrose + sucrose
alpha-D-glucose + inulin-type oligosaccharide + inulin
Limosilactobacillus reuteri TMW1.106
-
-
-
?
sucrose + sucrose
kestose + nystose + fructooligosaccharides
at sucrose concentrations lower than 200 mM (at 37°C), hydrolysis is the main enzyme activity. At higher sucrose concentrations, transglycosylation increases gradually, reaching 90% or more of total enzyme activity at 1.7 M sucrose. From the very early stage of the reaction, after 5 min incubation, traces of nystose are visible. The nystose concentration remains constant once it reached a similar level to kestose (after 1 h), and synthesis of FOS of a larger size starts. The enzyme synthesizes mainly a broad range of fructooligosaccharides of the inulin type in a non-processive reaction
-
-
?
sucrose + sucrose
kestose + nystose + fructooligosaccharides
at sucrose concentrations lower than 200 mM (at 37°C), hydrolysis is the main enzyme activity. At higher sucrose concentrations, transglycosylation increases gradually, reaching 90% or more of total enzyme activity at 1.7 M sucrose. From the very early stage of the reaction, after 5 min incubation, traces of nystose are visible. The nystose concentration remains constant once it reached a similar level to kestose (after 1 h), and synthesis of FOS of a larger size starts. The enzyme synthesizes mainly a broad range of fructooligosaccharides of the inulin type in a non-processive reaction
-
-
?
sucrose + sucrose
[(beta-D-fructose-(2-1))n]-alpha-D-glucose + alpha-D-glucose
-
transgylcosylation activity. Transglycosylation activity is higher in the whole concentration range tested and completely dominating at higher sucrose concentrations
-
-
?
sucrose + sucrose
[(beta-D-fructose-(2-1))n]-alpha-D-glucose + alpha-D-glucose
transglycosylation activity, ratio of transglycosylation to hydrolysis activities is almost 1:1 at 37°C but increases about 26fold at 55°C
-
-
?
sucrose + sucrose
[(beta-D-fructose-(2-1))n]-alpha-D-glucose + alpha-D-glucose
transglycosylation activity, ratio of transglycosylation to hydrolysis activities is almost 1:1 at 37°C but increases about 26fold at 55°C
-
-
?
sucrose + sucrose
[(beta-D-Fruf-(2-1))5]-alpha-D-Glup + alpha-D-glucose
-
-
the enzyme selectively produces GF5 from sucose
?
sucrose + sucrose
[(beta-D-Fruf-(2-1))5]-alpha-D-Glup + alpha-D-glucose
-
-
the enzyme selectively produces GF4 from sucose
?
sucrose + sucrose
[(beta-D-Fruf-(2-1))5]-alpha-D-Glup + alpha-D-glucose
-
-
the enzyme selectively produces GF4 from sucose
?
sucrose + sucrose
[(beta-D-Fruf-(2-1))5]-alpha-D-Glup + alpha-D-glucose
-
-
the enzyme selectively produces GF5 from sucose
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
Aspergillus sydowii IAM 2544
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
Bacillus sp. 217C-11
-
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
Limosilactobacillus reuteri TMW1.106
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
Streptococcus mutans JC-1
-
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
Weissella confusa MBFCNC-2(1)
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
glucose + [(2->1)-beta-D-fructosyl]n+1
-
via first transfructosylation product 1-kestose, binding mode, overview, an inulin-type linkage is formed. Particular residues from the nonconserved 1B-1C loop determine product linkage type specificity in GH68 fructansucrases
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
glucose + [(2->1)-beta-D-fructosyl]n+1
-
via first transfructosylation product 1-kestose, binding mode, overview, an inulin-type linkage is formed. Particular residues from the nonconserved 1B-1C loop determine product linkage type specificity in GH68 fructansucrases
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
glucose + [(2->1)-beta-D-fructosyl]n+1
via first transfructosylation product 1-kestose
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
glucose + [(2->1)-beta-D-fructosyl]n+1
via first transfructosylation product 1-kestose
-
-
?
sucrose + [(beta-D-Fruf-(2-1))n]-alpha-D-Glup
alpha-D-glucose + [(beta-D-Fruf-(2-1))n+1]-alpha-D-Glup
-
-
-
-
?
sucrose + [(beta-D-Fruf-(2-1))n]-alpha-D-Glup
alpha-D-glucose + [(beta-D-Fruf-(2-1))n+1]-alpha-D-Glup
-
fructoologosaccharides are synthesized from sucrose at the expense of fructose residues from inulin and related polysaccharides. Fructose residues are transferred from polysaccharide to sucrose molecules, forming a trisaccharide in the first instance. Further fructose residues might then be transferred to the trisaccharide, yielding a tetrasaccharide, and so on. No significant reaction with sucrose alone
-
-
?
sucrose + [(beta-D-Fruf-(2-1))n]-alpha-D-Glup
alpha-D-glucose + [(beta-D-Fruf-(2-1))n+1]-alpha-D-Glup
-
-
-
-
?
sucrose + [(beta-D-Fruf-(2-1))n]-alpha-D-Glup
alpha-D-glucose + [(beta-D-Fruf-(2-1))n+1]-alpha-D-Glup
-
wild-type and recombinant enzyme produce inulin from sucose
-
-
?
sucrose + [(beta-D-Fruf-(2-1))n]-alpha-D-Glup
alpha-D-glucose + [(beta-D-Fruf-(2-1))n+1]-alpha-D-Glup
-
-
-
-
?
sucrose + [(beta-D-Fruf-(2-1))n]-alpha-D-Glup
alpha-D-glucose + [(beta-D-Fruf-(2-1))n+1]-alpha-D-Glup
-
the recombinant truncated enzyme produces both the fructooligosaccharides 1-kestose and nystose and high-molecular-weight-fructan with beta-(2, 1) linkages. The wild-type enzyme only produces 1-kestose, 95%, and nystose, 5%
-
-
?
sucrose + [(beta-D-Fruf-(2-1))n]-alpha-D-Glup
alpha-D-glucose + [(beta-D-Fruf-(2-1))n+1]-alpha-D-Glup
-
-
-
-
?
sucrose + [(beta-D-Fruf-(2-1))n]-alpha-D-Glup
alpha-D-glucose + [(beta-D-Fruf-(2-1))n+1]-alpha-D-Glup
-
the enzyme selectively produces GF5 from sucose
-
-
?
sucrose + [(beta-D-Fruf-(2-1))n]-alpha-D-Glup
alpha-D-glucose + [(beta-D-Fruf-(2-1))n+1]-alpha-D-Glup
-
-
-
-
?
sucrose + [(beta-D-Fruf-(2-1))n]-alpha-D-Glup
alpha-D-glucose + [(beta-D-Fruf-(2-1))n+1]-alpha-D-Glup
-
the enzyme selectively produces GF5 from sucose
-
-
?
sucrose + [(beta-D-Fruf-(2-1))n]-alpha-D-Glup
alpha-D-glucose + [(beta-D-Fruf-(2-1))n+1]-alpha-D-Glup
-
-
-
-
?
sucrose + [(beta-D-Fruf-(2-1))n]-alpha-D-Glup
alpha-D-glucose + [(beta-D-Fruf-(2-1))n+1]-alpha-D-Glup
-
the enzyme selectively produces GF5 from sucose
-
-
?
additional information
?
-
-
the production of fructooligosaccharide by this enzyme is possible only in the presence of sucrose which is an exclusive donor of fructosyl residue in the transferase reaction. The acceptor can be another molecule of sucrose or frucotoligosaccharide
-
-
?
additional information
?
-
enzymatic synthesis of maltosylfructosides derived from sucrose-maltose mixtures by the enzyme from strain DSM 20604, structure analysis, and relation to fructooligosaccharides contents, overview
-
-
?
additional information
?
-
-
enzymatic synthesis of maltosylfructosides derived from sucrose-maltose mixtures by the enzyme from strain DSM 20604, structure analysis, and relation to fructooligosaccharides contents, overview
-
-
?
additional information
?
-
-
sucrose or raffinose act as substrates, both donor and acceptor of fructose moieties. Sucrose is the preferred substrate. The enzyme synthezises fructooligosaccharides from degree of polymerization of 3 (1-kestose) to 9, as well as minor amounts of neo-kestose and inulobiose, product analysis by NMR spectroscopy, overview. Synthezised oligomers are identified as alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranosyl-(1->2)-beta-D-fructofuranosyl-(1->2)-beta-D-fructofuranoside, alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranosyl-(1->2)-beta-D-fructofuranosyl-(1->2)-beta-D-fructofuranosyl-(1->2)-beta-D-fructofuranoside, alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranosyl-(1->2)-beta-D-fructofuranosyl-(1->2)-beta-D-fructofuranosyl-(1->2)-beta-D-fructofuranosyl-(1->2)-beta-D-fructofuranoside, alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranosyl-(1->2)-beta-D-fructofuranosyl-(1->2)-beta-D-fructofuranosyl-(1->2)-beta-D-fructofuranosyl-(1->2)-beta-D-fructofuranosyl-(1->2)-beta-D-fructofuranoside, and alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranosyl-(1->2)-beta-D-fructofuranosyl-(1->2)-beta-D-fructofuranosyl-(1->2)-beta-D-fructofuranosyl-(1->2)-beta-D-fructofuranosyl-(1->2)-beta-D-fructofuranosyl-(1->2)-beta-D-fructofuranoside
-
-
?
additional information
?
-
-
sucrose or raffinose act as substrates, both donor and acceptor of fructose moieties. Sucrose is the preferred substrate. The enzyme synthezises fructooligosaccharides from degree of polymerization of 3 (1-kestose) to 9, as well as minor amounts of neo-kestose and inulobiose, product analysis by NMR spectroscopy, overview. Synthezised oligomers are identified as alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranosyl-(1->2)-beta-D-fructofuranosyl-(1->2)-beta-D-fructofuranoside, alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranosyl-(1->2)-beta-D-fructofuranosyl-(1->2)-beta-D-fructofuranosyl-(1->2)-beta-D-fructofuranoside, alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranosyl-(1->2)-beta-D-fructofuranosyl-(1->2)-beta-D-fructofuranosyl-(1->2)-beta-D-fructofuranosyl-(1->2)-beta-D-fructofuranoside, alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranosyl-(1->2)-beta-D-fructofuranosyl-(1->2)-beta-D-fructofuranosyl-(1->2)-beta-D-fructofuranosyl-(1->2)-beta-D-fructofuranosyl-(1->2)-beta-D-fructofuranoside, and alpha-D-galactopyranosyl-(1->6)-alpha-D-glucopyranosyl-(1->2)-beta-D-fructofuranosyl-(1->2)-beta-D-fructofuranosyl-(1->2)-beta-D-fructofuranosyl-(1->2)-beta-D-fructofuranosyl-(1->2)-beta-D-fructofuranosyl-(1->2)-beta-D-fructofuranoside
-
-
?
additional information
?
-
enzymatic synthesis of maltosylfructosides derived from sucrose-maltose mixtures by the enzyme from strain DSM 20604, structure analysis, and relation to fructooligosaccharides contents, overview
-
-
?
additional information
?
-
-
enzymatic synthesis of maltosylfructosides derived from sucrose-maltose mixtures by the enzyme from strain DSM 20604, structure analysis, and relation to fructooligosaccharides contents, overview
-
-
?
additional information
?
-
-
very low activity in acceptor reactions with non-sugar acceptors, specificity analysis, overview
-
-
?
additional information
?
-
-
the truncated enzyme mutant IslA4 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
?
-
the enzyme is able to catalyse a disproportionation type of reaction with 1-kestose, 1,1-nystose and 1,1,1-kestopentaose
-
-
?
additional information
?
-
-
the enzyme is able to catalyse a disproportionation type of reaction with 1-kestose, 1,1-nystose and 1,1,1-kestopentaose
-
-
?
additional information
?
-
wild-type inulosucrase synthesizes mostly fructooligosaccharides up to a degree of polymerization of 15 and relatively low amounts of inulin polymer
-
-
?
additional information
?
-
-
the enzyme also hydrolyzes sucrose to D-fructose and D-glucose
-
-
-
additional information
?
-
-
the enzyme also hydrolyzes sucrose to D-fructose and D-glucose
-
-
-
additional information
?
-
wild-type inulosucrase synthesizes mostly fructooligosaccharides up to a degree of polymerization of 15 and relatively low amounts of inulin polymer
-
-
?
additional information
?
-
the enzyme is able to catalyse a disproportionation type of reaction with 1-kestose, 1,1-nystose and 1,1,1-kestopentaose
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL 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
3 sucrose + sucrose
3 alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
-
-
-
?
sucrose + [(beta-D-Fruf-(2-1))n]-alpha-D-Glup
alpha-D-glucose + [(beta-D-Fruf-(2-1))n+1]-alpha-D-Glup
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
FTase possesses only transfructosylating activity, acts on sucrose by cleaving the beta-1,2 linkage and transferring the fructosyl group to an acceptor molecule such as sucrose and fructooligosaccharides, releasing D-glucose
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
FTase possesses only transfructosylating activity, acts on sucrose by cleaving the beta-1,2 linkage and transferring the fructosyl group to an acceptor molecule such as sucrose and fructooligosaccharides, releasing D-glucose
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
FTase possesses only transfructosylating activity, acts on sucrose by cleaving the beta-1,2 linkage and transferring the fructosyl group to an acceptor molecule such as sucrose and fructooligosaccharides, releasing D-glucose
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
FTase possesses only transfructosylating activity, acts on sucrose by cleaving the beta-1,2 linkage and transferring the fructosyl group to an acceptor molecule such as sucrose and fructooligosaccharides, releasing D-glucose
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
FTase possesses only transfructosylating activity, acts on sucrose by cleaving the beta-1,2 linkage and transferring the fructosyl group to an acceptor molecule such as sucrose and fructooligosaccharides, releasing D-glucose
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
FTase possesses only transfructosylating activity, acts on sucrose by cleaving the beta-1,2 linkage and transferring the fructosyl group to an acceptor molecule such as sucrose and fructooligosaccharides, releasing D-glucose
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
FTase possesses only transfructosylating activity, acts on sucrose by cleaving the beta-1,2 linkage and transferring the fructosyl group to an acceptor molecule such as sucrose and fructooligosaccharides, releasing D-glucose
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
FTase possesses only transfructosylating activity, acts on sucrose by cleaving the beta-1,2 linkage and transferring the fructosyl group to an acceptor molecule such as sucrose and fructooligosaccharides, releasing D-glucose
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
-
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
-
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
-
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
-
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
FTase possesses only transfructosylating activity, acts on sucrose by cleaving the beta-1,2 linkage and transferring the fructosyl group to an acceptor molecule such as sucrose and fructooligosaccharides, releasing D-glucose
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
FTase possesses only transfructosylating activity, acts on sucrose by cleaving the beta-1,2 linkage and transferring the fructosyl group to an acceptor molecule such as sucrose and fructooligosaccharides, releasing D-glucose
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
FTase possesses only transfructosylating activity, acts on sucrose by cleaving the beta-1,2 linkage and transferring the fructosyl group to an acceptor molecule such as sucrose and fructooligosaccharides, releasing D-glucose
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
FTase possesses only transfructosylating activity, acts on sucrose by cleaving the beta-1,2 linkage and transferring the fructosyl group to an acceptor molecule such as sucrose and fructooligosaccharides, releasing D-glucose
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
FTase possesses only transfructosylating activity, acts on sucrose by cleaving the beta-1,2 linkage and transferring the fructosyl group to an acceptor molecule such as sucrose and fructooligosaccharides, releasing D-glucose
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
alpha-D-glucose + (2,1-beta-D-fructosyl)n+1
-
FTase possesses only transfructosylating activity, acts on sucrose by cleaving the beta-1,2 linkage and transferring the fructosyl group to an acceptor molecule such as sucrose and fructooligosaccharides, releasing D-glucose
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
D-glucose + (2,1-beta-D-fructosyl)n+1
-
-
-
?
sucrose + (2,1-beta-D-fructosyl)n
D-glucose + (2,1-beta-D-fructosyl)n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
Aspergillus sydowii IAM 2544
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
Bacillus sp. 217C-11
-
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
Limosilactobacillus reuteri TMW1.106
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
Streptococcus mutans JC-1
-
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
Weissella confusa MBFCNC-2(1)
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
glucose + [(2->1)-beta-D-fructosyl]n+1
-
-
-
?
sucrose + [(beta-D-Fruf-(2-1))n]-alpha-D-Glup
alpha-D-glucose + [(beta-D-Fruf-(2-1))n+1]-alpha-D-Glup
-
-
-
-
?
sucrose + [(beta-D-Fruf-(2-1))n]-alpha-D-Glup
alpha-D-glucose + [(beta-D-Fruf-(2-1))n+1]-alpha-D-Glup
-
-
-
-
?
sucrose + [(beta-D-Fruf-(2-1))n]-alpha-D-Glup
alpha-D-glucose + [(beta-D-Fruf-(2-1))n+1]-alpha-D-Glup
-
-
-
-
?
sucrose + [(beta-D-Fruf-(2-1))n]-alpha-D-Glup
alpha-D-glucose + [(beta-D-Fruf-(2-1))n+1]-alpha-D-Glup
-
-
-
-
?
sucrose + [(beta-D-Fruf-(2-1))n]-alpha-D-Glup
alpha-D-glucose + [(beta-D-Fruf-(2-1))n+1]-alpha-D-Glup
-
-
-
-
?
sucrose + [(beta-D-Fruf-(2-1))n]-alpha-D-Glup
alpha-D-glucose + [(beta-D-Fruf-(2-1))n+1]-alpha-D-Glup
-
-
-
-
?
additional information
?
-
wild-type inulosucrase synthesizes mostly fructooligosaccharides up to a degree of polymerization of 15 and relatively low amounts of inulin polymer
-
-
?
additional information
?
-
wild-type inulosucrase synthesizes mostly fructooligosaccharides up to a degree of polymerization of 15 and relatively low amounts of inulin polymer
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Fe2+
Mg2+
Mn2+
additional information
Ca2+
sequence contains a putative Ca2+ binding site. Addition of Ca2+ to EDTA-treated protein restores activity
Ca2+
important structural role, Asp520 is important for Ca2+-binding, binding site structure, determination of Ca2+-binding affinity
additional information
no effect by Mg2+, K+, and Na+ at 1 mM
additional information
the enzyme is not affected by Ca2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the enzyme is not inhibited by EDTA
-
EDTA
0.7 mM, 5% residual activity. Addition of Ca2+ restores activity
EDTA
50 microM of EDTA and 5 min of incubation are enough to deplete truncated versions IslA4 and IslA3 of Ca2+ ions and activity, 1000 microM and 180 min are required to achieve the same effect with IslA2. Addition of Ca2+ restores activity
EDTA
40% inhibition at 30-37°C, no inhibition at room temperature, inhibitory effect increases with temperature
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11.4
sucrose
-
hydrolytic activity, measurement of beta-D-fructose, pH 6.5, 30°C
35.2
sucrose
-
overall activity, measurement of alpha-D-glucose, pH 6.5, 30°C
99.2
sucrose
-
transferase activity, measurement of alpha-D-glucose minus D-fructose, pH 6.5, 30°C
additional information
additional information
kinetics at 20°C and 50°C assay temperature
-
additional information
additional information
-
kinetics at 20°C and 50°C assay temperature
-
additional information
additional information
transfructosylation reaction does not obey Michaelis-Menten kinetics
-
additional information
additional information
-
transfructosylation reaction does not obey Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10
sucrose
-
hydrolytic activity, measurement of beta-D-fructose, pH 6.5, 30°C
10
sucrose
recombinant enzyme, hydrolytic reaction, pH 5.4, 20°C
25.5
sucrose
-
hydrolytic activity, measurement of beta-D-fructose, pH 6.5, 30°C
43.6
sucrose
-
overall activity, measurement of alpha-D-glucose, pH 6.5, 30°C
43.6
sucrose
recombinant enzyme, transferase reaction, pH 5.4, 20°C
55.2
sucrose
-
transferase activity, measurement of alpha-D-glucose minus beta-D-fructose, pH 6.5, 30°C
63.5
sucrose
-
transferase activity, measurement of alpha-D-glucose minus beta-D-fructose, pH 6.5, 30°C
76.7
sucrose
-
overall activity, measurement of alpha-D-glucose, pH 6.5, 30°C
88.9
sucrose
recombinant enzyme, hydrolytic reaction, pH 5.4, 50°C
504
sucrose
recombinant enzyme, transferase reaction, pH 5.4, 50°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00032
-
purified recombinant mutant D272N, inulin synthesizing activity
0.00066
-
purified recombinant mutant D424N, inulin synthesizing activity
0.0028
-
purified recombinant mutant E523Q, inulin synthesizing activity
0.3
below, purified recombinant mutant D520A, 50°C, without Ca2+
10.5
purified recombinant truncated His-tagged enzyme, pH 5.2, 55°C
180
purified recombinant wild-type enzyme, 50°C, 1 mM Ca2+
47
-
purified recombinant wild-type enzyme, inulin synthesizing activity
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 5.5
5.2
5.4
5.5
6.5
5.5
optimal pH for sucrose hydrolysis and transfructosylation activities
5.5
free enzyme and enzyme immobilized on core-shell chitosan beads
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 9
-
the optimal pH for the enzyme spans a relatively broad range, from pH 5.0 to 7.0. A relatively substantial amount of activity continues at the pH extremes of pH 4.0 (79.6 %) and pH 9.0 (49.2 %)
6 - 10
the enzyme is active between pH 6.0 and 10.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
30
35
37
45
50
50 - 55
-
the total activity increases until a plateau is reached from 50-55°C. Beyond 55°C the enzyme loses activity rapidly
55
60
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 60
transferase activity: 20% activity at 20°C, 90% activity at 60°C, rapid decrease in activity above 60°C, inactive at 70°C
22 - 55
in presence of Ca2+ at 1 mM: optimal activity at 55°C, in absence of Ca2+ and EDTA: decrease in activity above 45°C, completely inactive at 55°C, overview
40 - 60
the free enzyme shows more than 50% activity between 40 and 60°C. The enzyme is inactive at 70°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Enzyme is a multidomain fructosyltrasferase containing domains from glucosyltransferase
UniProt
brenda
Limosilactobacillus reuteri TMW1.106
isolated from Pozol, a traditional lactic acid fermented beverage of Mayan origin produced from lime treated corn in the south of Mexico
-
-
brenda
Enzyme is a multidomain fructosyltrasferase containing domains from glucosyltransferase
UniProt
brenda
isolated from Pozol, a traditional lactic acid fermented beverage of Mayan origin produced from lime treated corn in the south of Mexico
-
-
brenda
presence of sucrose is without effect on expression of inulosucrase gene
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
the highest enzyme production by both the strains is 3% (w/v) sucrose and 3% (w/v) peptone, or 3.5% (w/v) total sugars present in cane molasses and 1.5% (w/v) yeast powder
brenda
additional information
-
the highest enzyme production by both the strains is 3% (w/v) sucrose and 3% (w/v) peptone, or 3.5% (w/v) total sugars present in cane molasses and 1.5% (w/v) yeast powder
-
brenda
additional information
-
the highest enzyme production by both the strains is 3% (w/v) sucrose and 3% (w/v) peptone, or 3.5% (w/v) total sugars present in cane molasses and 1.5% (w/v) yeast powder
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
additional information
evolution
-
the enzyme belongs to the glycoside hydroylase family GH68
evolution
-
the enzyme belongs to the glycoside hydroylase family GH68
-
malfunction
-
mutation of two of the asparagine residues (N301 and N305) in the 1B-1C loop to serine or alanine significantly decreases the total enzyme activity of InuJ. Deletion of residues 301-303 from this loop even further reduces the activity
malfunction
-
mutation of two of the asparagine residues (N301 and N305) in the 1B-1C loop to serine or alanine significantly decreases the total enzyme activity of InuJ. Deletion of residues 301-303 from this loop even further reduces the activity
-
additional information
-
three-dimensional structure of a truncated active GH68 inulosucrase InuJ of Lactobacillus johnsonii strain NCC533, comprising residues 145-708, in its apo form, with a bound substrate sucrose, and with a transfructosylation product 1-kestose, overview. Particular residues from the nonconserved 1B-1C loop determine product linkage type specificity in GH68 fructansucrases. Residues 210-662 of InuJ constitute the globular catalytic core domain, adopting the five-bladed beta-propeller fold typical of GH68 enzymes. Domain and active site structure analysis, overview
additional information
-
inulosucrase IslA is a multidomain fructosyltransferase
additional information
-
three-dimensional structure of a truncated active GH68 inulosucrase InuJ of Lactobacillus johnsonii strain NCC533, comprising residues 145-708, in its apo form, with a bound substrate sucrose, and with a transfructosylation product 1-kestose, overview. Particular residues from the nonconserved 1B-1C loop determine product linkage type specificity in GH68 fructansucrases. Residues 210-662 of InuJ constitute the globular catalytic core domain, adopting the five-bladed beta-propeller fold typical of GH68 enzymes. Domain and active site structure analysis, overview
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). INUS_LACJO
Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533)
797
1
87186
Swiss-Prot
-
A0A2D1CSM2_SALAG
453
0
50582
TrEMBL
-
A0A650FPJ1_ASPOZ
593
0
64138
TrEMBL
other Location (Reliability: 5)
G2KV82_FRUST
Fructilactobacillus sanfranciscensis (strain TMW 1.1304)
832
1
90348
TrEMBL
-
A0A1B0XB20_ASPAC
654
0
70826
TrEMBL
Secretory Pathway (Reliability: 3)
F1ADK9_ASPJA
654
0
70854
TrEMBL
Secretory Pathway (Reliability: 3)
A0A0X9N9T0_ASPOZ
525
0
57302
TrEMBL
Secretory Pathway (Reliability: 2)
A0A109Y6G5_ASPOZ
525
0
57466
TrEMBL
Secretory Pathway (Reliability: 2)
D0R4Z3_LACJF
Lactobacillus johnsonii (strain FI9785)
720
1
78730
TrEMBL
-
A0A109XBI4_ASPOZ
525
0
57481
TrEMBL
Secretory Pathway (Reliability: 2)
D1MGT1_ASPOZ
525
0
57465
TrEMBL
Secretory Pathway (Reliability: 2)
A0A109XKY3_ASPOZ
525
0
57498
TrEMBL
Secretory Pathway (Reliability: 2)
C7S6G5_ASPOZ
593
0
64270
TrEMBL
other Location (Reliability: 5)
A0A0X9L2L1_ASPOZ
525
0
57437
TrEMBL
Secretory Pathway (Reliability: 2)
D9X8L9_STRVT
Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494)
444
0
49046
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
x * 60000, N- and C-terminally truncated enzyme, SDS-PAGE
additional information
the C-terminal region of IslA is involved in anchoring the enzyme to the cell wall. In addition, besides conferring stability, the C-terminal domain modifies the accessibility to the active site, affecting its catalytic properties
additional information
-
the C-terminal region of IslA is involved in anchoring the enzyme to the cell wall. In addition, besides conferring stability, the C-terminal domain modifies the accessibility to the active site, affecting its catalytic properties
-
additional information
three-dimensional structures of wild-type and mutant enzymes, comparison to the structure of levansucrase, EC 2.4.1.10, overview
additional information
-
three-dimensional structures of wild-type and mutant enzymes, comparison to the structure of levansucrase, EC 2.4.1.10, overview
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His-tagged inulosucrase residues 145-708 fragment, X-ray diffraction structure determination and analysis at 1.75 A resolution, molecular replacement
-
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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
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 10
the enzyme remains stable after 3 h at pH 2.0-10.0. The free and immobilized enzymes retain 80 and 100% activity after 3 h at pH 4.0-8.0, respectively
758340
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
35 - 50
the enzyme shows 50% activity after 420 min at 35°C and is inactive after 30 min at 50°C
40
50
50 - 60
the enzyme maintains 84% activity after incubation at 50°C for 3 h. 44% of the residual activity remains after 1 h at 55°C, and the enzyme loses 50% of its initial activity after incubation at 60°C for 20 min
additional information
35
wild-type, half-life 420 min, truncated versions IslA2, half-life 407 min, IslA3, 346 min, IslA4, 128 min
40
-
half-life of wild-type enzyme: 70 min, half-life of the two C-terminally truncated mutant enzymes is 20 min and 12 min
50
the immobilized enzyme retains about 84% of activity after incubation at 50°C for 12 h, whereas the residual activity of the free enzyme is lower than 50% under the same conditions
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme immobilized on core-shell chitosan beads retains approximately 45% of its initial catalytic activity after being reused for 12 cycles
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, purified recombinant undiluted enzyme, 10% glycerol, completely stable for at least several months
4°C, purified recombinant enzyme, undiluted stable for several days, 10times diluted stable for more than a month
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial
partially purified by Toyopearl DEAE-650M column chromatography
recombinant enzyme
recombinant His-tagged full-length wild-type enzyme and truncated mutant enzyme from Escherichia coli strain BL21 by nickel affinity chromatography and ultrafiltration
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli TOP10 cells by nickel affinity chromatography
recombinant His6-tagged truncated enzyme mutant from Escherichia coli strain DH10B by nickel affinity chromatography
recombinant Myc/His-tagged wild-type and mutant enzymes from Escherichia coli
-
recombinant Myc/His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli and Bacillus subtilis
expressed in Escherichia coli BL21(DE3) cells
expression of His-tagged wild-type and mutant enzymes in Escherichia coli TOP10 cells
expression of Myc/His-tagged wild-type and mutant enzymes in Escherichia coli
expression of the full-length enzyme and two C-terminally truncated enzyme forms in Escherichia coli. Natural chimeric enzyme with three domains: the first and third with high identity with alternansucrase, the second domain, which is the catalytic one has similarity with levansucrase and inulosucrase
-
expression of the full-length protein and a truncated protein with a 100 amino acid truncation at the C-terminus from amino acid 699 onwards, with a C-terminal His-tag, InuDELTA699His
-
gene inuGB, recombinant expression of His6-tagged truncated enzyme mutant lacking the cell-anchoring motif in Escherichia coli strain DH10B
recombinant expression of C-terminally His-tagged fragment of inulosucrase comprising residues 145-708
-
recombinant expression of His-tagged full-length wild-type enzyme and truncated mutant enzyme in Escherichia coli strain BL21
-
recombinant overexpression of the enzyme lacking the cell-anchoring motif in Escherichia coli
-
the N- and C-terminally truncated enzyme is expressed in Saccharomyces cerevisiae strain 2805gs
the truncated mutant IslA4 is expressed in Escherichia coli BL21(DE3) cells
-
expression of Myc/His-tagged wild-type and mutant enzymes in Escherichia coli
-
expression of Myc/His-tagged wild-type and mutant enzymes in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Edelman, J.; Bacon, J.S.D.
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1951
Helianthus tuberosus
brenda
Van Hijum, S.A.F.T.M.; van Geel-Schutten, G.H.; Rahaoui, H.; van der Maarel, M.J.E.C.; Dijkhuizen, L.
Characterization of a novel fructosyltransferase from Lactobacillus reuteri that synthesizes high molecular weight inulin and inulin oligosaccharides
Appl. Environ. Microbiol.
68
4390-4398
2002
Limosilactobacillus reuteri
brenda
Olivares-Illana, V.; Lopez-Munguia, A.; Olvera, C.
Molecular characterization of inulosucrase from Leuconostoc citreum: a fructosyltransferase within a glucosyltransferase
J. Bacteriol.
185
3606-3612
2003
Leuconostoc citreum
brenda
Park, J.P.; Bae, J.T.; Yun, J.W.
Critical effect of ammonium ions on the enzymatic reaction of a novel transfructosylating enzyme for fructooligosaccharide production from sucrose
Biotechnol. Lett.
21
987-990
1999
Paenibacillus macerans, Paenibacillus macerans EG-7
-
brenda
Kim, B.W.; Choin, J.W.; Yun, J.W.
Selective production of GF4-fructosylating enzyme
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20
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1998
Paenibacillus macerans, Paenibacillus macerans EG-6
-
brenda
Ortiz-Soto, M.E.; Olivares-Illana, V.; Lopez-Munguia, A.
Biochemical properties of inulosucrase from Leuconostoc citreum CW28 used for inulin synthesis
Biocatal. Biotransform.
22
275-281
2004
Limosilactobacillus reuteri, Leuconostoc citreum, Leuconostoc citreum CW28, Limosilactobacillus reuteri 121
-
brenda
van Hijum, S.A.; van der Maarel, M.J.; Dijkhuizen, L.
Kinetic properties of an inulosucrase from Lactobacillus reuteri 121
FEBS Lett.
534
207-210
2003
Limosilactobacillus reuteri (Q8GP32), Limosilactobacillus reuteri, Limosilactobacillus reuteri 121 (Q8GP32)
brenda
Ozimek, L.K.; van Hijum, S.A.; van Koningsveld, G.A.; van Der Maarel, M.J.; van Geel-Schutten, G.H.; Dijkhuizen, L.
Site-directed mutagenesis study of the three catalytic residues of the fructosyltransferases of Lactobacillus reuteri 121
FEBS Lett.
560
131-133
2004
Limosilactobacillus reuteri, Limosilactobacillus reuteri 121
brenda
Ozimek, L.K.; Euverink, G.J.; van der Maarel, M.J.; Dijkhuizen, L.
Mutational analysis of the role of calcium ions in the Lactobacillus reuteri strain 121 fructosyltransferase (levansucrase and inulosucrase) enzymes
FEBS Lett.
579
1124-1128
2005
Limosilactobacillus reuteri (Q8GP32), Limosilactobacillus reuteri, Limosilactobacillus reuteri 121 (Q8GP32)
brenda
Ozimek, L.K.; Kralj, S.; Kaper, T.; van der Maarel, M.J.; Dijkhuizen, L.
Single amino acid residue changes in subsite -1 of inulosucrase from Lactobacillus reuteri 121 strongly influence the size of products synthesized
FEBS J.
273
4104-4113
2006
Limosilactobacillus reuteri, Limosilactobacillus reuteri 121
brenda
Dorta, C.; Cruz, R.; de Oliva-Neto, P.; Moura, D.J.
Sugarcane molasses and yeast powder used in the fructooligosaccharides production by Aspergillus japonicus-FCL 119T and Aspergillus niger ATCC 20611
J. Ind. Microbiol. Biotechnol.
33
1003-1009
2006
Aspergillus japonicus, Aspergillus niger, Aspergillus japonicus FCL 119T
brenda
Ozimek, L.K.; Kralj, S.; van der Maarel, M.J.; Dijkhuizen, L.
The levansucrase and inulosucrase enzymes of Lactobacillus reuteri 121 catalyse processive and non-processive transglycosylation reactions
Microbiology
152
1187-1196
2006
Limosilactobacillus reuteri (Q8GP32), Limosilactobacillus reuteri, Limosilactobacillus reuteri 121 (Q8GP32)
brenda
Anwar, M.A.; Kralj, S.; van der Maarel, M.J.; Dijkhuizen, L.
The probiotic Lactobacillus johnsonii NCC 533 produces high-molecular-mass inulin from sucrose by using an inulosucrase enzyme
Appl. Environ. Microbiol.
74
3426-3433
2008
Lactobacillus johnsonii (Q74K42), Lactobacillus johnsonii, Lactobacillus johnsonii NCC 533 (Q74K42), Lactobacillus johnsonii NCC 533
brenda
Del Moral, S.; Olvera, C.; Rodriguez, M.E.; Munguia, A.L.
Functional role of the additional domains in inulosucrase (IslA) from Leuconostoc citreum CW28
BMC Biochem.
9
6-16
2008
Leuconostoc citreum (Q7X481), Leuconostoc citreum CW2 (Q7X481)
brenda
Antosova, M.; Illeova, V.; Vandakova, M.; Druzkovska, A.; Polakovic, M.
Chromatographic separation and kinetic properties of fructosyltransferase from Aureobasidium pullulans
J. Biotechnol.
135
58-63
2008
Aureobasidium pullulans
brenda
Walter, J.; Schwab, C.; Loach, D.M.; Gaenzle, M.G.; Tannock, G.W.
Glucosyltransferase A (GtfA) and inulosucrase (Inu) of Lactobacillus reuteri TMW1.106 contribute to cell aggregation, in vitro biofilm formation, and colonization of the mouse gastrointestinal tract
Microbiology
154
72-80
2008
Limosilactobacillus reuteri, Limosilactobacillus reuteri TMW1.106
brenda
Schwab, C.; Walter, J.; Tannock, G.W.; Vogel, R.F.; Gaenzle, M.G.
Sucrose utilization and impact of sucrose on glycosyltransferase expression in Lactobacillus reuteri
Syst. Appl. Microbiol.
30
433-443
2007
Limosilactobacillus reuteri
brenda
Rodriguez-Alegria, M.; Enciso-Rodriguez, A.; Ortiz-Soto, M.; Cassani, J.; Olvera, C.; Munguia, A.
Fructooligosaccharide production by a truncated Leuconostoc citreum inulosucrase mutant
Biocatal. Biotransform.
28
51-59
2010
Leuconostoc citreum
-
brenda
Maiorano, A.E.; Piccoli, R.M.; da Silva, E.S.; de Andrade Rodrigues, M.F.
Microbial production of fructosyltransferases for synthesis of pre-biotics
Biotechnol. Lett.
30
1867-1877
2008
Aspergillus japonicus, Aspergillus niger, Aspergillus oryzae, Aureobasidium pullulans, Paenibacillus macerans, Thermothelomyces heterothallicus, Penicillium citrinum, Talaromyces purpureogenus, Aureobasidium pullulans KCCM12017, Aspergillus japonicus JN19, Aspergillus oryzae CRF 202, Paenibacillus macerans EG-6, Aureobasidium pullulans CFR77, Penicillium citrinum FERM P-15944
brenda
Salinas, M.A.; Perotti, N.I.
Production of fructosyltransferase by Aureobasidium sp. ATCC 20524 in batch and two-step batch cultures
J. Ind. Microbiol. Biotechnol.
36
39-43
2009
Aureobasidium sp.
brenda
Anwar, M.A.; Leemhuis, H.; Pijning, T.; Kralj, S.; Dijkstra, B.W.; Dijkhuizen, L.
The role of conserved inulosucrase residues in the reaction and product specificity of Lactobacillus reuteri inulosucrase
FEBS J.
279
3612-3621
2012
Limosilactobacillus reuteri (Q8GP32), Limosilactobacillus reuteri 121 (Q8GP32)
brenda
Pijning, T.; Anwar, M.A.; Boeger, M.; Dobruchowska, J.M.; Leemhuis, H.; Kralj, S.; Dijkhuizen, L.; Dijkstra, B.W.
Crystal structure of inulosucrase from Lactobacillus: insights into the substrate specificity and product specificity of GH68 fructansucrases
J. Mol. Biol.
412
80-93
2011
Lactobacillus johnsonii, Lactobacillus johnsonii NCC 533
brenda
Mena-Arizmendi, A.; Alderete, J.; Aguila, S.; Marty, A.; Miranda-Molina, A.; Lopez-Munguia, A.; Castillo, E.
Enzymatic fructosylation of aromatic and aliphatic alcohols by Bacillus subtilis levansucrase: reactivity of acceptors
J. Mol. Catal. B
70
41-48
2011
Leuconostoc citreum
-
brenda
Diez-Municio, M.; de las Rivas, B.; Jimeno, M.L.; Munoz, R.; Moreno, F.J.; Herrero, M.
Enzymatic synthesis and characterization of fructooligosaccharides and novel maltosylfructosides by inulosucrase from Lactobacillus gasseri DSM 20604
Appl. Environ. Microbiol.
79
4129-4140
2013
Lactobacillus gasseri (D3WYV9), Lactobacillus gasseri, Lactobacillus gasseri DSM 20604 (D3WYV9), Lactobacillus gasseri DSM 20604
brenda
Diez-Municio, M.; Herrero, M.; de Las Rivas, B.; Munoz, R.; Jimeno, M.L.; Moreno, F.J.
Synthesis and structural characterization of raffinosyl-oligofructosides upon transfructosylation by Lactobacillus gasseri DSM 20604 inulosucrase
Appl. Microbiol. Biotechnol.
100
6251-6263
2016
Lactobacillus gasseri, Lactobacillus gasseri DSM 20604
brenda
Pena-Cardena, A.; Rodriguez-Alegria, M.E.; Olvera, C.; Munguia, A.L.
Synthesis of fructooligosaccharides by IslA4, a truncated inulosucrase from Leuconostoc citreum
BMC Biotechnol.
15
2-2
2015
Leuconostoc citreum
brenda
Ni, D.; Xu, W.; Zhu, Y.; Zhang, W.; Zhang, T.; Guang, C.; Mu, W.
Inulin and its enzymatic production by inulosucrase Characteristics, structural features, molecular modifications and applications
Biotechnol. Adv.
37
306-318
2019
Lactobacillus gasseri, Lactobacillus gasseri (D3WYV9), Limosilactobacillus reuteri, Limosilactobacillus reuteri (Q0VJC5), Streptococcus mutans, Bacillus sp. 217C-11, Salipaludibacillus agaradhaerens (A0A2D1CSM2), Weissella confusa (D2WS87), Streptomyces viridochromogenes (D9X8L9), Lactobacillus johnsonii (Q74K42), Leuconostoc citreum (Q7X481), Aspergillus sydowii (Q9P853), Weissella confusa MBFCNC-2(1) (D2WS87), Streptococcus mutans JC-1, Streptomyces viridochromogenes DSM 40736 (D9X8L9), Streptococcus mutans JC-2, Salipaludibacillus agaradhaerens WDG185 (A0A2D1CSM2), Lactobacillus johnsonii NCC 533 (Q74K42), Leuconostoc citreum CW28 (Q7X481), Aspergillus sydowii IAM 2544 (Q9P853), Limosilactobacillus reuteri 121, Limosilactobacillus reuteri TMW1.106 (Q0VJC5), Lactobacillus gasseri DSM 20604 (D3WYV9), Lactobacillus gasseri DSM 20243, Streptococcus mutans BHT
brenda
Charoenwongpaiboon, T.; Sitthiyotha, T.; Na Ayutthaya, P.P.; Wangpaiboon, K.; Chunsrivirot, S.; Hengsakul Prousoontorn, M.; Pichyangkura, R.
Modulation of fructooligosaccharide chain length and insight into the product binding motif of Lactobacillus reuteri 121 inulosucrase
Carbohydr. Polym.
209
111-121
2019
Limosilactobacillus reuteri, Limosilactobacillus reuteri 121
brenda
Charoenwongpaiboon, T.; Wangpaiboon, K.; Panpetch, P.; Field, R.A.; Barclay, J.E.; Pichyangkura, R.; Kuttiyawong, K.
Temperature-dependent inulin nanoparticles synthesized by Lactobacillus reuteri 121 inulosucrase and complex formation with flavonoids
Carbohydr. Polym.
223
115044
2019
Limosilactobacillus reuteri, Limosilactobacillus reuteri 121
brenda
Xu, W.; Ni, D.; Zhang, W.; Guang, C.; Zhang, T.; Mu, W.
Recent advances in levansucrase and inulosucrase evolution, characteristics, and application
Crit. Rev. Food Sci. Nutr.
59
3630-3647
2019
Limosilactobacillus reuteri, Limosilactobacillus reuteri (Q0VJC5), Leuconostoc citreum, Lactobacillus gasseri (D3WYV9), Lactobacillus johnsonii (Q74K42), Lactobacillus johnsonii NCC 533 (Q74K42), Leuconostoc citreum CW28, Limosilactobacillus reuteri 121, Limosilactobacillus reuteri TMW1.106 (Q0VJC5), Lactobacillus gasseri DSM 20604 (D3WYV9)
brenda
Ko, H.; Bae, J.H.; Sung, B.H.; Kim, M.J.; Park, H.J.; Sohn, J.H.
Microbial production of medium chain fructooligosaccharides by recombinant yeast secreting bacterial inulosucrase
Enzyme Microb. Technol.
130
109364
2019
Limosilactobacillus reuteri (Q8GP32), Limosilactobacillus reuteri
brenda
Ni, D.; Zhu, Y.; Xu, W.; Bai, Y.; Zhang, T.; Mu, W.
Biosynthesis of inulin from sucrose using inulosucrase from Lactobacillus gasseri DSM 20604
Int. J. Biol. Macromol.
109
1209-1218
2018
Lactobacillus gasseri (D3WYV9), Lactobacillus gasseri DSM 20604 (D3WYV9), Lactobacillus gasseri DSM 20604
brenda
Frasch, H.J.; Leeuwen, S.S.V.; Dijkhuizen, L.
Molecular and biochemical characteristics of the inulosucrase HugO from Streptomyces viridochromogenes DSM40736 (Tue494)
Microbiology
163
1030-1041
2017
Streptomyces viridochromogenes, Streptomyces viridochromogenes DSM 40736
brenda
Charoenwongpaiboon, T.; Wangpaiboon, K.; Pichyangkura, R.; Prousoontorn, M.
Highly porous core-shell chitosan beads with superb immobilization efficiency for Lactobacillus reuteri 121 inulosucrase and production of inulin-type fructooligosaccharides
RSC Adv.
8
17008-17016
2018
Limosilactobacillus reuteri (Q8GP32), Limosilactobacillus reuteri 121 (Q8GP32)
-
brenda
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