3.2.1.54: cyclomaltodextrinase
This is an abbreviated version!
For detailed information about cyclomaltodextrinase, go to the full flat file.
Word Map on EC 3.2.1.54
-
3.2.1.54
-
starch
-
cyclodextrins
-
maltose
-
maltodextrins
-
ceramidase
-
neopullulanase
-
transglycosylation
-
thermoactinomyces
-
alpha-amylases
-
maltogenic
-
maltotriose
-
glucanotransferase
-
amylolytic
-
acarbose
-
amylases
-
maltoheptaose
-
malto-oligosaccharides
-
cgtases
-
cyclomaltodextrins
-
maltotetraose
-
panose
-
beta-cd
-
alkalophilic
-
amylomaltase
-
alpha-cd
-
anoxybacillus
-
biotechnology
-
synthesis
-
food industry
-
analysis
- 3.2.1.54
- starch
- cyclodextrins
- maltose
- maltodextrins
- ceramidase
- neopullulanase
-
transglycosylation
-
thermoactinomyces
- alpha-amylases
-
maltogenic
- maltotriose
-
glucanotransferase
-
amylolytic
- acarbose
- amylases
- maltoheptaose
- malto-oligosaccharides
- cgtases
- cyclomaltodextrins
- maltotetraose
- panose
- beta-cd
-
alkalophilic
- amylomaltase
-
alpha-cd
- anoxybacillus
- biotechnology
- synthesis
- food industry
- analysis
Reaction
Synonyms
AfCda13, AglB, alpha-amylase, alpha-amylase II, CD-/pullulan-hydrolyzing enzyme, CD-ase, CD-degrading enzyme, CD-hydrolyzing amylase, CDA, CDase, CDase I-5, CMD, cyclodextrinase, cycloheptaglucanase, cyclohexaglucanase, cyclomaltodextrin dextrin-hydrolase, Cyclomaltodextrin hydrolase, decycling, cyclomaltodextrinase, CymH, cytoplasmic decycling maltodextrinase, EC 3.2.1.12, Env cda13A, FspCMD, H-17 CDase, H-17 thermostable CDase, LLCD, LsCda13, Lsp26X-Mdase, maltodextrin glucosidase, More, neopullulanase, PFTA, RA.04, thermophilic CDase, TK1770, TVA II
ECTree
Advanced search results
Reaction
Reaction on EC 3.2.1.54 - cyclomaltodextrinase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
cyclomaltodextrin + H2O = linear maltodextrin
active site structure
cyclomaltodextrin + H2O = linear maltodextrin
also hydrolyses linear maltodextrin, model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors
-
cyclomaltodextrin + H2O = linear maltodextrin
model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, catalytically important residues are Asp325, Glu354, and Asp421, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors
-
cyclomaltodextrin + H2O = linear maltodextrin
model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors
-
cyclomaltodextrin + H2O = linear maltodextrin
model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors
-
cyclomaltodextrin + H2O = linear maltodextrin
model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors
-
cyclomaltodextrin + H2O = linear maltodextrin
model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors
-
cyclomaltodextrin + H2O = linear maltodextrin
model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors
-
cyclomaltodextrin + H2O = linear maltodextrin
model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors
-
cyclomaltodextrin + H2O = linear maltodextrin
model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors
-
cyclomaltodextrin + H2O = linear maltodextrin
model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors
-
cyclomaltodextrin + H2O = linear maltodextrin
model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors
-
cyclomaltodextrin + H2O = linear maltodextrin
model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors
-
cyclomaltodextrin + H2O = linear maltodextrin
model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors
-
cyclomaltodextrin + H2O = linear maltodextrin
PFTA is a bifunctional enzyme showing alpha-amylase as well as cyclodextrin-hydrolyzing activity
-
cyclomaltodextrin + H2O = linear maltodextrin
TVA II is a bifunctional enzyme showing alpha-amylase as well as cyclodextrin-hydrolyzing activity, the enzyme hydrolyzes alpha-1,4-glucosidic linkages and alpha-1,6-glucosidic linkages, active site structure and substrate binding structure, Trp356 is involved in substrate binding, and Tyr374 is involved in substrate orientation for catalysis
-
cyclomaltodextrin + H2O = linear maltodextrin
model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors
-
-
cyclomaltodextrin + H2O = linear maltodextrin
model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, catalytically important residues are Asp325, Glu354, and Asp421, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors
-
-
cyclomaltodextrin + H2O = linear maltodextrin
TVA II is a bifunctional enzyme showing alpha-amylase as well as cyclodextrin-hydrolyzing activity, the enzyme hydrolyzes alpha-1,4-glucosidic linkages and alpha-1,6-glucosidic linkages, active site structure and substrate binding structure, Trp356 is involved in substrate binding, and Tyr374 is involved in substrate orientation for catalysis
-
-
cyclomaltodextrin + H2O = linear maltodextrin
model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors
-
-
cyclomaltodextrin + H2O = linear maltodextrin
model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors
-
-
cyclomaltodextrin + H2O = linear maltodextrin
model of coupled hydrolysis and transglycosylation catalyzed by cyclodextrin-degrading enzymes, catalytic mechanism of double-displacement reaction, active site cleft structure, conserved Glu332 plays an important role in the binding of oligosaccharide acceptors
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
-