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Information on EC 5.4.99.11 - isomaltulose synthase
for references in articles please use BRENDA:EC5.4.99.11
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EC Tree 5 Isomerases
5.4 Intramolecular transferases
5.4.99 Transferring other groups
5.4.99.11 isomaltulose synthase
IUBMB Comments
The enzyme simultaneously produces isomaltulose (6-O-α-D-glucopyranosyl-D-fructose) and smaller amounts of trehalulose (1-O-α-D-glucopyranosyl-β-D-fructose) from sucrose.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 5.4.99.11
- synthesis
- erwinia
- rhapontici
- palatinose
-
protaminobacter
-
2.4.1.1
- pantoea
-
1,4-alpha-d-glucan:orthophosphate
- molasses
- plymuthica
- food industry
-
vacuole-targeted
- dispersa
- whiteflies
- bemisia
- honeydew
showSynonyms
sucrose isomerase, siase, alpha-glucosyltransferase, isomaltulose synthase, trehalulose synthase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-Glucosyltransferase
-
-
-
-
Avin_08330
AZOG
EC 5.4.99.10
-
-
formerly
-
isomaltulose synthase
Isomaltulose synthetase
-
-
-
-
MutB
NX-5
pal-2
PalI
PdSIase
SIase
SmuA
Sucrose 6-glucosylmutase
-
-
-
-
Sucrose alpha-glucosyltransferase
sucrose isomerase
Sucrose mutase
-
-
-
-
Synthase, isomaltulose
-
-
-
-
Trehalulose synthase
Sucrose alpha-glucosyltransferase
-
-
-
-
Trehalulose synthase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Sucrose = 6-O-alpha-D-glucopyranosyl-D-fructofuranose
intramolecular transglycosylation mechanism in which both glucose and fructose residues appear to be enzyme-bound
-
Sucrose = 6-O-alpha-D-glucopyranosyl-D-fructofuranose
Glu295 plays a role as the general acid catalyst to protonate the oxygen of the glycosidic linkage for substrate hydrolysis, the Odelta2 of Asp241 acts as the nucleophile to attack the C1 of the D-glucosyl and forms a bond with C1 to obtain beta-glucosyl-enzyme intermediate, and the isomaltulose is produced when the O-6 of the hydrolysis product D-fructose nucleophilically binds to the C1 of the D-glucosyl group of the intermediate
-
Sucrose = 6-O-alpha-D-glucopyranosyl-D-fructofuranose
Glu295 plays a role as the general acid catalyst to protonate the oxygen of the glycosidic linkage for substrate hydrolysis, the Odelta2 of Asp241 acts as the nucleophile to attack the C1 of the D-glucosyl and forms a bond with C1 to obtain beta-glucosyl-enzyme intermediate, and the isomaltulose is produced when the O-6 of the hydrolysis product D-fructose nucleophilically binds to the C1 of the D-glucosyl group of the intermediate
-
-
Sucrose = 6-O-alpha-D-glucopyranosyl-D-fructofuranose
Glu295 plays a role as the general acid catalyst to protonate the oxygen of the glycosidic linkage for substrate hydrolysis, the Odelta2 of Asp241 acts as the nucleophile to attack the C1 of the D-glucosyl and forms a bond with C1 to obtain beta-glucosyl-enzyme intermediate, and the isomaltulose is produced when the O-6 of the hydrolysis product D-fructose nucleophilically binds to the C1 of the D-glucosyl group of the intermediate
Serratia plymuthica ATCC 15928
-
-
Sucrose = 6-O-alpha-D-glucopyranosyl-D-fructofuranose
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
isomerization
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
Sucrose glucosylmutase
The enzyme simultaneously produces isomaltulose (6-O-alpha-D-glucopyranosyl-D-fructose) and smaller amounts of trehalulose (1-O-alpha-D-glucopyranosyl-beta-D-fructose) from sucrose.
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CAS REGISTRY NUMBER
COMMENTARY
159940-49-5
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
sucrose
alpha-D-glucopyranosyl-1,6-D-fructofuranose + alpha-D-glucopyranosyl-1,1-D-fructofuranose
sucrose
alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-D-glucoside
?
Substrates: wild-type AZOG and enzyme chimeric mutant AZF3
Products: -
Products: -
?
4-nitrophenyl alpha-D-glucoside
?
Substrates: enzyme chimeric mutant AZF3
Products: -
Products: -
?
isomaltotriose
?
Azotobacter vinelandii DJ / ATCC BAA-1303 / KCTC 12137
Substrates: wild-type AZOG
Products: -
Products: -
?
isomaltulose
sucrose
Substrates: wild-type AZOG and enzyme chimeric mutant AZF3
Products: -
Products: -
r
isomaltulose
sucrose
Azotobacter vinelandii DJ / ATCC BAA-1303 / KCTC 12137
Substrates: wild-type AZOG and enzyme chimeric mutant AZF3
Products: -
Products: -
r
isomaltulose
sucrose
Substrates: enzyme chimeric mutant AZF3
Products: -
Products: -
r
methyl alpha-D-glucoside
?
Substrates: wild-type AZOG
Products: -
Products: -
?
methyl alpha-D-glucoside
?
Azotobacter vinelandii DJ / ATCC BAA-1303 / KCTC 12137
Substrates: wild-type AZOG
Products: -
Products: -
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
Substrates: product specificity of enzyme NX-5 towards isomaltulose and the role of the loop330-339 in NX-5 catalysis
Products: -
Products: -
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
Substrates: product specificity of enzyme NX-5 towards isomaltulose and the role of the loop330-339 in NX-5 catalysis
Products: main product isomaltulose, i.e. alpha-D-glucopyranosyl-1,6-D-fructofuranose or palatinose, and by-product trehalulose, i.e. alpha-D-glucopyranosyl-1,1-D-fructofuranose are two structural isomers of sucrose
Products: main product isomaltulose, i.e. alpha-D-glucopyranosyl-1,6-D-fructofuranose or palatinose, and by-product trehalulose, i.e. alpha-D-glucopyranosyl-1,1-D-fructofuranose are two structural isomers of sucrose
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
Substrates: product specificity of enzyme NX-5 towards isomaltulose and the role of the loop330-339 in NX-5 catalysis
Products: -
Products: -
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
Substrates: product specificity of enzyme NX-5 towards isomaltulose and the role of the loop330-339 in NX-5 catalysis
Products: main product isomaltulose, i.e. alpha-D-glucopyranosyl-1,6-D-fructofuranose or palatinose, and by-product trehalulose, i.e. alpha-D-glucopyranosyl-1,1-D-fructofuranose are two structural isomers of sucrose
Products: main product isomaltulose, i.e. alpha-D-glucopyranosyl-1,6-D-fructofuranose or palatinose, and by-product trehalulose, i.e. alpha-D-glucopyranosyl-1,1-D-fructofuranose are two structural isomers of sucrose
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
Substrates: -
Products: -
Products: -
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
Substrates: the purified sucrose isomerase converts sucrose into 63% of isomaltulose and 30% of trehalulose at pH 6.3 and 33°C. Optimal reaction conditions for the conversion of sucrose into isomaltulose catalyzed by the immobilized sucrose isomerase is at a pH range 6.0-6.5 and 35-40°C
Products: -
Products: -
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
Substrates: production of trehalulose and isomaltulose in a ratio of 64:36
Products: -
Products: -
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
Substrates: production of trehalulose and isomaltulose in a ratio of 64:36 at 40°C. The product ratio depends on the reaction temperature, overview. The amount of trehalulose increases from 47.5% to 79.1% as temperature is lowered from 50°C to 30°C
Products: -
Products: -
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
Substrates: production of trehalulose and isomaltulose in a ratio of 64:36
Products: -
Products: -
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
Substrates: production of trehalulose and isomaltulose in a ratio of 64:36 at 40°C. The product ratio depends on the reaction temperature, overview. The amount of trehalulose increases from 47.5% to 79.1% as temperature is lowered from 50°C to 30°C
Products: -
Products: -
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
Substrates: -
Products: main products
Products: main products
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
Substrates: -
Products: high product specificity for trehalulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose)
Products: high product specificity for trehalulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose)
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
Substrates: -
Products: -
Products: -
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
Substrates: -
Products: -
Products: -
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
Substrates: -
Products: -
Products: -
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
Substrates: activity involves residues D241, E295, H368, and D369
Products: -
Products: -
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
Substrates: -
Products: -
Products: -
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
Substrates: activity involves residues D241, E295, H368, and D369
Products: -
Products: -
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
Substrates: -
Products: -
Products: -
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: wild-type AZOG and enzyme chimeric mutant AZF3
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Azotobacter vinelandii DJ / ATCC BAA-1303 / KCTC 12137
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Azotobacter vinelandii DJ / ATCC BAA-1303 / KCTC 12137
Substrates: wild-type AZOG and enzyme chimeric mutant AZF3
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Bemisia argentifolia
-
Substrates: -
Products: -
Products: -
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: enzyme chimeric mutant AZF3
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: isomaltulose + alpha 1,1-linked disaccharide
Products: isomaltulose + alpha 1,1-linked disaccharide
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: ir
Products: i.e. isomaltulose, i.e. palatinose , formation of isomaltulose and a second alpha-1,1-linked disaccharide, trehalulose, by hydrolysis of sucrose followed by reaction of glucose with the C-6 and C-1 positions of the fructofuranose respectively
Products: i.e. isomaltulose, i.e. palatinose , formation of isomaltulose and a second alpha-1,1-linked disaccharide, trehalulose, by hydrolysis of sucrose followed by reaction of glucose with the C-6 and C-1 positions of the fructofuranose respectively
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: the enzyme is sucrose-specific
Products: i.e. isomaltulose, i.e. palatinose , formation of isomaltulose and a second alpha-1,1-linked disaccharide, trehalulose, by hydrolysis of sucrose followed by reaction of glucose with the C-6 and C-1 positions of the fructofuranose respectively
Products: i.e. isomaltulose, i.e. palatinose , formation of isomaltulose and a second alpha-1,1-linked disaccharide, trehalulose, by hydrolysis of sucrose followed by reaction of glucose with the C-6 and C-1 positions of the fructofuranose respectively
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Erwinia rhapontici wac2928
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Erwinia rhapontici wac2928
-
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
E3DGG4
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Pantoea dispersa UQ68
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: isomaltulose + trehalulose. The ratio of trehalulose to isomaltulose increases at lower reaction temperatures. The optimal conditions for trehalulose production are pH 5.5-6.5 at 20 C
Products: isomaltulose + trehalulose. The ratio of trehalulose to isomaltulose increases at lower reaction temperatures. The optimal conditions for trehalulose production are pH 5.5-6.5 at 20 C
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: isomaltulose + trehalulose. The ratio of trehalulose to isomaltulose increases at lower reaction temperatures. The optimal conditions for trehalulose production are pH 5.5-6.5 at 20 C
Products: isomaltulose + trehalulose. The ratio of trehalulose to isomaltulose increases at lower reaction temperatures. The optimal conditions for trehalulose production are pH 5.5-6.5 at 20 C
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Raoultella planticola CCRC 19112
-
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
VUC84579.1
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Raoultella terrigena NCTC 9189
VUC84579.1
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: i.e. beta-D-glucopyranosyl-D-fructofuranose
Products: isomaltulose + glucose,fructose 1,1'-disaccharide
Products: isomaltulose + glucose,fructose 1,1'-disaccharide
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: isomerization of sucrose to isomaltulose is a highly efficient reaction, the formation of the beta-glucopyranosyl-enzyme complex followed by the nucleophilic attack of the 6'-OH group of fructose is concerted
Products: -
Products: -
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: formation of a hygroscopic by-product, trehalulose, necessitates additional separation to obtain a crystalline 6-O-alpha-D-glucopyranosyl-D-fructofuranose
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Serratia plymuthica ATCC 15928
-
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Serratia plymuthica ATCC 15928
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: isomerization of sucrose to isomaltulose is a highly efficient reaction, the formation of the beta-glucopyranosyl-enzyme complex followed by the nucleophilic attack of the 6'-OH group of fructose is concerted
Products: -
Products: -
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: i.e. beta-D-glucopyranosyl-D-fructofuranose
Products: isomaltulose + glucose,fructose 1,1'-disaccharide
Products: isomaltulose + glucose,fructose 1,1'-disaccharide
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
r
sucrose
alpha-D-glucopyranosyl-1,1-D-fructofuranose
-
Substrates: -
Products: more than 90% conversion of sucrose. Small amounts of trehalulose, glucose, and fructose are produced as by-products
Products: more than 90% conversion of sucrose. Small amounts of trehalulose, glucose, and fructose are produced as by-products
?
sucrose
alpha-D-glucopyranosyl-1,1-D-fructofuranose
-
Substrates: -
Products: more than 90% conversion of sucrose. Small amounts of trehalulose, glucose, and fructose are produced as by-products
Products: more than 90% conversion of sucrose. Small amounts of trehalulose, glucose, and fructose are produced as by-products
?
sucrose
alpha-D-glucopyranosyl-1,1-D-fructofuranose
-
Substrates: -
Products: plus small amounts of glucose, fructose and eventually isomaltose as by-products
Products: plus small amounts of glucose, fructose and eventually isomaltose as by-products
?
sucrose
alpha-D-glucopyranosyl-1,6-D-fructofuranose + alpha-D-glucopyranosyl-1,1-D-fructofuranose
-
Substrates: -
Products: the major product is alpha-D-glucopyranosyl-1,6-D-fructofuranose, small amounts of alpha-D-glucopyranosyl-1,1-D-fructofuranose
Products: the major product is alpha-D-glucopyranosyl-1,6-D-fructofuranose, small amounts of alpha-D-glucopyranosyl-1,1-D-fructofuranose
?
sucrose
alpha-D-glucopyranosyl-1,6-D-fructofuranose + alpha-D-glucopyranosyl-1,1-D-fructofuranose
-
Substrates: -
Products: wild-type enzyme: 82.8% alpha-D-glucopyranosyl-1,6-D-fructofuranose and 12.1% alpha-D-glucopyranosyl-1,1-D-fructofuranose
Products: wild-type enzyme: 82.8% alpha-D-glucopyranosyl-1,6-D-fructofuranose and 12.1% alpha-D-glucopyranosyl-1,1-D-fructofuranose
?
sucrose
alpha-D-glucopyranosyl-1,6-D-fructofuranose + alpha-D-glucopyranosyl-1,1-D-fructofuranose
-
Substrates: two-step reaction mechanism for hydrolysis and isomerization, which occurs in the same pocket
Products: -
Products: -
?
sucrose
alpha-D-glucopyranosyl-1,6-D-fructofuranose + alpha-D-glucopyranosyl-1,1-D-fructofuranose
Substrates: -
Products: ratio of alpha-D-glucopyranosyl-1,6-D-fructofuranose to alpha-D-glucopyranosyl-1,1-D-fructofuranose produced is about 22:1 across pH- and temperature-range. Reaction is fast, conversion of 97% of sucrose in assay within 45 min
Products: ratio of alpha-D-glucopyranosyl-1,6-D-fructofuranose to alpha-D-glucopyranosyl-1,1-D-fructofuranose produced is about 22:1 across pH- and temperature-range. Reaction is fast, conversion of 97% of sucrose in assay within 45 min
ir
sucrose
alpha-D-glucopyranosyl-1,6-D-fructofuranose + alpha-D-glucopyranosyl-1,1-D-fructofuranose
Substrates: -
Products: ratio of alpha-D-glucopyranosyl-1,6-D-fructofuranose to alpha-D-glucopyranosyl-1,1-D-fructofuranose produced is about 22:1 across pH- and temperature-range. Reaction is fast, conversion of 97% of sucrose in assay within 45 min
Products: ratio of alpha-D-glucopyranosyl-1,6-D-fructofuranose to alpha-D-glucopyranosyl-1,1-D-fructofuranose produced is about 22:1 across pH- and temperature-range. Reaction is fast, conversion of 97% of sucrose in assay within 45 min
ir
sucrose
alpha-D-glucopyranosyl-1,6-D-fructofuranose + alpha-D-glucopyranosyl-1,1-D-fructofuranose
Substrates: -
Products: ratio of alpha-D-glucopyranosyl-1,6-D-fructofuranose to alpha-D-glucopyranosyl-1,1-D-fructofuranose produced is about 8:1 across pH- and temperature-range. Enzyme converts 84% of sucrose present in assay within 2 h
Products: ratio of alpha-D-glucopyranosyl-1,6-D-fructofuranose to alpha-D-glucopyranosyl-1,1-D-fructofuranose produced is about 8:1 across pH- and temperature-range. Enzyme converts 84% of sucrose present in assay within 2 h
ir
sucrose
alpha-D-glucopyranosyl-1,6-D-fructofuranose + alpha-D-glucopyranosyl-1,1-D-fructofuranose
Substrates: -
Products: ratio of alpha-D-glucopyranosyl-1,6-D-fructofuranose to alpha-D-glucopyranosyl-1,1-D-fructofuranose produced is about 8:1 across pH- and temperature-range. Enzyme converts 84% of sucrose present in assay within 2 h
Products: ratio of alpha-D-glucopyranosyl-1,6-D-fructofuranose to alpha-D-glucopyranosyl-1,1-D-fructofuranose produced is about 8:1 across pH- and temperature-range. Enzyme converts 84% of sucrose present in assay within 2 h
ir
sucrose
isomaltulose + trehalulose
Substrates: -
Products: the product ratio is 78% isomaltulose and 22% trehalulose
Products: the product ratio is 78% isomaltulose and 22% trehalulose
?
sucrose
isomaltulose + trehalulose + D-glucose
Substrates: MutB catalyzes the isomerization of sucrose to mainly trehalulose (1-O-alpha-D-glucopyranosyl-beta-D-fructose)
Products: -
Products: -
r
sucrose
isomaltulose + trehalulose + D-glucose
Substrates: MutB catalyzes the isomerization of sucrose to mainly trehalulose (1-O-alpha-D-glucopyranosyl-beta-D-fructose)
Products: -
Products: -
r
sucrose
palatinose + trehalulose + D-glucose + D-fructose
-
Substrates: -
Products: at 30°C, 76.8% palatinose, 21.2% trehalulose, 1% each of D-glucose and D-fructose. Percentage of palatinose increases with temperature and reaches a maximum of 79.7% at 40°C
Products: at 30°C, 76.8% palatinose, 21.2% trehalulose, 1% each of D-glucose and D-fructose. Percentage of palatinose increases with temperature and reaches a maximum of 79.7% at 40°C
ir
sucrose
palatinose + trehalulose + D-glucose + D-fructose
-
Substrates: -
Products: at 30°C, 76.8% palatinose, 21.2% trehalulose, 1% each of D-glucose and D-fructose. Percentage of palatinose increases with temperature and reaches a maximum of 79.7% at 40°C
Products: at 30°C, 76.8% palatinose, 21.2% trehalulose, 1% each of D-glucose and D-fructose. Percentage of palatinose increases with temperature and reaches a maximum of 79.7% at 40°C
ir
turanose
?
Substrates: enzyme chimeric mutant AZF3
Products: -
Products: -
?
turanose
?
Substrates: enzyme chimeric mutant AZF3
Products: -
Products: -
?
additional information
?
-
Substrates: gene Avin_08330 encodes the putative sucrose isomerase AZOG in the nitrogen-fixing bacterium Azotobacter vinelandii. The enzyme is a type of pseudo-sucrose isomerase harboring the RLDRD motif, a sucrose isomerase-specific region in 329-333. Neither sucrose isomerization nor hydrolysis activities are observed in recombinant AZOG (rAZOG). The rAZOG shows similar substrate specificity to the enzyme from Bacillus sp. O16G as it catalyzes the hydrolysis of isomaltulose and isomaltose, which contain alpha-1,6-glycosidic linkages. rAZOG generates isomaltose from the small substrate methyl-alpha-glucoside (MaG) via intermolecular transglycosylation. In addition, sucrose isomers isomaltulose and trehalulose are produced when 250 mM fructose is added to the MaG reaction mixture. Enzyme substrate specificity, overview. No activity with trehalose, maltose, nigerose, turanose, and panose. Comparison of substrate specificity with oligo-1,6-glucosidase, EC 3.2.1.10, from Bacillus halodurans strain O16G, UniProt ID BH2903, gene BH2903
Products: -
Products: -
?
additional information
?
-
-
Substrates: gene Avin_08330 encodes the putative sucrose isomerase AZOG in the nitrogen-fixing bacterium Azotobacter vinelandii. The enzyme is a type of pseudo-sucrose isomerase harboring the RLDRD motif, a sucrose isomerase-specific region in 329-333. Neither sucrose isomerization nor hydrolysis activities are observed in recombinant AZOG (rAZOG). The rAZOG shows similar substrate specificity to the enzyme from Bacillus sp. O16G as it catalyzes the hydrolysis of isomaltulose and isomaltose, which contain alpha-1,6-glycosidic linkages. rAZOG generates isomaltose from the small substrate methyl-alpha-glucoside (MaG) via intermolecular transglycosylation. In addition, sucrose isomers isomaltulose and trehalulose are produced when 250 mM fructose is added to the MaG reaction mixture. Enzyme substrate specificity, overview. No activity with trehalose, maltose, nigerose, turanose, and panose. Comparison of substrate specificity with oligo-1,6-glucosidase, EC 3.2.1.10, from Bacillus halodurans strain O16G, UniProt ID BH2903, gene BH2903
Products: -
Products: -
?
additional information
?
-
Bemisia argentifolia
-
Substrates: the enzymic potential for metabolizing sucrose shifts from favoring sucrose hydrolysis at low sucrose concentrations to sucrose isomerization at high sucrose concentrations. Trehalulose is synthesized for excretion when the carbon input from sucrose is in excess of metabolic needs
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme substrate specificity, overview. No activity with methyl alpha-D-glucoside, trehalose, nigerose, maltose, isomaltotriose, and panose, and poor activity with kojibiose and isomaltose. The sucrose is converted into isomaltose, isomatulose and trehalulose, as well as the hydrolysis products glucose and fructose by enzyme mutant AZF3, while wild-type AZOG only produces glucose and fructose
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the isomerization of sucrose (alpha-D-glucosylpyranosyl-1,2-beta-D-fructofuranose) to isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose) as the main product, and trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofuranose) as minor product, and produces glucose and fructose in residual amounts because of sucrose hydrolysis
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the isomerization of sucrose (alpha-D-glucosylpyranosyl-1,2-beta-D-fructofuranose) to isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose) as the main product, and trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofuranose) as minor product, and produces glucose and fructose in residual amounts because of sucrose hydrolysis
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
Products: -
Products: -
?
additional information
?
-
Erwinia rhapontici wac2928
Substrates: the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
Products: -
Products: -
?
additional information
?
-
Erwinia sp. D12
-
Substrates: the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme does not catalyze the formation of any disaccharide from glucose and fructose. No trehalulose is detected when palatinose is the substrate and vice versa
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme does not catalyze the formation of any disaccharide from glucose and fructose. No trehalulose is detected when palatinose is the substrate and vice versa
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
Products: -
Products: -
?
additional information
?
-
Substrates: no apparent reverse reaction producing glucose, fructose, or trehalose, from isomaltulose
Products: -
Products: -
?
additional information
?
-
-
Substrates: no apparent reverse reaction producing glucose, fructose, or trehalose, from isomaltulose
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
Products: -
Products: -
?
additional information
?
-
Substrates: no apparent reverse reaction producing glucose, fructose, or trehalose, from isomaltulose
Products: -
Products: -
?
additional information
?
-
-
Substrates: no apparent reverse reaction producing glucose, fructose, or trehalose, from isomaltulose
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
Products: -
Products: -
?
additional information
?
-
Substrates: the isomaltulose-producing enzyme from Pseudomonas mesoacidophila MX-45 shows the main product trehalulose. It is also named alpha-glucosyltransferase and is renamed trehalulose synthase
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
Products: -
Products: -
?
additional information
?
-
Substrates: the isomaltulose-producing enzyme from Pseudomonas mesoacidophila MX-45 shows the main product trehalulose. It is also named alpha-glucosyltransferase and is renamed trehalulose synthase
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the isomerization of sucrose (alpha-D-glucosylpyranosyl-1,2-beta-D-fructofuranose) to trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofuranose) and isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose) as the main products, and produces glucose and fructose in residual amounts because of sucrose hydrolysis
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the isomerization of sucrose (alpha-D-glucosylpyranosyl-1,2-beta-D-fructofuranose) to trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofuranose) and isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose) as the main products, and produces glucose and fructose in residual amounts because of sucrose hydrolysis
Products: -
Products: -
?
additional information
?
-
Substrates: the isomaltulose-producing enzyme from Pseudomonas mesoacidophila MX-45 shows the main product trehalulose. It is also named alpha-glucosyltransferase and is renamed trehalulose synthase
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the isomerization of sucrose (alpha-D-glucosylpyranosyl-1,2-beta-D-fructofuranose) to trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofuranose) and isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose)
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the isomerization of sucrose (alpha-D-glucosylpyranosyl-1,2-beta-D-fructofuranose) to trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofuranose) and isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose)
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
Products: -
Products: -
?
additional information
?
-
Serratia plymuthica ATCC 15928
-
Substrates: the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the isomerization of sucrose (alpha-D-glucosylpyranosyl-1,2-beta-D-fructofuranose) to trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofuranose) and isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose)
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the enzymatic rearrangement of the alpha-1,2 linkage between glucose and fructose to an alpha-1,6 linkage (producing isomaltulose) or alpha-1,4 linkage (producing trehalulose). In addition, the enzyme hydrolyzes sucrose to produce small amounts of glucose and fructose monosaccharides
Products: -
Products: -
?
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
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
Substrates: product specificity of enzyme NX-5 towards isomaltulose and the role of the loop330-339 in NX-5 catalysis
Products: -
Products: -
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
Substrates: product specificity of enzyme NX-5 towards isomaltulose and the role of the loop330-339 in NX-5 catalysis
Products: -
Products: -
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
Substrates: -
Products: -
Products: -
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
Substrates: production of trehalulose and isomaltulose in a ratio of 64:36
Products: -
Products: -
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
Substrates: production of trehalulose and isomaltulose in a ratio of 64:36
Products: -
Products: -
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
Substrates: -
Products: main products
Products: main products
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
Substrates: -
Products: high product specificity for trehalulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose)
Products: high product specificity for trehalulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose)
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
Substrates: -
Products: -
Products: -
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
Substrates: -
Products: -
Products: -
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
Substrates: -
Products: -
Products: -
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
Substrates: -
Products: -
Products: -
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Azotobacter vinelandii DJ / ATCC BAA-1303 / KCTC 12137
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Erwinia rhapontici wac2928
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Erwinia rhapontici wac2928
-
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
E3DGG4
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Pantoea dispersa UQ68
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Raoultella planticola CCRC 19112
-
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
VUC84579.1
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Raoultella terrigena NCTC 9189
VUC84579.1
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Serratia plymuthica ATCC 15928
-
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Serratia plymuthica ATCC 15928
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Substrates: -
Products: -
Products: -
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
Substrates: -
Products: -
Products: -
r
additional information
?
-
Bemisia argentifolia
-
Substrates: the enzymic potential for metabolizing sucrose shifts from favoring sucrose hydrolysis at low sucrose concentrations to sucrose isomerization at high sucrose concentrations. Trehalulose is synthesized for excretion when the carbon input from sucrose is in excess of metabolic needs
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the isomerization of sucrose (alpha-D-glucosylpyranosyl-1,2-beta-D-fructofuranose) to isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose) as the main product, and trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofuranose) as minor product, and produces glucose and fructose in residual amounts because of sucrose hydrolysis
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the isomerization of sucrose (alpha-D-glucosylpyranosyl-1,2-beta-D-fructofuranose) to isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose) as the main product, and trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofuranose) as minor product, and produces glucose and fructose in residual amounts because of sucrose hydrolysis
Products: -
Products: -
?
additional information
?
-
Substrates: the isomaltulose-producing enzyme from Pseudomonas mesoacidophila MX-45 shows the main product trehalulose. It is also named alpha-glucosyltransferase and is renamed trehalulose synthase
Products: -
Products: -
?
additional information
?
-
Substrates: the isomaltulose-producing enzyme from Pseudomonas mesoacidophila MX-45 shows the main product trehalulose. It is also named alpha-glucosyltransferase and is renamed trehalulose synthase
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the isomerization of sucrose (alpha-D-glucosylpyranosyl-1,2-beta-D-fructofuranose) to trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofuranose) and isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose) as the main products, and produces glucose and fructose in residual amounts because of sucrose hydrolysis
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the isomerization of sucrose (alpha-D-glucosylpyranosyl-1,2-beta-D-fructofuranose) to trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofuranose) and isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose) as the main products, and produces glucose and fructose in residual amounts because of sucrose hydrolysis
Products: -
Products: -
?
additional information
?
-
Substrates: the isomaltulose-producing enzyme from Pseudomonas mesoacidophila MX-45 shows the main product trehalulose. It is also named alpha-glucosyltransferase and is renamed trehalulose synthase
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the isomerization of sucrose (alpha-D-glucosylpyranosyl-1,2-beta-D-fructofuranose) to trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofuranose) and isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose)
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the isomerization of sucrose (alpha-D-glucosylpyranosyl-1,2-beta-D-fructofuranose) to trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofuranose) and isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose)
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the isomerization of sucrose (alpha-D-glucosylpyranosyl-1,2-beta-D-fructofuranose) to trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofuranose) and isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose)
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Mn2+
additional information
Mg2+ and Zn2+ show no significant influence on enzyme activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
castanospermine
-
competitive, crystal structure in complex with enzyme
deoxynojirimycin
-
competitive, crystal structure in complex with enzyme
EDTA
E3DGG4
0.1% (w/v), 8.7% loss of activity of wild-type enzyme, 7.5% loss of activity of mutant enzyme Q209S/R456H
Glutaraldehyde
-
the application of 1 or 2% glutaraldehyde after immobilization of Protaminobacter rubrum in alginate results in the complete destruction of the isomaltulose synthase activity
SDS
E3DGG4
0.1% (w/v), 93% loss of activity of wild-type enzyme, 93.5% loss of activity of mutant enzyme Q209S/R456H
Tris(hydroxymethyl)aminomethane
-
competitive, crystal structure in complex with enzyme
Urea
E3DGG4
0.1% (w/v), 35.2% loss of activity of wild-type enzyme, 32.5% loss of activity of mutant enzyme Q209S/R456H
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NP 40
E3DGG4
0.1% (w/v), activation to 126.5% of control (wild-type enzyme), activation to 159.8% of control (mutant enzyme Q209S/R456H)
sucrose
-
the production of isomaltulose with alginate-immobilized Protaminobacter rubrum at 30 °C is influenced by sucrose concentration. Isomaltulose yields above 90% in 8 h are reached in 40-65% sucrose solutions, and yields up to 82% in 24 h were obtained with 70% sucrose. At higher concentrations (75%) a significant decrease in the isomaltulose yield (42.7-55%) is observed
Triton-X 100
E3DGG4
0.1% (w/v), activation to 107.2% of control (wild-type enzyme), activation to 115.7% of control (mutant enzyme Q209S/R456H)
Tween 20
E3DGG4
0.1% (w/v), activation to 104.2% of control (wild-type enzyme), activation to 108.6% of control (mutant enzyme Q209S/R456H)
Tween 80
E3DGG4
0.1% (w/v), activation to 106.3% of control (wild-type enzyme), activation to 112.3% of control (mutant enzyme Q209S/R456H)
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0192
sucrose
pH not specified in the publication, 20°C, native enzyme
0.03
sucrose
pH and temperature not specified in the publication, recombinant enzyme
0.0324
sucrose
-
pH and temperature not specified in the publication, recombinant enzyme
0.04
sucrose
recombinant enzyme, pH not specified in the publication, 35°C
0.0427
sucrose
recombinant enzyme, pH not specified in the publication, 35°C
0.049
sucrose
pH not specified in the publication, 50°C, recombinant enzyme
0.0546
sucrose
recombinant enzyme, pH not specified in the publication, 35°C
0.076
sucrose
recombinant enzyme, pH not specified in the publication, 35°C
0.2
sucrose
recombinant enzyme, pH not specified in the publication, 30°C
0.222
sucrose
pH not specified in the publication, 30°C, native enzyme
0.257
sucrose
pH not specified in the publication, 30°C, recombinant enzyme
0.28
sucrose
pH not specified in the publication, 30°C, native enzyme
29.32
sucrose
E3DGG4
pH 6.0, temperature not specified in the publication, enzyme immobilized on graphene oxide with addition of surfactant NP40
30.09
sucrose
E3DGG4
pH 6.0, temperature not specified in the publication, enzyme immobilized on graphene oxide
35.51
sucrose
E3DGG4
pH 6.0, temperature not specified in the publication, soluble enzyme
62.9
sucrose
VUC84579.1
pH and temperature not specified in the publication
additional information
additional information
ratio of Kcat/KM-value is 0.000179 per M and s
-
additional information
additional information
-
ratio of Kcat/KM-value is 0.000179 per M and s
-
additional information
additional information
ratio of Kcat/KM-value is 0.000062 per M and s
-
additional information
additional information
-
ratio of Kcat/KM-value is 0.000062 per M and s
-
additional information
additional information
Michaelis-Menten kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
Michaelis-Menten kinetics of wild-type and mutant enzymes, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
730.89
sucrose
E3DGG4
pH 6.0, temperature not specified in the publication, enzyme immobilized on graphene oxide
801.6
sucrose
E3DGG4
pH 6.0, temperature not specified in the publication, enzyme immobilized on graphene oxide with addition of surfactant NP40
804.9
sucrose
E3DGG4
pH 6.0, temperature not specified in the publication, soluble enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.19
sucrose
recombinant enzyme, pH not specified in the publication, 35°C
17.9
sucrose
recombinant enzyme, pH not specified in the publication, 35°C
22.67
sucrose
E3DGG4
pH 6.0, temperature not specified in the publication, soluble enzyme
24.29
sucrose
E3DGG4
pH 6.0, temperature not specified in the publication, enzyme immobilized on graphene oxide
27.34
sucrose
E3DGG4
pH 6.0, temperature not specified in the publication, enzyme immobilized on graphene oxide with addition of surfactant NP40
36
sucrose
pH and temperature not specified in the publication, recombinant enzyme
1301
sucrose
-
pH and temperature not specified in the publication, recombinant enzyme
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.04
0.06
0.22
0.97
recombinant enzyme, pH 6.0, 35°C, substrate methyl alpha-D-glucoside
1.03
1017.6
purified recombinant mutant E175N pH 6.0, 30°C, substrate sucrose
1045.7
purified recombinant mutant K576D, pH 6.0, 30°C, substrate sucrose
1218.9
purified recombinant mutant E175N/K576D, pH 6.0, 30°C, substrate sucrose
13.98
substrate sucrose, pH not specified in the publication, 20°C, native enzyme
2.9
recombinant enzyme, pH 6.0, 35°C, substrate 4-nitrophenyl alpha-D-trehalose
2362
351
423
pH not specified in the publication, 30°C, native enzyme
562
69.53
E3DGG4
enzyme immobilized on macroporous adsorption resin amberliteTM xad1600n, pH 6.0, temperature not specified in the publication
69.84
E3DGG4
enzyme immobilized on macroporous adsorption resin hpd850, pH 6.0, temperature not specified in the publication
718.2
E3DGG4
enzyme immobilized on graphene oxide, pH 6.0, temperature not specified in the publication
83.26
E3DGG4
enzyme immobilized on macroporous adsorption resin H103, pH 6.0, temperature not specified in the publication
900
957.5
additional information
0.04
recombinant mutant AZF3, pH 6.0, 35°C, substrate isomaltulose
0.04
recombinant mutant AZF3, pH 6.0, 35°C, substrate isomaltulose
1.03
recombinant mutant AZF3, pH 6.0, 35°C, substrate 4-nitrophenyl-alpha-D-trehalose
1.03
recombinant mutant AZF3, pH 6.0, 35°C, substrate 4-nitrophenyl alpha-D-trehalose
2362
recombinant enzyme, pH not specified in the publication, 35°C
351
recombinant enzyme, pH not specified in the publication, 35°C
900
substrate sucrose, pH and temperature not specified in the publication, recombinant enzyme
957.5
purified recombinant wild-type enzyme, pH 6.0, 30°C, substrate sucrose
additional information
-
the specific activity of the Protaminobacter rubrum immobilized pellets in calcium alginate at 30°C range from 1.6 to 4.0 g isomaltulose/g pellet/h, respectively with 70% and 65% sucrose solution, while in lower sucrose concentration have higher specific activities presumably due to substrate inhibition of the isomaltulose synthase in higher sucrose concentrations
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
5.8
5.5
soluble enzyme and enzyme immobilized onto polyvinyl alcohol-alginate
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5 - 7
VUC84579.1
pH 3.5: 65.7% of maximal activity, pH 7.0: about 62.9% of maximal activity
3.5 - 7.5
4 - 10
-
the activity diminishes significantly at a pH above 9.0 or below 5.0, and completely inactivates at pH 10.0
4 - 7
4 - 8
-
and above, the immobilized enzyme retains over 50% of its relative activity
4 - 9
4.2 - 7.8
-
pH 4.2: about 30% of maximal activity, pH 7.8: about 50% of maximal activity
4.5 - 7
pH 4.5: about 55% of maximal activity, pH 7.0: about 60% of maximal activity
5 - 8.5
3.5 - 7.5
pH 3.5: about 50% of maximal activity, pH 7.5: about 55% of maximal activity, soluble enzyme
3.5 - 7.5
pH 3.5: about 70% of maximal activity, pH 7.5: about 70% of maximal activity, enzyme immobilized onto polyvinyl alcohol-alginate
4 - 9
89%, 86%, 80%, 34%, and 30% of maximum activity at pH 4.0, pH 6.0, pH 7.0, pH 8.0, and pH 9.0
5 - 8.5
E3DGG4
pH 5.0: about 55% of maximal activity, pH 8.5: about 50% of maximal activity, soluble enzyme
5 - 8.5
E3DGG4
pH 5.0: about 75% of maximal activity, pH 8.5: about 60% of maximal activity, enzyme immobilized on graphene oxide
5 - 8.5
E3DGG4
pH 5.0: about 70% of maximal activity, pH 8.5: about 45% of maximal activity
5 - 8.5
E3DGG4
pH 5.0: about 80% of maximal activity, pH 8.5: about 55% of maximal activity
5 - 8.5
E3DGG4
pH 5.0: about 75% of maximal activity, pH 8.5: about 45% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
30 - 35
35
40
45
50
additional information
-
the ratio of trehalulose to isomaltulose increases at lower temperatures. The optimum for trehalulose production is 20°C
30
-
half-life: 141 min (sucrose isomerase on the cell surface of Yarrowia lipolytica), 62 min (soluble enzyme)
35
soluble enzyme and enzyme immobilized onto polyvinyl alcohol-alginate
45
-
recombinant enzyme displayed on Saccharomyces cerevisiae surface and expressed in Escherichia coli strain DH10B
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 45
20 - 50
20 - 55
20 - 60
-
20°C: about 50% of maximal activity, 40°C: about 40% of maximal activity
25 - 50
E3DGG4
25°C: about 65% of maximal activity, 50°C: about 65% of maximal activity
30 - 50
E3DGG4
30°C: about 60% of maximal activity, 50°C: about 65% of maximal activity, soluble enzyme
30 - 55
E3DGG4
30°C: about 60% of maximal activity, 55°C: about 70 % of maximal activity, enzyme immobilized on graphene oxide
35 - 50
more than 90% of maximal activity occurring at 35°C to 50°C
35 - 60
-
recombinant enzyme displayed on Saccharomyces cerevisiae surface shows higher activity than the enzyme expressed in Escherichia coli strain DH10B
20 - 45
20°C: about 75% of maximal activity, 45°C: about 55% of maximal activity, soluble enzyme
20 - 45
20°C: about 75% of maximal activity, 45°C: about 90% of maximal activity, enzyme immobilized onto polyvinyl alcohol-alginate
20 - 50
-
more than 70% of the initial activity remaining between 20 and 50°C
20 - 50
activity range of recombinant enzyme expressed from Escherichia coli, profile overview
20 - 50
temperature profiles of wild-type and mutant enzymes, overview
20 - 55
E3DGG4
20°C: about 45% of maximal activity, 55°C: about 45% of maximal activity, wild-type enzyme
20 - 55
E3DGG4
20°C: about 40% of maximal activity, 55°C: about 50% of maximal activity, mutant enzyme Q209S/R456H
20 - 55
activity range of recombinant enzyme expressed from Yarrowia lipolytica, profile overview
20 - 55
VUC84579.1
20°C: 53.4% of maximal activity, 55°C: 63.4% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Erwinia rhapontici wac2928
Serratia plymuthica ATCC 15928
i.e. Protaminobacter rubrum CBS 574.77, gene smuA
UniProt
brenda
i.e. Pseudomonas mesoacidophila MX-45, gene mutB
UniProt
brenda
sucrose isomerase SmuA additionally produces alpha-D-glucopyranosyl-1,1-D-fructofuranose from sucrose
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
optimization of enzyme production from native free cells, culture conditions optimization, overview
brenda
additional information
optimization of enzyme production from native free cells, culture conditions optimization, overview
brenda
additional information
optimization of enzyme production from native free cells, culture conditions optimization, overview
brenda
additional information
optimization of enzyme production from native free cells, culture conditions optimization, overview
brenda
additional information
-
optimization of enzyme production from native free cells, culture conditions optimization, overview
-
brenda
additional information
Erwinia sp. D12
-
optimization of enzyme production from native free cells, culture conditions optimization, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to the glycoside hydrolase family 13 (GH13) in the CAZy classification
physiological function
additional information
physiological function
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
physiological function
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
physiological function
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
physiological function
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
physiological function
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
physiological function
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
physiological function
-
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
physiological function
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
physiological function
Erwinia sp. D12
-
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
physiological function
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
physiological function
-
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
-
physiological function
-
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
-
physiological function
-
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
-
physiological function
-
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
-
physiological function
-
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
-
physiological function
-
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
-
physiological function
-
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
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physiological function
Erwinia rhapontici wac2928
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physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
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physiological function
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physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
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physiological function
Serratia plymuthica ATCC 15928
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physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
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additional information
active site structure and substrate and ligand binding structures, overview
additional information
-
active site structure and substrate and ligand binding structures, overview
additional information
enzyme-substrate complex, docking study with sucrose and fructose
additional information
-
enzyme-substrate complex, docking study with sucrose and fructose
additional information
-
structural basis for the product specificity of NX-5, docking of fructofuranose and fructopyranose into the active site of the enzyme mutant D241A-glucose complex, molecular dynamics simulations, molecular mechanism controlling sucrose isomer formation, overview. Phe297 and Phe321 in enzyme NX-5 form an aromatic clamp near the entrance of the active pocket. Residues Asp102, His145, Arg239, His368, Asp369, Glu428, and Arg456 are responsible for sucrose binding and residues Asp241 (the nucleophile) and Glu295 (the acid catalyst) are crucial for sucrose hydrolysis. The active site pocket is stabilized by the salt bridge interactions between Arg239-Asp241, Asp102-Arg456 and Asp369-Arg456. Residues Arg325 and Arg328 are located in the325RLDRD329 motif and play roles in the product specificity
additional information
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the unique RLDRD motif is located in a loop adjacent to the active site cleft and is determined to play an important role in the isomerization process and in the control of product specificity
additional information
proteins AS9 PalI and SmuA differ in only one amino acid, structure of the wild-type sucrose isomerases is obtained by single point mutation through pymol using the crystal structure of SmuA from Protaminobacter rubrum strain CBS 547.77 (PDB ID 3GBD). Homology models of structures of the mutant sucrose isomerases are constructed based on the crystal structure of SmuA, using the EMBL-EBI server
additional information
-
proteins AS9 PalI and SmuA differ in only one amino acid, structure of the wild-type sucrose isomerases is obtained by single point mutation through pymol using the crystal structure of SmuA from Protaminobacter rubrum strain CBS 547.77 (PDB ID 3GBD). Homology models of structures of the mutant sucrose isomerases are constructed based on the crystal structure of SmuA, using the EMBL-EBI server
additional information
-
enzyme-substrate complex, docking study with sucrose and fructose
-
additional information
-
the unique RLDRD motif is located in a loop adjacent to the active site cleft and is determined to play an important role in the isomerization process and in the control of product specificity
-
additional information
-
structural basis for the product specificity of NX-5, docking of fructofuranose and fructopyranose into the active site of the enzyme mutant D241A-glucose complex, molecular dynamics simulations, molecular mechanism controlling sucrose isomer formation, overview. Phe297 and Phe321 in enzyme NX-5 form an aromatic clamp near the entrance of the active pocket. Residues Asp102, His145, Arg239, His368, Asp369, Glu428, and Arg456 are responsible for sucrose binding and residues Asp241 (the nucleophile) and Glu295 (the acid catalyst) are crucial for sucrose hydrolysis. The active site pocket is stabilized by the salt bridge interactions between Arg239-Asp241, Asp102-Arg456 and Asp369-Arg456. Residues Arg325 and Arg328 are located in the325RLDRD329 motif and play roles in the product specificity
-
additional information
-
proteins AS9 PalI and SmuA differ in only one amino acid, structure of the wild-type sucrose isomerases is obtained by single point mutation through pymol using the crystal structure of SmuA from Protaminobacter rubrum strain CBS 547.77 (PDB ID 3GBD). Homology models of structures of the mutant sucrose isomerases are constructed based on the crystal structure of SmuA, using the EMBL-EBI server
-
additional information
Serratia plymuthica ATCC 15928
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the unique RLDRD motif is located in a loop adjacent to the active site cleft and is determined to play an important role in the isomerization process and in the control of product specificity
-
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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). C1DMP8_AZOVD
Azotobacter vinelandii (strain DJ / ATCC BAA-1303)
600
0
68350
TrEMBL
Secretory Pathway (Reliability: 5)
M1E1F3_9HYPH
557
0
63830
TrEMBL
Secretory Pathway (Reliability: 1)
M1E1F6_9HYPH
584
0
66739
TrEMBL
Secretory Pathway (Reliability: 5)
Q2PS28_9BURK
584
0
66792
TrEMBL
-
Q8KR84_9ENTR
598
0
69930
TrEMBL
other Location (Reliability: 2)
Q9AI64_ERWRD
600
0
69866
TrEMBL
Mitochondrion (Reliability: 3)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65000
66000
67000
70000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
x * 65600, native enzyme, x * 66000, recombinant enzyme
?
x * 66000, recombinant enzyme expressed in Yarrowia lipolytica, SDS-PAGE
?
Pantoea dispersa UQ68
-
x * 66000, recombinant enzyme expressed in Yarrowia lipolytica, SDS-PAGE
-
?
x 67560, sequence calculation, x * 65000, recombinant enzyme, SDS-PAGE
?
-
x 67560, sequence calculation, x * 65000, recombinant enzyme, SDS-PAGE
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
sequence contains a periplasm-targeting leader of 33 amino acids
additional information
-
sequence contains a periplasm-targeting leader of 33 amino acids
additional information
-
sequence contains a periplasm-targeting leader of 33 amino acids
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type NX-5 and enzyme mutant complexes E295Q-sucrose and D241A-glucose, sitting drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein solution with 0.001 ml of reservoir solution containing 0.1 M trisodium citrate, pH 5.6, 0.2 M ammonium acetate, and 30% PEG 4000, and for sucrose-complexed mutant enzyme crystal 20 mM sucrose, 0.1 M bicine, pH 9.0, and 30% PEG 6000. The D241A-glucose complex and R335H/R336T/K337I/D338P-glucose complex are co-crystallized in the presence of 20 mM sucrose, 0.1 M sodium cacodylate, pH 6.5, and 29% PEG 8000, 20°C, 3-5 days, X-ray diffraction structure determination and analysis at 1.70 A, 1.70 a, and 2.00 A resolutions, respectively
-
hanging-drop vapor diffusion method, structure solved at 2.2 A resolution
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crystal structure determinations of native enzyme and enzyme mutants D200A and E254Q, PDB IDs 1ZJB, 2PWH, 1ZJA, 2PWD, 2PWG, 2PWF, and 2PWE, interacting compounds are Ca2+, sucrose, D-glucose, tromethamine, Tris, 1-deoxynojirimycin, and castanospermine
wild-type in native state and in complex with competitive inhibitors Tris, deoxynojirimycin, and castanospermine, and inactive mutants D200A, and E254Q, in complex with D-glucose and sucrose
-
purified recombinant enzyme mutants R284C in complex with transition-state mimic deoxynojirimycin, and F164L in complex with glucose, sucrose, trehalulose, or isomaltulose, X-ray diffraction structure determination and analysis at 1.7-2.15 A resolution
crystal structure determinations of enzyme mutants F164L and R284C, PDB IDs 4H2C, 4GIN, 4GI6, 4GI8, 4GIA, and 4GI9, interacting compounds are Ca2+, glycerin, D-glucose, and Tris
crystal structure determination, PDB IDs GBD and GBE, with ethylene glycol, citrate, 1,2-ethanediol, and 1-deoxynojirimycin as interacting compounds
-
in complex with deoxynojirimycin, sitting drop vapor diffusion method, using
native enzyme, crystals belong to space group P212121 and diffract to 1.95 A resolution
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D241A
-
site-directed mutagenesis, glucose binding structure in comparison to the wild-type enzyme by crystal structure analysis
E295Q
-
site-directed mutagenesis, sucrose binding structure in comparison to the wild-type enzyme by crystal structure analysis
F297A
-
site-directed mutagenesis, the mutant shows an altered product ratio of trehalulose and isomaltulose compared to the wild-type enzyme
F321A
-
site-directed mutagenesis, the mutant shows an altered product ratio of trehalulose and isomaltulose compared to the wild-type enzyme
R325D
-
site-directed mutagenesis, the mutant shows an altered product ratio of trehalulose and isomaltulose compared to the wild-type enzyme
R328D
-
site-directed mutagenesis, the mutant shows an altered product ratio of trehalulose and isomaltulose compared to the wild-type enzyme
R335H/R336T/K337I/D338P
-
site-directed mutagenesis, glucose binding structure in comparison to the wild-type enzyme by crystal structure analysis
D241A
-
site-directed mutagenesis, glucose binding structure in comparison to the wild-type enzyme by crystal structure analysis
-
E295Q
-
site-directed mutagenesis, sucrose binding structure in comparison to the wild-type enzyme by crystal structure analysis
-
F297A
-
site-directed mutagenesis, the mutant shows an altered product ratio of trehalulose and isomaltulose compared to the wild-type enzyme
-
R335H/R336T/K337I/D338P
-
site-directed mutagenesis, glucose binding structure in comparison to the wild-type enzyme by crystal structure analysis
-
Q209N
E3DGG4
specific activity is 1.5fold higher than that of the wild-type activity. Kcat/Km is 1.9fold higher than the wild-type value
Q209S
E3DGG4
specific activity is 7.3fold higher than that of the wild-type activity. Kcat/Km is 2.4fold higher than the wild-type value
Q209S/R456H
E3DGG4
specific activity is 17.5fold higher than that of the wild-type activity. Kcat/Km is 16.2fold higher than the wild-type value
R456H
E3DGG4
specific activity is 11.5 fold higher than that of the wild-type activity. Kcat/Km is 6fold higher than the wild-type value. Activity of the mutant enzyme is significantly increased compared with wild type in the presence of 0.1% (w/v) Tween 20, NP 40, Tween 80 and Triton-X 100. NP 40 increases activity of the mutant to 159.8%
R456K
E3DGG4
specific activity is 4.2fold higher than that of the wild-type activity. Kcat/Km is 4.1fold higher than the wild-type value
D327N
-
turnover number for sucrose: 1.4fold decrease, KM-value for sucrose: 1.65fold increase, alpha-D-glucopyranosyl-1,6-D-fructofuranose content: 43.7% decrease, alpha-D-glucopyranosyl-1,1-D-fructofuranose content: 41.0% increase
D327R
-
turnover number for sucrose: 2.45fold decrease, KM-value for sucrose: 2.2fold increase, alpha-D-glucopyranosyl-1,6-D-fructofuranose content: 26.5% decrease, alpha-D-glucopyranosyl-1,1-D-fructofuranose content: 17.7% increase
D329N
-
turnover number for sucrose: 1.17fold decrease, KM-value for sucrose: 2.9fold increase, alpha-D-glucopyranosyl-1,6-D-fructofuranose content: 52.4% decrease, alpha-D-glucopyranosyl-1,1-D-fructofuranose content: 54.7% increase
E498P
-
temperature-optimum is 40°C compared to 35°C for the wild-type enzyme, maximal specific activity increases by 7%. Half-life at 50°C is 9.45 min compared to 1.81 min for wild-type enzyme. Mutation slightly increases the ratio of turnover number to KM-value. Percent content of monosaccharide decreases from 5.9% of the wild-type enzyme to 3.4%
E498P/R310P
-
temperature-optimum is 45°C compared to 35°C for the wild-type enzyme, maximal specific activity increases by 16%. Half-life is 13.61 min compared to 1.81 min for wild-type enzyme. Mutation slightly increases the ratio of turnover number to KM-value. Percent content of monosaccharide decreases from 5.9% of the wild-type enzyme to 3.3%
R325D
-
turnover number for sucrose: 14.5fold decrease, KM-value for sucrose: 1.2fold decrease, alpha-D-glucopyranosyl-1,6-D-fructofuranose content: 67% decrease, alpha-D-glucopyranosyl-1,1-D-fructofuranose content: 43.6% increase
R325L
-
turnover number for sucrose: 14.5fold decrease, KM-value for sucrose: 1.1fold decrease, alpha-D-glucopyranosyl-1,6-D-fructofuranose content: 54.3% decrease, alpha-D-glucopyranosyl-1,1-D-fructofuranose content: 31.3% increase
R328D
-
turnover number for sucrose: 11.9fold decrease, KM-value for sucrose: 2fold increase, alpha-D-glucopyranosyl-1,6-D-fructofuranose content: 65.6% decrease, alpha-D-glucopyranosyl-1,1-D-fructofuranose content: 61.2% increase
R328L
-
turnover number for sucrose: 14.5fold decrease, KM-value for sucrose: 5fold increase, alpha-D-glucopyranosyl-1,6-D-fructofuranose content: 51.9% decrease, alpha-D-glucopyranosyl-1,1-D-fructofuranose content: 50.3% increase
D442N
the mutant favors the transfer reaction with an isomer preference for isomaltulose
R311C
the mutant demonstrates higher catalytic efficiency for D-glucose production over trehalulose production
D442N
-
the mutant favors the transfer reaction with an isomer preference for isomaltulose
-
R311C
-
the mutant demonstrates higher catalytic efficiency for D-glucose production over trehalulose production
-
H287R
VUC84579.1
activity of the mutant enzyme is increased by 11.1%. The isomaltulose conversion rate is improved to 90.7%
H481P
VUC84579.1
activity of the mutant enzyme is increased by 15.2%. The isomaltulose conversion rate is improved to 92.4%
Y246L
VUC84579.1
activity of the mutant enzyme is increased by 27.5%. The isomaltulose conversion rate is improved to 89.1%
Y246L
Raoultella terrigena NCTC 9189
-
activity of the mutant enzyme is increased by 27.5%. The isomaltulose conversion rate is improved to 89.1%
-
F164L
site-directed mutagenesis, three-dimensional structure from crystal structure analysis, comparison to the wild-type. The mutant shows hydrolytic activity converting sucrose to glucose and fructose, kinetics
R284C
site-directed mutagenesis, three-dimensional structure from crystal structure analysis, comparison to the wild-type. The mutant shows hydrolytic activity converting sucrose to glucose and fructose, kinetics. Presence of Mg2+, Ca2+ and Zn2+ ions and glucose have no effect on the activity of the R284C mutant
E175N
site-directed mutagenesis, the mutant shows increased activity and exhibits an identical pH optimum and a slightly increased optimal temperature (35°C) compared to wild-type enzyme (30°C)
E175N/K576
site-directed mutagenesis, the mutant shows increased activity and exhibits an identical pH optimum and a slightly increased optimal temperature (35°C) compared to wild-type enzyme (30°C)
E428D
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
F297A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F297P
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F297P/R333K
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
F321A
site-directed mutagenesis, the mutant shows only hydrolytic activity
F321A/F319A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
G176D
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
K174D
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
K576D
site-directed mutagenesis, the mutant shows increased activity and exhibits an identical pH optimum and a slightly increased optimal temperature (35°C) compared to wild-type enzyme (30°C)
N577K
site-directed mutagenesis, the mutant's activity is similar to the wild-type enzyme
R333K
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S575D
site-directed mutagenesis, the mutant's activity is similar to the wild-type enzyme
V465E
-
mutation boosts the recombinant protein yield to 19.6 mg/l, with an increased proportion of soluble folded protein of 72.5%
Y219L/D398G/V465E
-
the mutant enzyme shows 2.3 times less trehalulose production than the wild-type enzyme but still has high catalytic efficiency (kcat/KM: 11.8 mM/s). This mutant enzyme appears particular promising for industrial use in the biocatalytic preparation of isomaltulose with improved product quality
Y219L/T369F/D398G/F453Y
-
the trehalulose by-product percentage was iteratively decreased from 3.5% to as low as 1.4%. The Tm-value of the mutant enzyme is lower than the wild-type value by 8°C
Y219L/T369F/D398G/F453Y/V465E
-
the mutant enzyme produces only 1.4% trehalulose and shows an isomaltulose/trehalulose ratio of 65.0:1. The progressive reduction in trehalulose yield also correlates with an increased production of glucose and fructose up to 6.6%
E175N
-
site-directed mutagenesis, the mutant shows increased activity and exhibits an identical pH optimum and a slightly increased optimal temperature (35°C) compared to wild-type enzyme (30°C)
-
G176D
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
-
K174D
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type
-
K576D
-
site-directed mutagenesis, the mutant shows increased activity and exhibits an identical pH optimum and a slightly increased optimal temperature (35°C) compared to wild-type enzyme (30°C)
-
S575D
-
site-directed mutagenesis, the mutant's activity is similar to the wild-type enzyme
-
F297A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
F297P
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
F297P/R333K
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
R333K
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
additional information
additional information
construction of chimeric mutant enzymes AZF3 and AZF5 from sucrose isomerase AZOG of Azotobacter vinelanddii and and sucrose isomerase, encoded by esi gene, from Enterobacter sp. FMB-1. Mutant AZF3 has the N-terminal region of Enterobacter SIase and C-terminal region of AZOG, while mutant AZF5 contains the N-terminal region of AZOG and C-terminal region of Enterobacter SIase. Determination of transglycosylation activity, overview. Mutant AZF3 shows altered substrate specificity and reduced activity compared to the wild-type enzyme
additional information
-
construction of chimeric mutant enzymes AZF3 and AZF5 from sucrose isomerase AZOG of Azotobacter vinelanddii and and sucrose isomerase, encoded by esi gene, from Enterobacter sp. FMB-1. Mutant AZF3 has the N-terminal region of Enterobacter SIase and C-terminal region of AZOG, while mutant AZF5 contains the N-terminal region of AZOG and C-terminal region of Enterobacter SIase. Determination of transglycosylation activity, overview. Mutant AZF3 shows altered substrate specificity and reduced activity compared to the wild-type enzyme
additional information
Azotobacter vinelandii DJ / ATCC BAA-1303 / KCTC 12137
-
construction of chimeric mutant enzymes AZF3 and AZF5 from sucrose isomerase AZOG of Azotobacter vinelanddii and and sucrose isomerase, encoded by esi gene, from Enterobacter sp. FMB-1. Mutant AZF3 has the N-terminal region of Enterobacter SIase and C-terminal region of AZOG, while mutant AZF5 contains the N-terminal region of AZOG and C-terminal region of Enterobacter SIase. Determination of transglycosylation activity, overview. Mutant AZF3 shows altered substrate specificity and reduced activity compared to the wild-type enzyme
-
additional information
-
isomaltulose production via yeast surface display of sucrose isomerase from Enterobacter sp. strain FMB-1 on Saccharomyces cerevisiae strain EBY100, stable at a broad range of temperatures (35-55°C) and pHs (pH 5-7) with optimal temperature and pH at 45°C and pH 7.0, respectively
additional information
construction of chimeric mutant enzymes AZF3 and AZF5 from sucrose isomerase SIase from Enterobacter sp. strain FMB-1 and AZOG of Azotobacter vinelanddii. Mutant AZF3 has the N-terminal region of Enterobacter SIase and C-terminal region of AZOG, while mutant AZF5 contains the N-terminal region of AZOG and C-terminal region of Bacillus halodurans SIase. Gene Avin_08330 encodes the putative sucrose isomerase AZOG in the nitrogen-fixing bacterium Azotobacter vinelandii. The enzyme is a type of pseudo-sucrose isomerase harboring the RLDRD motif, a sucrose isomerase-specific region in 329-333. Neither sucrose isomerization nor hydrolysis activities are observed in recombinant AZOG. Determination of transglycosylation activity, overview. Mutant AZF3 shows altered substrate specificity and reduced activity compared to the wild-type enzyme AZOG. The sucrose is converted into isomaltose, isomatulose and trehalulose, as well as the hydrolysis products glucose and fructose by mutant AZF3, while wild-type AZOG only produces glucose and fructose
additional information
immobilization of Escherichia coli strain BL21(DE3) cells recombinantly expressing the enzyme by sodium alginate and CaCl2 solution in untreated cane molasses and corn steep liquor medium for enzyme production and isomaltulose production
additional information
-
mutations of the loop region of enzyme NX-5 result in significant changes of the product ratio between isomaltulose and trehalulose
additional information
-
immobilization of cells expressing the recombinant wild-type enzyme, and mutant BN 68069 cells, on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
additional information
immobilization of cells expressing the recombinant wild-type enzyme, and mutant BN 68069 cells, on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
additional information
immobilization of cells expressing the recombinant wild-type enzyme, and mutant BN 68069 cells, on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
additional information
immobilization of cells expressing the recombinant wild-type enzyme, and mutant BN 68069 cells, on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
additional information
-
bioinspired production of antibacterial sucrose isomerase-sponge for the synthesis of isomaltulose, enzyme immobilization, method development, optimization, and evaluation, overview. The enzyme is immobilized on a epsilon-poly-L-lysine (epsilons-PL)-gelatin sponge as matrix is produced by the lyophilizing method, using water as a porogen. The carboxyl groups of gelatin are activated by 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide (EDC) and N-hydroxysuccinimide (NHS) to form reactive NHS esters, which can promote the rate of the synthesis reaction to form a stable amide bond. Then the esters react with amine groups of epsilon-PL to form peptide bonds. Through a series of cross-linking reactions, gelatin and epsilon-PL form a sponge. The affinity of immobilized enzyme SIase to substrate is basically unchanged. Immobilized SIase still exhibits more than 90% sucrose conversion after 13 consecutive cycles, which indicates that it has a good operational stability. Furthermore, the immobilized SIase has the potential for isomaltulose production, with 200 g/l sucrose solution as its substrate in the food industry. Isomaltulose is isolated in 83.58% yield and high purity (97.3%). epsilon-Poly-L-lysine (epsilon-PL), is an ideal carrier for enzyme immobilization and has attracted considerable attention because of its good biocompatibility, antimicrobial activity, and non-toxic characteristic. The loose and porous structures of epsilon-PL-gelatin sponge are critical for ensuring relatively high catalytic efficiency
additional information
-
immobilization of cells expressing the wild-type enzyme on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
additional information
immobilization of cells expressing the wild-type enzyme on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
additional information
immobilization of cells expressing the wild-type enzyme on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
additional information
immobilization of cells expressing the wild-type enzyme on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
additional information
-
immobilization of cells expressing the recombinant wild-type enzyme, and mutant BN 68069 cells, on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
-
additional information
-
immobilization of Escherichia coli strain BL21(DE3) cells recombinantly expressing the enzyme by sodium alginate and CaCl2 solution in untreated cane molasses and corn steep liquor medium for enzyme production and isomaltulose production
-
additional information
-
mutations of the loop region of enzyme NX-5 result in significant changes of the product ratio between isomaltulose and trehalulose
-
additional information
-
immobilization of cells expressing the wild-type enzyme on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
-
additional information
-
bioinspired production of antibacterial sucrose isomerase-sponge for the synthesis of isomaltulose, enzyme immobilization, method development, optimization, and evaluation, overview. The enzyme is immobilized on a epsilon-poly-L-lysine (epsilons-PL)-gelatin sponge as matrix is produced by the lyophilizing method, using water as a porogen. The carboxyl groups of gelatin are activated by 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide (EDC) and N-hydroxysuccinimide (NHS) to form reactive NHS esters, which can promote the rate of the synthesis reaction to form a stable amide bond. Then the esters react with amine groups of epsilon-PL to form peptide bonds. Through a series of cross-linking reactions, gelatin and epsilon-PL form a sponge. The affinity of immobilized enzyme SIase to substrate is basically unchanged. Immobilized SIase still exhibits more than 90% sucrose conversion after 13 consecutive cycles, which indicates that it has a good operational stability. Furthermore, the immobilized SIase has the potential for isomaltulose production, with 200 g/l sucrose solution as its substrate in the food industry. Isomaltulose is isolated in 83.58% yield and high purity (97.3%). epsilon-Poly-L-lysine (epsilon-PL), is an ideal carrier for enzyme immobilization and has attracted considerable attention because of its good biocompatibility, antimicrobial activity, and non-toxic characteristic. The loose and porous structures of epsilon-PL-gelatin sponge are critical for ensuring relatively high catalytic efficiency
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additional information
-
enzyme immobilization by adsorption on a chromatographic resin, optimal reaction conditions for the conversion of sucrose into isomaltulose catalyzed by the immobilized sucrose isomerase is at a pH range 6.0-6.5 and 35-40°C
additional information
Erwinia sp. D12
-
immobilization of cells expressing the wild-type enzyme on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
additional information
cloning of the PdSIase gene into the expression vector pET28a, functional recombinant expression in Yarrowia lipolytica strain CGMCC7326 on the cell surface using the cell wall protein Pir1 as an anchor protein. Selection via a hygromycin B resistance gene as a selection marker, method, overview
additional information
Pantoea dispersa UQ68
-
cloning of the PdSIase gene into the expression vector pET28a, functional recombinant expression in Yarrowia lipolytica strain CGMCC7326 on the cell surface using the cell wall protein Pir1 as an anchor protein. Selection via a hygromycin B resistance gene as a selection marker, method, overview
-
additional information
engineering of the enzyme to exhibit isomelezitose synthase activity for production of the probiotically nutrial component, overview
additional information
-
engineering of the enzyme to exhibit isomelezitose synthase activity for production of the probiotically nutrial component, overview
additional information
-
immobilization of cells expressing the recombinant wild-type enzyme on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
additional information
the half-lives of the enzyme mutants E175N, K576D and E175N/K576D are 2.30, 1.78 and 7.65 times greater than that of the wild-type enzyme at 45°C, respectively. The Km values for the E175N, K576D and E175N/K576D mutants decrease by 6.6%, 2.0% and 11.0%, respectively, and their kcat/Km values increase by 38.2%, 4.2% and 19.4%, respectively, compared with those of the wild-type enzyme. After optimizing the conditions for isomaltulose production at 45°C, the E175N, K576D and E175N/K576D mutants display slightly improved isomaltulose yields, compared with the wild-type enzyme. The catalytic efficiencies (kcat/Km values) of E175N, K576D and E175N/K576D are increased by 38.2%, 4.2% and 19.4%, respectively
additional information
-
the half-lives of the enzyme mutants E175N, K576D and E175N/K576D are 2.30, 1.78 and 7.65 times greater than that of the wild-type enzyme at 45°C, respectively. The Km values for the E175N, K576D and E175N/K576D mutants decrease by 6.6%, 2.0% and 11.0%, respectively, and their kcat/Km values increase by 38.2%, 4.2% and 19.4%, respectively, compared with those of the wild-type enzyme. After optimizing the conditions for isomaltulose production at 45°C, the E175N, K576D and E175N/K576D mutants display slightly improved isomaltulose yields, compared with the wild-type enzyme. The catalytic efficiencies (kcat/Km values) of E175N, K576D and E175N/K576D are increased by 38.2%, 4.2% and 19.4%, respectively
additional information
-
immobilization of cells expressing the wild-type enzyme on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
additional information
Serratia plymuthica ATCC 15928
-
immobilization of cells expressing the recombinant wild-type enzyme on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
-
additional information
Serratia plymuthica ATCC 15928
-
immobilization of cells expressing the wild-type enzyme on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
-
additional information
-
engineering of the enzyme to exhibit isomelezitose synthase activity for production of the probiotically nutrial component, overview
-
additional information
-
immobilization of cells expressing the recombinant wild-type enzyme on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
-
additional information
-
immobilization of cells expressing the wild-type enzyme on alginate cell pellets for isomaltulose production, overview. The operational stability and enzyme half-life are significantly improved
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 8
4.5 - 7
the yeast strain displaying recombinant enzyme PdSIase is stable throughout relatively broad ranges of pH values and temperatures
4.5 - 8
5 - 6
the enzymatic activity is significantly lower outside the optimal pH range of 5.0-6.0 implying that the enzyme is very sensitive to pH
5 - 7
5 - 7.5
-
the free enzyme retains more than 80% of its relative activity at pH 5.0-7.5
5.5
6.5
4 - 8
E3DGG4
40°C, 30 min, enzyme immobilized on graphene oxide retains more thah 75% of its initial activity
4 - 8
E3DGG4
40°C, 30 min, soluble enzyme retains more then 60% of its initial activity
4.5 - 8
-
the immobilized enzyme retains more than 80% of its relative activity at pH 4.5-8.0
4.5 - 8
24 h, the enzyme retains more than 90% of its maximal activity
5 - 7
-
recombinant enzyme displayed on Saccharomyces cerevisiae surface, stable at
5 - 7
-
the enzyme retains more than 60% of its original activity over a range of pH 5.0-7.0 at 30°C for 24 h
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
20 - 70
about 50% activity at 20°C, about 80% activity at 30°C, 100% activity at 40-50°C, about 20% activity at 55°C, complete loss of activity at 60-70°C
22
25 - 35
E3DGG4
pH 6.0, 1 h, enzyme retains about 95% of its initial activity
30
30 - 60
the enzyme is stable for longer than 48 h at 30°C. The stability of the enzyme decreases drastically at 50°C and 60°C with a half-life duration of 90 min and 5 min, respectively
35 - 50
30 min, the enzyme retains more than 95% of its maximal activity
35 - 55
-
recombinant enzyme displayed on Saccharomyces cerevisiae surface, stable at, half-life at 50°C is 2.4 h
40
45
50
52
50% activity remaining of recombinant enzyme expressed from Escherichia coli, inactivation at 65°C, profile overview
60
20
pH 6.0, 4 h, enzyme retains 90% of its initial activity, soluble enzyme
20
pH 6.0, 4 h, enzyme retains 100% of its initial activity, enzyme immobilized onto polyvinyl alcohol-alginate
30
pH 6.0, 4 h, enzyme retains 80% of its initial activity, soluble enzyme
30
pH 6.0, 4 h, enzyme retains 90% of its initial activity, enzyme immobilized onto polyvinyl alcohol-alginate
40
E3DGG4
30 min, soluble enzyme retains about 75% of its initial activity
40
E3DGG4
30 min, enzyme immobilized on graphene oxide retains about 85% of its initial activity
40
pH 6.0, 4 h, enzyme retains 70% of its initial activity, soluble enzyme
40
pH 6.0, 4 h, enzyme retains 85% of its initial activity, enzyme immobilized onto polyvinyl alcohol-alginate
40
-
half-life: 141 min (sucrose isomerase on the cell surface of Yarrowia lipolytica), 62 min (soluble enzyme)
45
E3DGG4
30 min, soluble enzyme retains about 50% of its initial activity
45
E3DGG4
30 min, enzyme immobilized on graphene oxide retains about 60% of its initial activity
45
pH 6.0, 4 h, enzyme retains 35% of its initial activity, soluble enzyme
45
pH 6.0, 4 h, enzyme retains 70% of its initial activity, enzyme immobilized onto polyvinyl alcohol-alginate
45
at 45°C and pH 6.0, the half-life of wild-type enzyme is 39.2 minutes. Whereas, the half-lives of mutants E175N, K576D, and E175N/K576D are 90.2 minutes, 69.8 minutes, and 300 minutes, respectively, which are 2.30, 1.78 and 7.65 times greater than that of the wild-type enzyme
50
-
half-life of wild-type enzyme: 1.81 min, half-life of mutant enzymes E498P is 9.45 min, half-life of mutant enzyme E498P/R310P is 13.61 min
50
pH 6.0, 4 h, enzyme retains 20% of its initial activity, soluble enzyme
50
pH 6.0, 4 h, enzyme retains 55% of its initial activity, enzyme immobilized onto polyvinyl alcohol-alginate
60
about 50% activity remaining of recombinant enzyme expressed from Yarrowia lipolytica, inactivation at 70°C, profile overview
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the isomaltulose synthase immobilized only with alginate remains stable for eight 24 h batch cycles or 192 h total time
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 50% glycerol, stable for at least 6 months
22C, 50% glycerol, 60% residual activity after 15 days
30°C, purified enzyme in 25 mM PBS (pH 5.8), 2 weeks, 35% loss of activity
-
4°C, 45 days, remaining activity of this the enzyme immobilized on graphene oxide is 91.76%, the remaining activity of the soluble enzyme is 84.73%
E3DGG4
4°C, purified enzyme in 25 mM PBS (pH 5.8), 2 weeks, 23% loss of activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE-Sepharose column chromatography, SP-Sepharose column chromatography, and Sephacryl S-300 gel filtration
-
recombinant enzyme from Escherichia coli strain BL21(DE3)
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatograhy and gel filtration
-
recombinant His6-tagged enzyme from Escherichia coli by nickle affinity chromatography and gel filtration
recombinant protein
recombinant wild-type enzyme and mutants E175N, K576D, and E175N/K576D from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation, dialysis, and cation exchange chromatography, to homogeneity
using subsequently a Sephadex G-25, a DEAE-cellulose and a Sephadex G-75 column
-
recombinant enzyme from Escherichia coli strain BL21(DE3)
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning and expression in Escherichia coli strain DH10B, expression on cell surface of Saccharomyces cerevisiae strain FMB-1
-
cloning of the PdSIase gene into the expression vector pET28a, functional recombinant expression in Yarrowia lipolytica strain CGMCC7326 on the cell surface using the cell wall protein Pir1 as an anchor protein, and recombinant expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
DNA and amino acid sequence determination and analysis, sequence comparisons, functional expression of His6-tagged enzyme in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in sugarcane (Saccharum sp.) cultivar Q117 embryogenic callus
expression in Escherichia coli
expression in Escherichia coli BL21(DE3)
expression in Escherichia coli, with His-tag
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
gene Avin_08330, sequence comparisons and phylogenetic tree, recombinant expression of wild-type AZOG enzyme and chimeric mutants AZF3 and AZF5 in Escherichia coli strain BL21(DE3)
gene esi, sequence comparisons and phylogenetic tree, recombinant expression chimeric mutants AZF3 and AZF5 in Escherichia coli strain BL21(DE3)
gene mutB, DNA and amino acid sequence determination and analysis, phylogenetic analysis, cloning and expression of wild-type and insertional disruption mutant in Escherichia coli strain BL21 (DE3)
gene smuA, DNA and amino acid sequence determination and analysis, phylogenetic analysis, cloning of full-length gene including the periplasmic signal sequence and expression of wild-type and insertional disruption mutant in Escherichia coli strain BL21 (DE3)
gene smuA, sequence comparison, expression of wild-type and mutant enzymes
gene smuA, synthetic gene, sequence comparisons, recombinant expression of codon-optimized wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain JM109
high-level extracellular production of a sucrose isomerase from Klebsiella sp.LX3 in Bacillus subtilis is achieved by optimizing the signal peptides. The signal peptide WapA has the highest secretion efficiency for KsLX3-SIase and resulted in an activity level of 23.0 U/ml in the culture medium
in order to anchor pSIase to the cell surface, the gene encoding sucrose isomerase from Pantoea dispersa is fused with the vector pINA1317-CWP110. The constructed pINA1317-CWP110-pSIase is transfered into Yarrowia lipolytica
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recombinant enzyme expression
recombinant enzyme expression from tac vector
recombinant enzyme expression, Protaminobacter sucrose isomerase is totally susceptible to inactivation and cannot be solubly expressed with a tac vector either but may fold correctly and is effectively expressed from the L-rhamnose-inducible vector
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recombinant expression in Escherichia coli strain BL21(DE3) periplasmic space using vector pET22b-palI, usage of untreated cane molasses and corn steep liquor for Escherichia coli fermentation
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
food industry
industry
synthesis
additional information
food industry
-
isomaltulose is widely used as sucrose substitute in diet and diabetes products
food industry
sucrose isomerase activity is used industrially for the conversion of sucrose into isomers, particularly isomaltulose or trehalulose, which have properties advantageous over sucrose for some food uses. The industrial potential may be further enhanced by selection for variants that do not catabolize the sucrose substrate
food industry
sucrose isomerase activity is used industrially for the conversion of sucrose into isomers, particularly isomaltulose or trehalulose, which have properties advantageous over sucrose for some food uses.The industrial potential may be further enhanced by selection for variants that do not catabolize the sucrose substrate
food industry
-
biological isomaltulose production from sucrose catalyzed by sucrose isomerase. Isomaltulose is a safe sucrose substitute, that is widely used as a functional sweetener due to its promising properties, such as slower digestion, prolonged energy release, and less cariogenicity. Sucrose isomerase is responsible for the commercial biological production of isomaltulose from sucrose. Some problems exist in industrial production, such as the low secretion level from food safety grade strain, weak thermal stability, and poor application performance of the enzyme
food industry
biological isomaltulose production from sucrose catalyzed by sucrose isomerase. Isomaltulose is a safe sucrose substitute, that is widely used as a functional sweetener due to its promising properties, such as slower digestion, prolonged energy release, and less cariogenicity. Sucrose isomerase is responsible for the commercial biological production of isomaltulose from sucrose. Some problems exist in industrial production, such as the low secretion level from food safety grade strain, weak thermal stability, and poor application performance of the enzyme
food industry
-
biological isomaltulose production from sucrose catalyzed by sucrose isomerase. Isomaltulose is a safe sucrose substitute, that is widely used as a functional sweetener due to its promising properties, such as slower digestion, prolonged energy release, and less cariogenicity. Sucrose isomerase is responsible for the commercial biological production of isomaltulose from sucrose. Some problems exist in industrial production, such as the low secretion level from food safety grade strain, weak thermal stability, and poor application performance of the enzyme
food industry
biological isomaltulose production from sucrose catalyzed by sucrose isomerase. Isomaltulose is a safe sucrose substitute, that is widely used as a functional sweetener due to its promising properties, such as slower digestion, prolonged energy release, and less cariogenicity. Sucrose isomerase is responsible for the commercial biological production of isomaltulose from sucrose. Some problems exist in industrial production, such as the low secretion level from food safety grade strain, weak thermal stability, and poor application performance of the enzyme
food industry
biological isomaltulose production from sucrose catalyzed by sucrose isomerase. Isomaltulose is a safe sucrose substitute, that is widely used as a functional sweetener due to its promising properties, such as slower digestion, prolonged energy release, and less cariogenicity. Sucrose isomerase is responsible for the commercial biological production of isomaltulose from sucrose. Some problems exist in industrial production, such as the low secretion level from food safety grade strain, weak thermal stability, and poor application performance of the enzyme
food industry
-
biological isomaltulose production from sucrose catalyzed by sucrose isomerase. Isomaltulose is a safe sucrose substitute, that is widely used as a functional sweetener due to its promising properties, such as slower digestion, prolonged energy release, and less cariogenicity. Sucrose isomerase is responsible for the commercial biological production of isomaltulose from sucrose. Some problems exist in industrial production, such as the low secretion level from food safety grade strain, weak thermal stability, and poor application performance of the enzyme
food industry
biological isomaltulose production from sucrose catalyzed by sucrose isomerase. Isomaltulose is a safe sucrose substitute, that is widely used as a functional sweetener due to its promising properties, such as slower digestion, prolonged energy release, and less cariogenicity. Sucrose isomerase is responsible for the commercial biological production of isomaltulose from sucrose. Some problems exist in industrial production, such as the low secretion level from food safety grade strain, weak thermal stability, and poor application performance of the enzyme
food industry
-
biological isomaltulose production from sucrose catalyzed by sucrose isomerase. Isomaltulose is a safe sucrose substitute, that is widely used as a functional sweetener due to its promising properties, such as slower digestion, prolonged energy release, and less cariogenicity. Sucrose isomerase is responsible for the commercial biological production of isomaltulose from sucrose. Some problems exist in industrial production, such as the low secretion level from food safety grade strain, weak thermal stability, and poor application performance of the enzyme
food industry
biological isomaltulose production from sucrose catalyzed by sucrose isomerase. Isomaltulose is a safe sucrose substitute, that is widely used as a functional sweetener due to its promising properties, such as slower digestion, prolonged energy release, and less cariogenicity. Sucrose isomerase is responsible for the commercial biological production of isomaltulose from sucrose. Some problems exist in industrial production, such as the low secretion level from food safety grade strain, weak thermal stability, and poor application performance of the enzyme
food industry
-
biological isomaltulose production from sucrose catalyzed by sucrose isomerase. Isomaltulose is a safe sucrose substitute, that is widely used as a functional sweetener due to its promising properties, such as slower digestion, prolonged energy release, and less cariogenicity. Sucrose isomerase is responsible for the commercial biological production of isomaltulose from sucrose. Some problems exist in industrial production, such as the low secretion level from food safety grade strain, weak thermal stability, and poor application performance of the enzyme
-
food industry
-
biological isomaltulose production from sucrose catalyzed by sucrose isomerase. Isomaltulose is a safe sucrose substitute, that is widely used as a functional sweetener due to its promising properties, such as slower digestion, prolonged energy release, and less cariogenicity. Sucrose isomerase is responsible for the commercial biological production of isomaltulose from sucrose. Some problems exist in industrial production, such as the low secretion level from food safety grade strain, weak thermal stability, and poor application performance of the enzyme
-
food industry
-
sucrose isomerase activity is used industrially for the conversion of sucrose into isomers, particularly isomaltulose or trehalulose, which have properties advantageous over sucrose for some food uses.The industrial potential may be further enhanced by selection for variants that do not catabolize the sucrose substrate
-
food industry
Erwinia rhapontici wac2928
-
biological isomaltulose production from sucrose catalyzed by sucrose isomerase. Isomaltulose is a safe sucrose substitute, that is widely used as a functional sweetener due to its promising properties, such as slower digestion, prolonged energy release, and less cariogenicity. Sucrose isomerase is responsible for the commercial biological production of isomaltulose from sucrose. Some problems exist in industrial production, such as the low secretion level from food safety grade strain, weak thermal stability, and poor application performance of the enzyme
-
food industry
-
biological isomaltulose production from sucrose catalyzed by sucrose isomerase. Isomaltulose is a safe sucrose substitute, that is widely used as a functional sweetener due to its promising properties, such as slower digestion, prolonged energy release, and less cariogenicity. Sucrose isomerase is responsible for the commercial biological production of isomaltulose from sucrose. Some problems exist in industrial production, such as the low secretion level from food safety grade strain, weak thermal stability, and poor application performance of the enzyme
-
food industry
Serratia plymuthica ATCC 15928
-
biological isomaltulose production from sucrose catalyzed by sucrose isomerase. Isomaltulose is a safe sucrose substitute, that is widely used as a functional sweetener due to its promising properties, such as slower digestion, prolonged energy release, and less cariogenicity. Sucrose isomerase is responsible for the commercial biological production of isomaltulose from sucrose. Some problems exist in industrial production, such as the low secretion level from food safety grade strain, weak thermal stability, and poor application performance of the enzyme
-
food industry
-
biological isomaltulose production from sucrose catalyzed by sucrose isomerase. Isomaltulose is a safe sucrose substitute, that is widely used as a functional sweetener due to its promising properties, such as slower digestion, prolonged energy release, and less cariogenicity. Sucrose isomerase is responsible for the commercial biological production of isomaltulose from sucrose. Some problems exist in industrial production, such as the low secretion level from food safety grade strain, weak thermal stability, and poor application performance of the enzyme
-
food industry
Raoultella planticola CCRC 19112
-
biological isomaltulose production from sucrose catalyzed by sucrose isomerase. Isomaltulose is a safe sucrose substitute, that is widely used as a functional sweetener due to its promising properties, such as slower digestion, prolonged energy release, and less cariogenicity. Sucrose isomerase is responsible for the commercial biological production of isomaltulose from sucrose. Some problems exist in industrial production, such as the low secretion level from food safety grade strain, weak thermal stability, and poor application performance of the enzyme
-
industry
a highly efficient and safe system for the expression of sucrose isomerase in Bacillus subtilis facilitates large-scale production and utilization of sucrose isomerase
industry
economical, effective, and promising approach for potential industrial isomaltulose production. Direct isomaltulose synthesis from beet molasses by immobilized sucrose isomerase. This process can produce a high concentration level of isomaltulose of 446.4 g/l with a yield of 0.94 g/g and a purity of 85.8% under the best conditions in the eighth batch, and also remain 97.5% of the sucrose conversion rate. Immobilized enzyme used in repeated batch reaction shows good reusability to convert pretreated beet molasse into isomaltulose. It is economically feasible. This study provides an economical, effective, and promising approach for potential industrial isomaltulose production
industry
E3DGG4
sucrose isomerase from Erwinia sp. immobilized with graphene oxide is a promising biocatalyst with high operational stability and catalytic activity for industrial production of isomaltulose
industry
expression and immobilization method that is promising in the industrial production of isomaltulose. High levels of secreted enzyme by overexpressing the gene from Pantoea dispersa in Yarrowia lipolytica, a successful host for efficient secretory expression, with a strong constitutive promoter. After optimization of the culture medium, the engineered strain JD secrets the enzyme with an activity of 49.3 U/ml. The recombinant SIase is effectively immobilized onto polyvinyl alcohol-alginate, and the enzymatic activity recovery rate is up to 82.4%. The stability of the enzyme is significantly improved by immobilization. Batch production of isomaltulose catalyzed by the immobilized enzyme is performed under optimal conditions, generating 620.7 g/l isomaltulose with a yield of 0.96 g/g. The conversion rate of sucrose after 13 batches remains above 90%
industry
VUC84579.1
sucrose isomerase from the Raoultella genus and its mutants show a potential to be used for the production of isomaltulose in the industry. The conversion rate of isomaltulose reaches 81.7% with only 2% of monosaccharide byproducts
industry
an engineered Corynebacterium glutamicum strain, IS7, is successfully constructed for the efficient and economic production of high-purity isomaltulose from sugar industrial molasses. Under the optimum conditions, the maximum production of isomaltulose using the engineered strain IS7 is 170.1 g/l with a yield of 0.97 g/g with cane molasses as substrate, and 167.0 g/l with a yield of 0.97 g/g with beet molasses as substrate, after 72 h fermentation. Isomaltulose purity is 98% using either cane or beet molasses as substrate
industry
Raoultella terrigena NCTC 9189
-
sucrose isomerase from the Raoultella genus and its mutants show a potential to be used for the production of isomaltulose in the industry. The conversion rate of isomaltulose reaches 81.7% with only 2% of monosaccharide byproducts
-
synthesis
-
formation of isomaltulose by immobilized Erwinia rhapontici cells
synthesis
-
production of palatinose, which is used as a sweetener and as a substitute for sucrose
synthesis
-
strain produces isomaltulose with maximum yield of 78-89% of supplied sucrose and 4% contaminating trehalose
synthesis
-
strain FMB1 show more than 90% conversion of sucrose at 4 g per l into isomaltulose in 2 days, with small amounts of trehalulose, glucose, and fructose as by-products. Use of strain in industrial production of isomaltulose
synthesis
isomaltulose production by the enzyme roduced from immobilized of Escherichia coli cells recombinantly expressing the enzyme, method overview
synthesis
immobilized cells of Protaminobacter rubrum strain CBS 574.77 are commonly used for the synthesis of isomaltulose from sucrose on an industrial scale
synthesis
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
synthesis
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
synthesis
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
synthesis
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
synthesis
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
synthesis
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
synthesis
-
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
synthesis
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
synthesis
Erwinia sp. D12
-
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
synthesis
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
synthesis
-
using Yarrowia lipolytica harboring displayed sucrose isomerase from Pantoea dispersa as whole-cell biocatalysts, cane molasses can be efficiently converted to the isomaltulose. In order to anchor sucrose isomerase from Pantoea dispersa (pSIase) to the cell surface, the gene encoding sucrose isomerase from Pantoea dispersa is fused with the vector pINA1317-CWP110. The constructed pINA1317-CWP110-pSIase is transfered into Yarrowia lipolytica. Using low-cost cane molasses as the substrate, the isomaltulose conversion rate remains at 85% even after 9 batches are processed
synthesis
E3DGG4
sucrose isomerase from Erwinia sp. immobilized with graphene oxide is a promising biocatalyst with high operational stability and catalytic activity for industrial production of isomaltulose
synthesis
-
strain FMB1 show more than 90% conversion of sucrose at 4 g per l into isomaltulose in 2 days, with small amounts of trehalulose, glucose, and fructose as by-products. Use of strain in industrial production of isomaltulose
-
synthesis
-
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
-
synthesis
-
strain produces isomaltulose with maximum yield of 78-89% of supplied sucrose and 4% contaminating trehalose
-
synthesis
-
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
-
synthesis
-
immobilized cells of Protaminobacter rubrum strain CBS 574.77 are commonly used for the synthesis of isomaltulose from sucrose on an industrial scale
-
synthesis
-
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
-
synthesis
-
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
-
synthesis
-
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
-
synthesis
-
isomaltulose production by the enzyme roduced from immobilized of Escherichia coli cells recombinantly expressing the enzyme, method overview
-
synthesis
-
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
-
synthesis
-
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
-
synthesis
Erwinia rhapontici wac2928
-
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
-
synthesis
-
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
-
synthesis
Serratia plymuthica ATCC 15928
-
isomaltulose (alpha-D-glucopyranosyl-1,6-D fructofuranose) is a carbohydrate used as ideal sucrose substitute. Sucrose isomerase is widely used in industries for the production of isomaltulose. The enzyme catalyzes the isomerization of sucrose into isomaltulose and trehalulose and may hydrolyze sucrose to produce small amounts of glucose and fructose
-
additional information
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
additional information
-
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
additional information
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
additional information
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
additional information
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
additional information
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
additional information
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
additional information
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
additional information
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
additional information
-
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
additional information
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
additional information
Erwinia sp. D12
-
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
additional information
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
additional information
-
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
-
additional information
-
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
-
additional information
-
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
-
additional information
-
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
-
additional information
-
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
-
additional information
-
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
-
additional information
-
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
-
additional information
Erwinia rhapontici wac2928
-
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
-
additional information
-
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
-
additional information
Serratia plymuthica ATCC 15928
-
in contrast to sucrose, isomaltulose is scarcely fermented by oral microbes and effectively inhibits the formation of water-insoluble glucans, showing that it is particularly suitable as a noncariogenic sucrose replacement
-
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Overexpression, purification, crystallization and preliminary diffraction studies of the Protaminobacter rubrum sucrose isomerase SmuA
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Klebsiella pneumoniae, Klebsiella pneumoniae NK33-98-8
-
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Trehalulose synthase native and carbohydrate complexed structures provide insights into sucrose isomerization
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Physiological and biochemical characteristics of an isomaltulose synthase producer Erwinia rhapontici
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44
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-
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brenda
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Isomaltulose production from sucrose by Protaminobacter rubrum immobilized in calcium alginate
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Structural determinants of product specificity of sucrose isomerases
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-
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-
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98
6569-6582
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brenda
Jung, J.H.; Kim, M.J.; Jeong, W.S.; Seo, D.H.; Ha, S.J.; Kim, Y.W.; Park, C.S.
Characterization of divergent pseudo-sucrose isomerase from Azotobacter vinelandii Deciphering the absence of sucrose isomerase activity
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483
115-121
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Azotobacter vinelandii (C1DMP8), Azotobacter vinelandii, Enterobacter sp. FMB-1 (B5ABD8), Azotobacter vinelandii DJ / ATCC BAA-1303 / KCTC 12137 (C1DMP8)
brenda
Li, L.; Wang, H.; Cheng, H.; Deng, Z.
Isomaltulose production by yeast surface display of sucrose isomerase from Pantoea dispersa on Yarrowia lipolytica
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32
208-217
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Pantoea dispersa (Q6XNK6), Pantoea dispersa UQ68 (Q6XNK6)
-
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Duan, X.; Cheng, S.; Ai, Y.; Wu, J.
Enhancing the thermostability of Serratia plymuthica sucrose isomerase using B-factor-directed mutagenesis
PLoS ONE
11
e0149208
2016
Serratia plymuthica (D0VX20), Serratia plymuthica, Serratia plymuthica AS9 (D0VX20), Serratia plymuthica AS9
brenda
Zheng, Y.; Wang, Z.; Ji, X.; Sheng, J.
Display of a sucrose isomerase on the cell surface of Yarrowia lipolytica for synthesis of isomaltulose from sugar cane by-products
3 Biotech
9
179
2019
Yarrowia lipolytica
brenda
Zhang, F.; Cai, X.; Cheng, F.; Yu, J.M.; Wang, B.; Liu, Z.Q.; Zheng, Y.G.
Immobilization of sucrose isomerase from Erwinia sp. with graphene oxide and its application in synthesizing isomaltulose
Appl. Biochem. Biotechnol.
194
709-724
2022
Erwinia sp. Ejp617 (E3DGG4)
brenda
Zhang, F.; Cheng, F.; Jia, D.X.; Liu, Q.; Liu, Z.Q.; Zheng, Y.G.
Tuning the catalytic performances of a sucrose isomerase for production of isomaltulose with high concentration
Appl. Microbiol. Biotechnol.
106
2493-2501
2022
Erwinia sp. Ejp617 (E3DGG4)
brenda
Liu, L.; Yu, S.; Zhao, W.
A novel sucrose isomerase producing isomaltulose from Raoultella terrigena
Appl. Sci.
11
5521
2021
Raoultella terrigena (VUC84579.1), Raoultella terrigena NCTC 9189 (VUC84579.1)
-
brenda
Zhang, F.; Cheng, F.; Jia, D.X.; Gu, Y.H.; Liu, Z.Q.; Zheng, Y.G.
Characterization of a recombinant sucrose isomerase and its application to enzymatic production of isomaltulose
Biotechnol. Lett.
43
261-269
2021
Erwinia sp. Ejp617 (E3DGG4)
brenda
Liu, L.; Bilal, M.; Luo, H.; Zhao, Y.; Duan, X.
Studies on biological production of isomaltulose using sucrose isomerase Current Status and Future Perspectives
Catal. Lett.
151
1868-1881
2021
Erwinia rhapontici, Erwinia rhapontici (D9MPF2), Enterobacter sp. FMB-1 (B5ABD8), Serratia plymuthica, Serratia plymuthica (D0VX20), Klebsiella sp. LX3 (Q8KR84), Burkholderia ubonensis subsp. mesacidophila (Q2PS28), Rhizobium sp., Klebsiella pneumoniae, Pantoea dispersa, Raoultella planticola, Pantoea dispersa UQ68J, Erwinia rhapontici NX-5 (D9MPF2), Erwinia rhapontici wac2928, Serratia plymuthica AS9, Serratia plymuthica ATCC 15928 (D0VX20), Klebsiella pneumoniae NK33, Raoultella planticola CCRC 19112
-
brenda
Pilak, P.; Schiefner, A.; Seiboth, J.; Oehrlein, J.; Skerra, A.
Engineering a highly active sucrose isomerase for enhanced product specificity by using a ''Battleship'' strategy
ChemBioChem
21
2161-2169
2020
Serratia plymuthica
brenda
Guo, D.; Li, M.; Jiang, M.; Cong, G.; Liu, Y.; Wang, C.; Li, X.
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Efficient and economical biosynthesis of high-purity isomaltulose from sugar industrial waste molasses using an engineered Corynebacterium glutamicum strain
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