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
Subunits
Subunits 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.
dimer
dodecamer
homotetramer
monomer
octamer
oligomer
tetramer
additional information
dimer
2 * 71000, at pH 6.5, the enzyme exiosts mainly as dimer, SDS-PAGE
dimer
-
2 * 71000, at pH 6.5, the enzyme exiosts mainly as dimer, SDS-PAGE
dimer
-
2 * 67000, molecular weight estimated to be 126000 by gel filtration, 67000 by SDS-PAGE
-
dodecameric assembly of 6 copies of the dimer, most active form
dodecamer
-
exists exclusively as dodecamer at pH 7.0, forming an assembly of six 3D domain-swapped dimeric subunit. At pH 5.0-6.0 the enzyme is present as a dimer. Above pH 6.5 the dodecameric form is predominant. No dissociation of the dodecamer at pH 7.0 and above. Dissociation of wild-type CDase I-5 proceeds very fast at pH 7.0 in presence of 0.2-1.0 M of KCl. The mutant enzyme H49V/H89V/H539V dissociates into dimers faster than the wild-type enzyme at both pH 6.0 and 7.0
dodecamer
-
exists exclusively as dodecamer at pH 7.0, forming an assembly of six 3D domain-swapped dimeric subunit. At pH 5.0-6.0 the enzyme is present as a dimer. Above pH 6.5 the dodecameric form is predominant. No dissociation of the dodecamer at pH 7.0 and above. Dissociation of wild-type CDase I-5 proceeds very fast at pH 7.0 in presence of 0.2-1.0 M of KCl. The mutant enzyme H49V/H89V/H539V dissociates into dimers faster than the wild-type enzyme at both pH 6.0 and 7.0
-
monomer
1 * 65000, recombinant His6-tagged enzyme, SDS-PAGE and gel filtration, 1 * 75956, sequence calculation
monomer
-
1 * 65000, recombinant His6-tagged enzyme, SDS-PAGE and gel filtration, 1 * 75956, sequence calculation
-
-
multidomain (alphabeta)8 barrel structure, scheme of dimeric enzyme in transglycosylation mode, transglycosylation is best performed in the dimeric statethe oligomeric state of the enzyme in vitro depends on the protein concentration and the type of added salt
additional information
-
multidomain (alphabeta)8 barrel structure, scheme of dimeric enzyme in transglycosylation mode, transglycosylation is best performed in the dimeric state, the oligomeric state of the enzyme in vitro depends on the protein concentration and the type of added salt
additional information
-
pH-dependent association and dissociation of the enzyme dimeric units, structure determination and analysis, enzyme has a beta-stranded N-terminal domain, residues 1-123, a central (alphabeta)8 barrel domain, and a beta-stranded C-terminal domain, residues 505-583
additional information
-
multidomain (alphabeta)8 barrel structure, the oligomeric state of the enzyme in vitro depends on the protein concentration and the type of added salt
additional information
-
multidomain (alphabeta)8 barrel structure, the oligomeric state of the enzyme in vitro depends on the protein concentration and the type of added salt
additional information
-
multidomain (alphabeta)8 barrel structure, scheme of dimeric enzyme in transglycosylation mode, transglycosylation is best performed in the dimeric state
additional information
-
multidomain (alphabeta)8 barrel structure
additional information
-
multidomain (alphabeta)8 barrel structure
-
additional information
-
multidomain (alphabeta)8 barrel structure, the oligomeric state of the enzyme in vitro depends on the protein concentration and the type of added salt
additional information
-
multidomain (alphabeta)8 barrel structure, the oligomeric state of the enzyme in vitro depends on the protein concentration and the type of added salt
-
additional information
-
multidomain (alphabeta)8 barrel structure, the oligomeric state of the enzyme in vitro depends on the protein concentration and the type of added salt
additional information
-
multidomain (alphabeta)8 barrel structure, scheme of dimeric enzyme in transglycosylation mode, transglycosylation is best performed in the dimeric state, the oligomeric state of the enzyme in vitro depends on the protein concentration and the type of added salt
additional information
-
multidomain (alphabeta)8 barrel structure
additional information
-
multidomain (alphabeta)8 barrel structure
-
additional information
-
multidomain (alphabeta)8 barrel structure, no N-terminal domain, the oligomeric state of the enzyme in vitro depends on the protein concentration and the type of added salt
additional information
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
multidomain (alphabeta)8 barrel structure, no N-terminal domain, the oligomeric state of the enzyme in vitro depends on the protein concentration and the type of added salt
-
additional information
-
multidomain (alphabeta)8 barrel structure, the oligomeric state of the enzyme in vitro depends on the protein concentration and the type of added salt
additional information
-
multidomain (alphabeta)8 barrel structure, the oligomeric state of the enzyme in vitro depends on the protein concentration and the type of added salt
additional information
-
multidomain (alphabeta)8 barrel structure, the oligomeric state of the enzyme in vitro depends on the protein concentration and the type of added salt
-