3.2.1.11: dextranase
This is an abbreviated version!
For detailed information about dextranase, go to the full flat file.
Word Map on EC 3.2.1.11
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3.2.1.11
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dextrans
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streptococcus
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dental
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glucans
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plaque
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penicillium
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caries
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leuconostoc
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sobrinus
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dextransucrase
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isomaltose
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water-insoluble
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cariogenic
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mesenteroides
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colon-specific
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lipomyces
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downei
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sanguis
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glucosyltransferases
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funiculosum
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salivarius
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mutanase
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synthesis
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medicine
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starkeyi
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isomaltotriose
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agriculture
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degradation
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nutrition
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drug development
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isomalto-oligosaccharides
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biotechnology
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food industry
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glucan-binding
- 3.2.1.11
- dextrans
- streptococcus
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dental
- glucans
- plaque
- penicillium
- caries
- leuconostoc
- sobrinus
- dextransucrase
- isomaltose
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water-insoluble
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cariogenic
- mesenteroides
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colon-specific
- lipomyces
- downei
- sanguis
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glucosyltransferases
- funiculosum
- salivarius
- mutanase
- synthesis
- medicine
- starkeyi
- isomaltotriose
- agriculture
- degradation
- nutrition
- drug development
- isomalto-oligosaccharides
- biotechnology
- food industry
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glucan-binding
Reaction
Synonyms
1,6-alpha-D-glucan-6-glucanohydrolase, 6-alpha-D-glucan 6-glucanohydrolase, alpha-1,6-D-glucan 6-glucanohydrolase, alpha-1,6-D-glucan-6-glucanohydrolase, Alpha-1,6-glucan-6-glucanohydrolase, alpha-D-1,6-glucan-6-glucanohydrolase, alpha-dextranase, alpha-glucanase, AODex, Dex, Dex2, Dex410, Dex49A, DexA, dextran hydrolase, dextranase, dextranase DL 2, dextranase I, dextranase II, Dextranase Plus L, dextransucrase, DL 2, DXSR, endo-dextranase, endodextranase, extracellular dextranase, Fjoh_4430, LSD1, More, rDex, SmDex, Teth39_0264, TLDex, TPDex
ECTree
Advanced search results
Engineering
Engineering on EC 3.2.1.11 - dextranase
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D279C/S289C
T245C/N248C
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the mutant shows a more than 3°C improvement on its optimal temperature compared to the wild type enzyme
D189A
application of achemical rescue approach using alpha-isomaltotetraosyl fluoride with NaN3. Mutant forms small sized dextran from alpha-isomaltotetraosyl fluoride in the presence of NaN3
D340G
application of a chemical rescue approach using alpha-isomaltotetraosyl fluoride with NaN3. Mutant forms beta-isomaltotetraosyl azide indicating residue D340 as nucleophile catalyst
E412Q
D189A
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application of achemical rescue approach using alpha-isomaltotetraosyl fluoride with NaN3. Mutant forms small sized dextran from alpha-isomaltotetraosyl fluoride in the presence of NaN3
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D340G
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application of a chemical rescue approach using alpha-isomaltotetraosyl fluoride with NaN3. Mutant forms beta-isomaltotetraosyl azide indicating residue D340 as nucleophile catalyst
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E412Q
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application of a chemical rescue approach using alpha-isomaltotetraosyl fluoride with NaN3. Mutant forms alpha-isomaltotetraosyl azide indicating residue E412 as acid/base catalyst
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A356F
the mutant exhibits improved thermostability compared to the wild type enzyme
G355F
the mutant exhibits improved thermostability compared to the wild type enzyme
S354F
the mutant exhibits improved thermostability compared to the wild type enzyme
S357F
the mutant exhibits improved thermostability compared to the wild type enzyme
S357F/G355F
the mutant exhibits improved thermostability compared to the wild type enzyme
A356F
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the mutant exhibits improved thermostability compared to the wild type enzyme
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G355F
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the mutant exhibits improved thermostability compared to the wild type enzyme
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S354F
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the mutant exhibits improved thermostability compared to the wild type enzyme
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S357F
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the mutant exhibits improved thermostability compared to the wild type enzyme
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S357F/G355F
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the mutant exhibits improved thermostability compared to the wild type enzyme
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T558H
the mutation affects the hydrolytic activities of the enzyme. The mutant increases the proportion of isomaltooligosaccharide with degrees of polymerization of 5 in hydrolysates following reactions with 4 mg/ml dextran
T563N
the mutation affects the hydrolytic activities of the enzyme
W279A
the mutation affects the hydrolytic activities of the enzyme
W279A/T563N
the mutations affect the hydrolytic activities of the enzyme
W279F
the mutation affects the hydrolytic activities of the enzyme
W279F/T563N
the mutations affect the hydrolytic activities of the enzyme
T558H
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the mutation affects the hydrolytic activities of the enzyme. The mutant increases the proportion of isomaltooligosaccharide with degrees of polymerization of 5 in hydrolysates following reactions with 4 mg/ml dextran
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W279A
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the mutation affects the hydrolytic activities of the enzyme
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W279A/T563N
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the mutations affect the hydrolytic activities of the enzyme
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W279F
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the mutation affects the hydrolytic activities of the enzyme
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W279F/T563N
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the mutations affect the hydrolytic activities of the enzyme
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D312G
additional information
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the mutant shows a more than 13°C improvement on its optimal temperature compared to the wild type enzyme
D279C/S289C
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the mutant shows a more than 3°C improvement on its optimal temperature compared to the wild type enzyme
E412Q
application of a chemical rescue approach using alpha-isomaltotetraosyl fluoride with NaN3. Mutant forms alpha-isomaltotetraosyl azide indicating residue E412 as acid/base catalyst
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immobilization of dextranase on several carriers by entrapment and covalent binding with cross-linking. Entrapment in sodium alginate with Ca2+. Dextranase immobilized on bovine serum albumin with a cross-linking agent shows the highest activity and considerable immobilization yield of 66.7%. The optimum pH of the immobilized enzyme is shifted to pH 6.0 as compared to the free enzyme pH 5.5. The optimum temperature of the reaction is at 60°C for both free and immobilized enzyme. Thermal and pH stability are significantly improved by the immobilization process. Km of the immobilized dextranase is higher than that of the free dextranase, while Vmax of the immobilized enzyme is lower than that of the free dextranase. The immobilized enzyme is able to retain 76% of the initial catalytic activity after 5.0 cycles
additional information
dexI mutants with improved thermostability. In terms of their relative specific activity towards dextran, noticeable differences among mutants showing increased, similar or reduced enzyme activity as compared to wild-type
additional information
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dexI mutants with improved thermostability. In terms of their relative specific activity towards dextran, noticeable differences among mutants showing increased, similar or reduced enzyme activity as compared to wild-type
additional information
a C-terminal truncated enzyme, residues Ala39-Ser1304, has 50% wild-type activity
additional information
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a C-terminal truncated enzyme, residues Ala39-Ser1304, has 50% wild-type activity
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additional information
generation of an engineered fusion enzyme of dextransucrase, from dsrBCB4 gene from Leuconostoc mesenteroides B-1299CB4, and Arthrobacter oxydans dextranase, i.e. DSXR. DSXR is potentially useful for reliable production of long isomalto-oligosaccharides from sucrose by a one-step reaction
additional information
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deletion mutant of the C-terminal region can hydrolyze blue dextrans. Double mutant W793L and deletion mutant of the C-terminal region has no dextranase activity
additional information
deletion mutant of the C-terminal region can hydrolyze blue dextrans. Double mutant W793L and deletion mutant of the C-terminal region has no dextranase activity
additional information
deletion mutant of the C-terminal region can hydrolyze blue dextrans. Double mutant W793L and deletion mutant of the C-terminal region has no dextranase activity
additional information
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deletion mutant of the C-terminal region can hydrolyze blue dextrans. Double mutant W793L and deletion mutant of the C-terminal region has no dextranase activity
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additional information
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loss of activity in N-terminal deletion mutants
additional information
generation of five truncated SmDexs by deleting the N-terminal variable region, the glucan-binding site, or the C-terminal variable region. Two truncation-mutant enzymes devoid of C-terminal variable region or of C-terminal variable region and N-terminal variable region are catalytically active, thereby indicating that the two regions are not essential for the catalytic activity, mutant structures compared to the wild-type enzyme, overview
additional information
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generation of five truncated SmDexs by deleting the N-terminal variable region, the glucan-binding site, or the C-terminal variable region. Two truncation-mutant enzymes devoid of C-terminal variable region or of C-terminal variable region and N-terminal variable region are catalytically active, thereby indicating that the two regions are not essential for the catalytic activity, mutant structures compared to the wild-type enzyme, overview
additional information
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generation of five truncated SmDexs by deleting the N-terminal variable region, the glucan-binding site, or the C-terminal variable region. Two truncation-mutant enzymes devoid of C-terminal variable region or of C-terminal variable region and N-terminal variable region are catalytically active, thereby indicating that the two regions are not essential for the catalytic activity, mutant structures compared to the wild-type enzyme, overview
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