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Information on EC 5.4.99.11 - isomaltulose synthase
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5.4.99.11 isomaltulose synthaseIUBMB Comments
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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Word Map
- 5.4.99.11
- synthesis
- erwinia
- rhapontici
- palatinose
-
protaminobacter
-
2.4.1.1
- pantoea
-
1,4-alpha-d-glucan:orthophosphate
- molasses
- plymuthica
- food industry
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vacuole-targeted
- dispersa
- whiteflies
- bemisia
- honeydew
The enzyme appears in viruses and cellular organisms
Synonyms
sucrose isomerase, siase, alpha-glucosyltransferase, isomaltulose synthase, trehalulose synthase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-Glucosyltransferase
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Avin_08330
AZOG
EC 5.4.99.10
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formerly
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isomaltulose synthase
Isomaltulose synthetase
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MutB
NX-5
PdSIase
SIase
SmuA
Sucrose 6-glucosylmutase
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Sucrose alpha-glucosyltransferase
sucrose isomerase
Sucrose mutase
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Synthase, isomaltulose
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Trehalulose synthase
Sucrose alpha-glucosyltransferase
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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
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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
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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
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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
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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
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
sucrose
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
4-nitrophenyl alpha-D-glucoside
?
wild-type AZOG and enzyme chimeric mutant AZF3
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?
4-nitrophenyl alpha-D-glucoside
?
Azotobacter vinelandii DJ / ATCC BAA-1303 / KCTC 12137
wild-type AZOG and enzyme chimeric mutant AZF3
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?
4-nitrophenyl alpha-D-glucoside
?
enzyme chimeric mutant AZF3
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?
isomaltulose
sucrose
wild-type AZOG and enzyme chimeric mutant AZF3
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r
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
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product specificity of enzyme NX-5 towards isomaltulose and the role of the loop330-339 in NX-5 catalysis
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
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?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
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product specificity of enzyme NX-5 towards isomaltulose and the role of the loop330-339 in NX-5 catalysis
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
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?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
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?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
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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
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-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
production of trehalulose and isomaltulose in a ratio of 64:36
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-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
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
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?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
production of trehalulose and isomaltulose in a ratio of 64:36
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?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
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
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?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
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?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
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main products
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?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
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high product specificity for trehalulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose)
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?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
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?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
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?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
activity involves residues D241, E295, H368, and D369
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?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
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?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
activity involves residues D241, E295, H368, and D369
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?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
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?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
wild-type AZOG and enzyme chimeric mutant AZF3
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r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Azotobacter vinelandii DJ / ATCC BAA-1303 / KCTC 12137
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r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Azotobacter vinelandii DJ / ATCC BAA-1303 / KCTC 12137
wild-type AZOG and enzyme chimeric mutant AZF3
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r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
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r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
enzyme chimeric mutant AZF3
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r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
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r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
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isomaltulose + alpha 1,1-linked disaccharide
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
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ir
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
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the enzyme is sucrose-specific
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
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r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
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r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Paraburkholderia acidicola
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r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Paraburkholderia acidicola
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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
Paraburkholderia acidicola MX-45
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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
Paraburkholderia acidicola MX-45
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?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Paraburkholderia acidicola MX-45
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r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
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r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
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i.e. beta-D-glucopyranosyl-D-fructofuranose
isomaltulose + glucose,fructose 1,1'-disaccharide
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
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
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?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
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?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
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
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?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
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i.e. beta-D-glucopyranosyl-D-fructofuranose
isomaltulose + glucose,fructose 1,1'-disaccharide
?
sucrose
alpha-D-glucopyranosyl-1,1-D-fructofuranose
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more than 90% conversion of sucrose. Small amounts of trehalulose, glucose, and fructose are produced as by-products
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?
sucrose
alpha-D-glucopyranosyl-1,1-D-fructofuranose
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more than 90% conversion of sucrose. Small amounts of trehalulose, glucose, and fructose are produced as by-products
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?
sucrose
alpha-D-glucopyranosyl-1,1-D-fructofuranose
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plus small amounts of glucose, fructose and eventually isomaltose as by-products
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?
sucrose
alpha-D-glucopyranosyl-1,6-D-fructofuranose + alpha-D-glucopyranosyl-1,1-D-fructofuranose
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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
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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
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two-step reaction mechanism for hydrolysis and isomerization, which occurs in the same pocket
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?
sucrose
alpha-D-glucopyranosyl-1,6-D-fructofuranose + alpha-D-glucopyranosyl-1,1-D-fructofuranose
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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
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ir
sucrose
alpha-D-glucopyranosyl-1,6-D-fructofuranose + alpha-D-glucopyranosyl-1,1-D-fructofuranose
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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
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ir
sucrose
alpha-D-glucopyranosyl-1,6-D-fructofuranose + alpha-D-glucopyranosyl-1,1-D-fructofuranose
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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
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ir
sucrose
alpha-D-glucopyranosyl-1,6-D-fructofuranose + alpha-D-glucopyranosyl-1,1-D-fructofuranose
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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
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ir
sucrose
isomaltulose + trehalulose
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the product ratio is 78% isomaltulose and 22% trehalulose
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?
sucrose
isomaltulose + trehalulose + D-glucose
Paraburkholderia acidicola
MutB catalyzes the isomerization of sucrose to mainly trehalulose (1-O-alpha-D-glucopyranosyl-beta-D-fructose)
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r
sucrose
isomaltulose + trehalulose + D-glucose
Paraburkholderia acidicola MX-45
MutB catalyzes the isomerization of sucrose to mainly trehalulose (1-O-alpha-D-glucopyranosyl-beta-D-fructose)
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r
sucrose
palatinose + trehalulose + D-glucose + D-fructose
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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
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ir
sucrose
palatinose + trehalulose + D-glucose + D-fructose
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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
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ir
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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Azotobacter vinelandii DJ / ATCC BAA-1303 / KCTC 12137
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
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?
additional information
?
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Bemisia argentifolia
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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
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?
additional information
?
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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
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?
additional information
?
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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
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-
?
additional information
?
-
-
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
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-
?
additional information
?
-
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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
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-
?
additional information
?
-
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
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?
additional information
?
-
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
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?
additional information
?
-
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
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-
?
additional information
?
-
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
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-
?
additional information
?
-
-
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
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-
?
additional information
?
-
-
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
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-
?
additional information
?
-
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
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?
additional information
?
-
Erwinia rhapontici wac2928
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
-
-
?
additional information
?
-
Erwinia sp. D12
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
no apparent reverse reaction producing glucose, fructose, or trehalose, from isomaltulose
-
-
?
additional information
?
-
-
no apparent reverse reaction producing glucose, fructose, or trehalose, from isomaltulose
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
no apparent reverse reaction producing glucose, fructose, or trehalose, from isomaltulose
-
-
?
additional information
?
-
-
no apparent reverse reaction producing glucose, fructose, or trehalose, from isomaltulose
-
-
?
additional information
?
-
Paraburkholderia acidicola
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
-
-
?
additional information
?
-
Paraburkholderia acidicola
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
-
-
?
additional information
?
-
Paraburkholderia acidicola MX-45
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
-
-
?
additional information
?
-
Paraburkholderia acidicola MX-45
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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)
-
-
?
additional information
?
-
-
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)
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
Serratia plymuthica ATCC 15928
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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)
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
product specificity of enzyme NX-5 towards isomaltulose and the role of the loop330-339 in NX-5 catalysis
-
-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
product specificity of enzyme NX-5 towards isomaltulose and the role of the loop330-339 in NX-5 catalysis
-
-
?
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
production of trehalulose and isomaltulose in a ratio of 64:36
-
-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
production of trehalulose and isomaltulose in a ratio of 64:36
-
-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
main products
-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
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
-
-
-
?
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
-
-
-
?
sucrose
1-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
-
-
-
?
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Azotobacter vinelandii DJ / ATCC BAA-1303 / KCTC 12137
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Paraburkholderia acidicola
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
Paraburkholderia acidicola MX-45
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
r
sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
-
-
?
additional information
?
-
Bemisia argentifolia
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
Paraburkholderia acidicola
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
-
-
?
additional information
?
-
Paraburkholderia acidicola MX-45
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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)
-
-
?
additional information
?
-
-
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)
-
-
?
additional information
?
-
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)
-
-
?
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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
Paraburkholderia acidicola
-
competitive, crystal structure in complex with enzyme
deoxynojirimycin
Paraburkholderia acidicola
-
competitive, crystal structure in complex with enzyme
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
Tris(hydroxymethyl)aminomethane
Paraburkholderia acidicola
-
competitive, crystal structure in complex with enzyme
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0192
sucrose
Paraburkholderia acidicola
pH not specified in the publication, 20°C, native enzyme
0.03
sucrose
Paraburkholderia acidicola
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
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
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
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
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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
36
sucrose
Paraburkholderia acidicola
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
Paraburkholderia acidicola
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
900
957.5
purified recombinant wild-type enzyme, pH 6.0, 30°C, substrate sucrose
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
Paraburkholderia acidicola
substrate sucrose, pH and temperature not specified in the publication, recombinant enzyme
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
5.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
Paraburkholderia acidicola
-
pH 4.2: about 30% of maximal activity, pH 7.8: about 50% of maximal activity
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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
30 - 35
35
40
45
50
additional information
Paraburkholderia acidicola
-
the ratio of trehalulose to isomaltulose increases at lower temperatures. The optimum for trehalulose production is 20°C
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 - 50
20 - 55
activity range of recombinant enzyme expressed from Yarrowia lipolytica, profile overview
20 - 60
Paraburkholderia acidicola
-
20°C: about 50% of maximal activity, 40°C: about 40% of maximal activity
35 - 60
-
recombinant enzyme displayed on Saccharomyces cerevisiae surface shows higher activity than the enzyme expressed in Escherichia coli strain DH10B
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
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Paraburkholderia acidicola
Paraburkholderia acidicola MX-45
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
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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
Paraburkholderia acidicola
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
Erwinia rhapontici wac2928
-
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
-
physiological function
Paraburkholderia acidicola MX-45
-
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
-
physiological function
Serratia plymuthica ATCC 15928
-
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
-
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
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
-
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
-
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
-
enzyme-substrate complex, docking study with sucrose and fructose
-
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
-
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
-
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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
-
Q2PS28_9BURK
Burkholderia ubonensis subsp. mesacidophila
584
0
66792
TrEMBL
-
Q4L2Q1_9ENTR
598
0
69989
TrEMBL
other Location (Reliability: 3)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65000
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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
-
?
Paraburkholderia acidicola MX-45
-
x * 63000, SDS-PAGE
-
?
Paraburkholderia acidicola MX-45
-
x * 64000, SDS-PAGE and calculated
-
?
Paraburkholderia acidicola MX-45
-
x * 64300, recombinant enzyme, x * 63000, native enzyme
-
?
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
-
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
Paraburkholderia acidicola
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
Paraburkholderia acidicola
-
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
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
-
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
-
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
Paraburkholderia acidicola
the mutant favors the transfer reaction with an isomer preference for isomaltulose
R311C
Paraburkholderia acidicola
the mutant demonstrates higher catalytic efficiency for D-glucose production over trehalulose production
D200A
Paraburkholderia acidicola MX-45
-
enzyme mutant structure analysis
-
D442N
Paraburkholderia acidicola MX-45
-
the mutant favors the transfer reaction with an isomer preference for isomaltulose
-
E254Q
Paraburkholderia acidicola MX-45
-
enzyme mutant structure analysis
-
R311C
Paraburkholderia acidicola MX-45
-
the mutant demonstrates higher catalytic efficiency for D-glucose production over trehalulose production
-
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
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)
-
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
-
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
-
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 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
-
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
-
mutations of the loop region of enzyme NX-5 result in significant changes of the product ratio between isomaltulose and trehalulose
-
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 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
-
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
-
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
-
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
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
-
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
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
-
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
-
additional information
-
engineering of the enzyme to exhibit isomelezitose synthase activity for production of the probiotically nutrial component, overview
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 7
the yeast strain displaying recombinant enzyme PdSIase is stable throughout relatively broad ranges of pH values and temperatures
748342
4.5 - 8
-
the immobilized enzyme retains more than 80% of its relative activity at pH 4.5-8.0
746691
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
704227
5 - 7
5 - 7.5
-
the free enzyme retains more than 80% of its relative activity at pH 5.0-7.5
746691
5.1 - 6.7
Paraburkholderia acidicola
-
highest stability
3468
5 - 7
-
recombinant enzyme displayed on Saccharomyces cerevisiae surface, stable at
727181
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
714486
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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 - 55
-
recombinant enzyme displayed on Saccharomyces cerevisiae surface, stable at, half-life at 50°C is 2.4 h
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
52
50% activity remaining of recombinant enzyme expressed from Escherichia coli, inactivation at 65°C, profile overview
60
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
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, 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
Paraburkholderia acidicola
expression in Escherichia coli
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
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
-
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
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
-
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
-
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
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 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
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
Paraburkholderia acidicola
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
-
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
-
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
-
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
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
Paraburkholderia acidicola MX-45
-
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 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
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
-
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
-
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
Paraburkholderia acidicola
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
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
Paraburkholderia acidicola MX-45
-
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
-
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
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cheetham, P.S.J.; Imber, C.E.; Isherwood, J.
The formation of isomaltulose by immobilized Erwinia rhapontici
Nature
299
628-631
1982
Erwinia rhapontici
-
brenda
Cheetham, P.S.J.
The extraction and mechanism of a novel isomaltulose-synthesizing enzyme from Erwinia rhapontici
Biochem. J.
220
213-220
1982
Erwinia rhapontici
brenda
McAllister, M.; Kelly, C.T.; Doyle, E.; Fogarty, W.M.
The isomaltoluse synthesising enzyme of Serratia plymuthica
Biotechnol. Lett.
12
667-672
1990
Serratia plymuthica
-
brenda
Nagai, Y.; Sugitani, T.; Tsuyuki, K.
Characterization of alpha-glucosyltransferase from Pseudomonas mesoacidophila MX-45
Biosci. Biotechnol. Biochem.
58
1789-1793
1994
Paraburkholderia acidicola, Paraburkholderia acidicola MX-45
brenda
Salvucci, M.E.; Wolfe, G.R.; Hendrix, D.L.
Effect of sucrose concentration on carbohydrate metabolism in Bemisia argentifolii: biochemical mechanism and physiological role for trehalulose synthesis in the silverleaf whitefly
J. Insect Physiol.
43
457-464
1997
Bemisia argentifolia
-
brenda
Egerer, P.
Downstream processing of sucrose 6-glucosylmutase and production of isomaltulose, a non-cariogenic, low-caloric sweetener
Hindustan Antibiot. Bull.
36
65-77
1994
Serratia plymuthica, Serratia plymuthica Z12
brenda
Cheetham, P.S.J.; Garrett, C.; Clark, J.
Isomaltulose production using immobilized cells
Biotechnol. Bioeng.
27
471-481
1985
Erwinia rhapontici
brenda
Cheetham, P.S.J.
Production of isomaltulose using immobilized microbial cells
Methods Enzymol.
136
432-454
1987
Erwinia rhapontici
-
brenda
Li, N.; Zhang, D.; Zhang, L.H.; Swaminathan, K.
Expression, crystallization and preliminary X-ray analysis of isomaltulose synthase (PalI) from Klebsiella sp. LX3
Acta Crystallogr. Sect. D
59
150-151
2003
Klebsiella sp.
brenda
Zhang, D.; Li, X.; Zhang, L.H.
Isomaltulose synthase from Klebsiella sp. strain LX3: gene cloning and characterization and engineering of thermostability
Appl. Environ. Microbiol.
68
2676-2682
2002
Klebsiella sp.
brenda
Zhang, D.; Li, N.; Swaminathan, K.; Zhang, L.H.
A motif rich in charged residues determines product specificity in isomaltulose synthase
FEBS Lett.
534
151-155
2003
Klebsiella sp.
brenda
Zhang, D.; Li, N.; Lok, S.M.; Zhang, L.H.; Swaminathan, K.
Isomaltulose synthase (PalI) of Klebsiella sp. LX3. Crystal structure and implication of mechanism
J. Biol. Chem.
278
35428-35434
2003
Klebsiella sp. LX3
brenda
Park, Y.K.; Uekane, R.T.; Pupin, A.M.
Conversion of sucrose to isomaltose by microbial glucosyltransferase
Biotechnol. Lett.
14
547-551
1992
Serratia plymuthica
-
brenda
Ravaud, S.; Watzlawick, H.; Haser, R.; Mattes, R.; Aghajari, N.
Expression, purification, crystallization and preliminary x-ray crystallographic studies of the trehalulose synthase MutB from Pseudomonas mesoacidophila MX-45
Acta Crystallogr. Sect. F
F61
100-103
2005
Paraburkholderia acidicola, Paraburkholderia acidicola MX-45
brenda
Wu, L.; Birch, R.G.
Characterization of the highly efficient sucrose isomerase from Pantoea dispersa UQ68J and cloning of the sucrose isomerase gene
Appl. Environ. Microbiol.
71
1581-1590
2005
Raoultella planticola (Q6XKX6), Raoultella planticola, Pantoea dispersa (Q6XNK6), Pantoea dispersa, Raoultella planticola UQ14S (Q6XKX6), Pantoea dispersa UQ68J (Q6XNK6), Pantoea dispersa UQ68J
brenda
Wu, L.; Birch, R.G.
Characterization of Pantoea dispersa UQ68J: producer of a highly efficient sucrose isomerase for isomaltulose biosynthesis
J. Appl. Microbiol.
97
93-103
2004
Pantoea dispersa, Pantoea dispersa UQ68J
brenda
Ravaud, S.; Watzlawick, H.; Haser, R.; Mattes, R.; Aghajari, N.
Overexpression, purification, crystallization and preliminary diffraction studies of the Protaminobacter rubrum sucrose isomerase SmuA
Acta Crystallogr. Sect. F
F62
74-76
2006
Serratia plymuthica
brenda
Cho, M.; Park, S.; Lim, J.K.; Kim, J.; Kim, J.H.; Kwon, D.Y.; Park, C.
Conversion of sucrose into isomaltulose by Enterobacter sp. FMB1, an isomaltulose-producing microorganism isolated from traditional Korean food
Biotechnol. Lett.
29
453-458
2007
Enterobacter sp., Enterobacter sp. FMB1
brenda
Aroonnual, A.; Nihira, T.; Seki, T.; Panbangred, W.
Role of several key residues in the catalytic activity of sucrose isomerase from Klebsiella pneumoniae NK33-98-8
Enzyme Microb. Technol.
40
1221-1227
2007
Klebsiella pneumoniae, Klebsiella pneumoniae NK33-98-8
-
brenda
Ravaud, S.; Robert, X.; Watzlawick, H.; Haser, R.; Mattes, R.; Aghajari, N.
Trehalulose synthase native and carbohydrate complexed structures provide insights into sucrose isomerization
J. Biol. Chem.
282
28126-28136
2007
Paraburkholderia acidicola, Paraburkholderia acidicola MX-45
brenda
Korneeva, O.S.; Bozhko, O.Y.; Mangueva, Z.M.
Physiological and biochemical characteristics of an isomaltulose synthase producer Erwinia rhapontici
Appl. Biochem. Microbiol.
44
566-570
2008
Erwinia rhapontici
-
brenda
Watzlawick, H.; Mattes, R.
Gene cloning, protein characterization, and alteration of product selectivity for the trehalulose hydrolase and trehalulose synthase from "Pseudomonas mesoacidophila" MX-45
Appl. Environ. Microbiol.
75
7026-7036
2009
Paraburkholderia acidicola (Q2PS28), Paraburkholderia acidicola MX-45 (Q2PS28)
brenda
de Oliva-Neto, P.; Menao, P.T.
Isomaltulose production from sucrose by Protaminobacter rubrum immobilized in calcium alginate
Biores. Technol.
100
4252-4256
2009
Serratia plymuthica, Serratia plymuthica CBS 574.77
brenda
Ravaud, S.; Robert, X.; Watzlawick, H.; Haser, R.; Mattes, R.; Aghajari, N.
Structural determinants of product specificity of sucrose isomerases
FEBS Lett.
583
1964-1968
2009
Serratia plymuthica (D0VX20), Serratia plymuthica
brenda
Cha, J.; Jung, J.H.; Park, S.E.; Cho, M.H.; Seo, D.H.; Ha, S.J.; Yoon, J.W.; Lee, O.H.; Kim, Y.C.; Park, C.S.
Molecular cloning and functional characterization of a sucrose isomerase (isomaltulose synthase) gene from Enterobacter sp. FMB-1
J. Appl. Microbiol.
107
1119-1130
2009
Enterobacter sp. FMB-1 (B5ABD8)
brenda
Li, S.; Cai, H.; Qing, Y.; Ren, B.; Xu, H.; Zhu, H.; Yao, J.
Cloning and characterization of a sucrose isomerase from Erwinia rhapontici NX-5 for isomaltulose hyperproduction
Appl. Biochem. Biotechnol.
163
52-63
2011
Erwinia rhapontici (D9MPF2), Erwinia rhapontici NX-5 (D9MPF2), Erwinia rhapontici NX-5
brenda
Ren, B.; Li, S.; Xu, H.; Feng, X.H.; Cai, H.; Ye, Q.
Purification and characterization of a highly selective sucrose isomerase from Erwinia rhapontici NX-5
Bioprocess Biosyst. Eng.
34
629-637
2011
Erwinia rhapontici, Erwinia rhapontici NX-5
brenda
Hamerli, D.; Birch, R.G.
Transgenic expression of trehalulose synthase results in high concentrations of the sucrose isomer trehalulose in mature stems of field-grown sugarcane
Plant Biotechnol. J.
9
32-37
2011
Paraburkholderia acidicola (Q2PS28), Paraburkholderia acidicola MX-45 (Q2PS28)
brenda
Lipski, A.; Watzlawick, H.; Ravaud, S.; Robert, X.; Rhimi, M.; Haser, R.; Mattes, R.; Aghajari, N.
Mutations inducing an active-site aperture in Rhizobium sp. sucrose isomerase confer hydrolytic activity
Acta Crystallogr. Sect. D
69
298-307
2013
Rhizobium sp. (M1E1F6), Rhizobium sp.
brenda
Contesini, F.; Carvalho, P.; Grosso, C.; Sato, H.
Single-step purification, characterization and immobilization of a sucrose isomerase from Erwinia sp
Biocatal. Agricult. Biotechnol.
2
322-327
2013
Erwinia sp.
-
brenda
Li, S.; Xu, H.; Yu, J.; Wang, Y.; Feng, X.; Ouyang, P.
Enhancing isomaltulose production by recombinant Escherichia coli producing sucrose isomerase: culture medium optimization containing agricultural wastes and cell immobilization
Bioprocess Biosyst. Eng.
36
1395-1405
2013
Erwinia rhapontici (D9MPF2), Erwinia rhapontici NX-5 (D9MPF2)
brenda
Lee, G.Y.; Jung, J.H.; Seo, D.H.; Hansin, J.; Ha, S.J.; Cha, J.; Kim, Y.S.; Park, C.S.
Isomaltulose production via yeast surface display of sucrose isomerase from Enterobacter sp. FMB-1 on Saccharomyces cerevisiae
Biores. Technol.
102
9179-9184
2011
Enterobacter sp.
brenda
Goerl, J.; Timm, M.; Seibel, J.
Mechanism-oriented redesign of an isomaltulose synthase to an isomelezitose synthase by site-directed mutagenesis
ChemBioChem
13
149-156
2012
Serratia plymuthica (D0VX20), Serratia plymuthica, Serratia plymuthica CBS 574.77 (D0VX20)
brenda
Goulter, K.C.; Hashimi, S.M.; Birch, R.G.
Microbial sucrose isomerases: producing organisms, genes and enzymes
Enzyme Microb. Technol.
50
57-64
2012
Serratia plymuthica (D0VX20), Serratia plymuthica, Rhizobium sp. (M1E1F3), Rhizobium sp. (M1E1F6), Rhizobium sp. (M1E1F7), Rhizobium sp., Serratia plymuthica L0W308 (D0VX20)
brenda
Nam, C.H.; Seo, D.H.; Jung, J.H.; Koh, Y.J.; Jung, J.S.; Heu, S.; Oh, C.S.; Park, C.S.
Functional characterization of the sucrose isomerase responsible for trehalulose production in plant-associated Pectobacterium species
Enzyme Microb. Technol.
55
100-106
2014
Pectobacterium carotovorum (S5YEW8), Pectobacterium carotovorum, Pectobacterium carotovorum KKH 3-1 (S5YEW8), Pectobacterium carotovorum KKH 3-1
brenda
Xu, Z.; Li, S.; Li, J.; Li, Y.; Feng, X.; Wang, R.; Xu, H.; Zhou, J.
The structural basis of Erwinia rhapontici isomaltulose synthase
PLoS ONE
8
e74788
2013
Erwinia rhapontici, Erwinia rhapontici NX-5
brenda
Wu, L.; Qiu, J.; Wu, S.; Liu, X.; Liu, C.; Xu, Z.; Li, S.; Xu, H.
Bioinspired production of antibacterial sucrose isomerase-sponge for the synthesis of isomaltulose
Adv. Synth. Catal.
358
4030-4040
2016
Erwinia rhapontici, Erwinia rhapontici NX-5
-
brenda
Mu, W.; Li, W.; Wang, X.; Zhang, T.; Jiang, B.
Current studies on sucrose isomerase and biological isomaltulose production using sucrose isomerase
Appl. Microbiol. Biotechnol.
98
6569-6582
2014
Erwinia rhapontici, Erwinia rhapontici (D9MPF2), Erwinia rhapontici (Q6XNK5), Erwinia rhapontici (Q9AI64), Serratia plymuthica, no activity in Bemisia argentifolii, Erwinia sp. D12, Enterobacter sp. FMB-1 (B5ABD8), Rhizobium sp. MX-45 (M1E1F6), Paraburkholderia acidicola (Q2PS28), Klebsiella pneumoniae (Q4L2Q1), Raoultella planticola (Q6XKX6), Pantoea dispersa (Q6XNK6), Klebsiella sp. LX3 (Q8KR84), Erwinia rhapontici DSM 4484 (Q9AI64), Klebsiella pneumoniae NK33-98-8 (Q4L2Q1), Raoultella planticola UQ14S (Q6XKX6), Erwinia rhapontici NCPPB 1578, Pantoea dispersa UQ68J (Q6XNK6), Serratia plymuthica CBS 574.77, Erwinia rhapontici wac2928 (Q6XNK5), Paraburkholderia acidicola MX-45 (Q2PS28), Serratia plymuthica ATCC 15928, Erwinia rhapontici NX-5 (D9MPF2)
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
Biochem. Biophys. Res. Commun.
483
115-121
2017
Azotobacter vinelandii (C1DMP8), Azotobacter vinelandii, Azotobacter vinelandii DJ / ATCC BAA-1303 / KCTC 12137 (C1DMP8), Enterobacter sp. FMB-1 (B5ABD8)
brenda
Li, L.; Wang, H.; Cheng, H.; Deng, Z.
Isomaltulose production by yeast surface display of sucrose isomerase from Pantoea dispersa on Yarrowia lipolytica
J. Funct. Foods
32
208-217
2017
Pantoea dispersa (Q6XNK6), Pantoea dispersa UQ68 (Q6XNK6)
-
brenda
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
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