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
-
cyclization
-
carbohydrate-binding
- isomaltooligosaccharides
- paenibacillus
-
transglucosylation
- starch
- synthesis
-
subsite
-
alpha-1,6-linkage
- maltooligosaccharides
- isomaltotetraose
- transglutaminase
-
dextranolytic
- amylose
-
hollow-fiber
- isomaltose
- dextranases
-
thermoanaerobacter
-
porous
-
sugar-binding
-
disproportionation
-
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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Inhibitors
Inhibitors on EC 2.4.1.248 - cycloisomaltooligosaccharide glucanotransferase
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1-ethyl-3-[(3-dimethylamino)propyl]carbodiimide
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inactivation o both wild-type and mutants A452N and V744L, inactivation is reduced in presence of 10 mM Ca2+
additional information
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activity of free enzyme is not influenced by NaCl up to 5 M. The activity of enzyme immobilized on Chitopearl BCW-3505 is not influenced by NaCl up to 2 M
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inactivation. In mutants A452N and V744L, inactivation by Cu2+ is reduced