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
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porous
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sugar-binding
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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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General Information on EC 2.4.1.248 - cycloisomaltooligosaccharide glucanotransferase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
malfunction
physiological function
additional information
catalytically important residues of CITase-598K are Asp144, Asp269, and Glu341
evolution
CITase is a member of the glycoside hydrolase family 66, GH66
evolution
CITase is a member of the glycoside hydrolase family 66, GH66
evolution
Niallia circulans T-3040
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CITase is a member of the glycoside hydrolase family 66, GH66
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malfunction
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
malfunction
Niallia circulans T-3040
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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
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physiological function
CITase production is induced by dextran 40, isomaltose, isomaltotriose, and panose, and soluble starch but not by G67 or dextrin, which suggests that alpha-1,6 glucosidic linkages are required for CITase induction. Although CITase is induced by isomaltose, isomaltotriose, and panose, no cyclodextrans are produced in the culture. Cyclodextran-producing activity in the presence of soluble starch as the substrate is observed only in cultures containing dextran 40 or soluble starch. The production of CITase is significantly unaffected by glucose addition, but soluble starch-CITase activity almost completely disappears after glucose addition. A 135-kDa protein contributes to cyclodextran formation from starch in the presence of CITase
physiological function
Niallia circulans T-3040
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CITase production is induced by dextran 40, isomaltose, isomaltotriose, and panose, and soluble starch but not by G67 or dextrin, which suggests that alpha-1,6 glucosidic linkages are required for CITase induction. Although CITase is induced by isomaltose, isomaltotriose, and panose, no cyclodextrans are produced in the culture. Cyclodextran-producing activity in the presence of soluble starch as the substrate is observed only in cultures containing dextran 40 or soluble starch. The production of CITase is significantly unaffected by glucose addition, but soluble starch-CITase activity almost completely disappears after glucose addition. A 135-kDa protein contributes to cyclodextran formation from starch in the presence of CITase
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