2.4.1.248: cycloisomaltooligosaccharide glucanotransferase
This is an abbreviated version!
For detailed information about cycloisomaltooligosaccharide glucanotransferase, go to the full flat file.
Word Map on EC 2.4.1.248
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2.4.1.248
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dextran
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circulans
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glycoside
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polymerization
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cyclization
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carbohydrate-binding
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isomaltooligosaccharides
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paenibacillus
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transglucosylation
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starch
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synthesis
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subsite
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alpha-1,6-linkage
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maltooligosaccharides
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isomaltotetraose
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transglutaminase
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dextranolytic
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amylose
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hollow-fiber
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isomaltose
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dextranases
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thermoanaerobacter
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porous
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sugar-binding
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disproportionation
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multilayer
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mutans
- 2.4.1.248
- dextran
- circulans
- glycoside
- polymerization
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cyclization
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carbohydrate-binding
- isomaltooligosaccharides
- paenibacillus
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transglucosylation
- starch
- synthesis
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subsite
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alpha-1,6-linkage
- maltooligosaccharides
- isomaltotetraose
- transglutaminase
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dextranolytic
- amylose
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hollow-fiber
- isomaltose
- dextranases
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thermoanaerobacter
-
porous
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sugar-binding
-
disproportionation
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multilayer
- mutans
Reaction
cyclizes part of a (1->6)-alpha-D-glucan chain by formation of a (1->6)-alpha-D-glucosidic bond =
Synonyms
cit, CITase, CITase-598K, CITase-T3040, isocyclomaltooligosaccharide glucanotransferase
ECTree
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Engineering
Engineering on EC 2.4.1.248 - cycloisomaltooligosaccharide glucanotransferase
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A452N
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3fold increase in reaction velocity, 9fold increase in Km value. Activation by Ca2+ and inactivation by Cu2+ are reduced
F268V/D469Y/A513V/Y515S
mutant produces three times as much megalo-cycloisomaltooligosaccharides (10-12 glucose units) and 1.5 times as much total cycloisomaltooligosaccharides (7-12 glucose units) as compared with the wild-type. The modified product size specificity is attributable to the construction of novel substrate-binding sites in the B-2 substrate-binding site and reactivity is improved by mutation on subsite -3 on the catalytic domain
V744L
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2fold increase in reaction velocity, 3fold increase in Km value. Activation by Ca2+ and inactivation by Cu2+ are reduced
A452N
Niallia circulans T-3040
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3fold increase in reaction velocity, 9fold increase in Km value. Activation by Ca2+ and inactivation by Cu2+ are reduced
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F268V/D469Y/A513V/Y515S
Niallia circulans T-3040
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mutant produces three times as much megalo-cycloisomaltooligosaccharides (10-12 glucose units) and 1.5 times as much total cycloisomaltooligosaccharides (7-12 glucose units) as compared with the wild-type. The modified product size specificity is attributable to the construction of novel substrate-binding sites in the B-2 substrate-binding site and reactivity is improved by mutation on subsite -3 on the catalytic domain
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V744L
Niallia circulans T-3040
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2fold increase in reaction velocity, 3fold increase in Km value. Activation by Ca2+ and inactivation by Cu2+ are reduced
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D144A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
D144N
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
D264A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D662A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E341Q
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
additional information
construction of CITase deletion mutants, 15 deletion mutant enzymes. M123DELTA (R4-deleted), MDELTA234 (R1-deleted), and MDELTA23DELTA (R1/R4-deleted) catalyze cycloisomaltooligosaccharide synthesis, but other mutants are inactive. M123DELTA, MDELTA234, and MDELTA23DELTA increase their Km values against dextran 40. The wild-type enzyme and M123DELTA produced cycloisomaltooligosaccharide-8 predominantly, but MDELTA234 and MDELTA23DELTA lose cycloisomaltooligosaccharide-8 production specificity. The kcat values of MDELTA234 and MDELTA23DELTA decrease, and these mutants show narrowed temperature and pH stability ranges, product size distribution of mutants, overview
additional information
utational studies show that substrate-binding sites B-1 and B-2 contribute to recruiting substrate and maintaining product size respectively
additional information
Niallia circulans T-3040
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construction of CITase deletion mutants, 15 deletion mutant enzymes. M123DELTA (R4-deleted), MDELTA234 (R1-deleted), and MDELTA23DELTA (R1/R4-deleted) catalyze cycloisomaltooligosaccharide synthesis, but other mutants are inactive. M123DELTA, MDELTA234, and MDELTA23DELTA increase their Km values against dextran 40. The wild-type enzyme and M123DELTA produced cycloisomaltooligosaccharide-8 predominantly, but MDELTA234 and MDELTA23DELTA lose cycloisomaltooligosaccharide-8 production specificity. The kcat values of MDELTA234 and MDELTA23DELTA decrease, and these mutants show narrowed temperature and pH stability ranges, product size distribution of mutants, overview
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additional information
Niallia circulans T-3040
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utational studies show that substrate-binding sites B-1 and B-2 contribute to recruiting substrate and maintaining product size respectively
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