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Information on EC 2.4.1.9 - inulosucrase and Organism(s) Lactobacillus johnsonii and UniProt Accession Q74K42

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.9 inulosucrase
IUBMB Comments
Converts sucrose into inulin and D-glucose. Some other sugars can act as D-fructosyl acceptors.
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This record set is specific for:
Lactobacillus johnsonii
UNIPROT: Q74K42
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The taxonomic range for the selected organisms is: Lactobacillus johnsonii
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
ftase, inulosucrase, isase, sucrose 1-fructosyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sucrose: 2,1-beta-D-fructan 1-beta-D-fructosyltransferase
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fructosyltransferase, sucrose 1-
-
-
-
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GH68 fructansucrase
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sucrose 1-fructosyltransferase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
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-
-
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fructosyl group transfer
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-
-
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PATHWAY SOURCE
PATHWAYS
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9030-16-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
sucrose + H2O
alpha-D-glucose + beta-D-fructose
show the reaction diagram
hydrolytic activity, ratio of transglycosylation to hydrolysis activities is almost 1:1 at 37°C but increases about 26fold at 55°C
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-
?
sucrose + sucrose
alpha-D-glucose + inulin-type fructan
show the reaction diagram
-
-
-
?
sucrose + sucrose
alpha-D-glucose + inulin-type oligosaccharide + inulin
show the reaction diagram
-
-
-
?
sucrose + sucrose
[(beta-D-fructose-(2-1))n]-alpha-D-glucose + alpha-D-glucose
show the reaction diagram
transglycosylation activity, ratio of transglycosylation to hydrolysis activities is almost 1:1 at 37°C but increases about 26fold at 55°C
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-
?
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
show the reaction diagram
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
glucose + [(2->1)-beta-D-fructosyl]n+1
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
sucrose + [(2->1)-beta-D-fructosyl]n
alpha-D-glucose + [(2->1)-beta-D-fructosyl]n+1
show the reaction diagram
-
-
-
?
sucrose + [(2->1)-beta-D-fructosyl]n
glucose + [(2->1)-beta-D-fructosyl]n+1
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
required for activity, binding site structure, overview
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
0.7 mM, 5% residual activity. Addition of Ca2+ restores activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
178
hydrolytic activity, 37°C, pH 7.0
187
transglycosylation activity, 37°C, pH 7.0
27
hydrolytic activity, 55°C, pH 7.0
365
total activity, 37°C, pH 7.0
698
transglycosylation activity, 55°C, pH 7.0
719
total activity, 55°C, pH 7.0
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 6
more than 85% of maximum activity
7.5
sharp decrease in activity above
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
sharp decrease in activity above
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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the enzyme belongs to the glycoside hydroylase family GH68
malfunction
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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
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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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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 hide
LITERATURE
N301A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
N301S
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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
additional information
-
deletion of residues 301-303 reduces the enzyme activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expression in Escherichia coli
recombinant expression of C-terminally His-tagged fragment of inulosucrase comprising residues 145-708
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Aspergillus sydowii (Q9P853), Aspergillus sydowii IAM 2544 (Q9P853), Bacillus sp. 217C-11, Lactobacillus gasseri, Lactobacillus gasseri (D3WYV9), Lactobacillus gasseri DSM 20243, Lactobacillus gasseri DSM 20604 (D3WYV9), Lactobacillus johnsonii (Q74K42), Lactobacillus johnsonii NCC 533 (Q74K42), Leuconostoc citreum (Q7X481), Leuconostoc citreum CW28 (Q7X481), Limosilactobacillus reuteri, Limosilactobacillus reuteri (Q0VJC5), Limosilactobacillus reuteri 121, Limosilactobacillus reuteri TMW1.106 (Q0VJC5), Salipaludibacillus agaradhaerens (A0A2D1CSM2), Salipaludibacillus agaradhaerens WDG185 (A0A2D1CSM2), Streptococcus mutans, Streptococcus mutans BHT, Streptococcus mutans JC-1, Streptococcus mutans JC-2, Streptomyces viridochromogenes (D9X8L9), Streptomyces viridochromogenes DSM 40736 (D9X8L9), Weissella confusa (D2WS87), Weissella confusa MBFCNC-2(1) (D2WS87)
Manually annotated by BRENDA team
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
Lactobacillus gasseri (D3WYV9), Lactobacillus gasseri DSM 20604 (D3WYV9), Lactobacillus johnsonii (Q74K42), Lactobacillus johnsonii NCC 533 (Q74K42), Leuconostoc citreum, Leuconostoc citreum CW28, Limosilactobacillus reuteri, Limosilactobacillus reuteri (Q0VJC5), Limosilactobacillus reuteri 121, Limosilactobacillus reuteri TMW1.106 (Q0VJC5)
Manually annotated by BRENDA team