2.4.1.19: cyclomaltodextrin glucanotransferase
This is an abbreviated version!
For detailed information about cyclomaltodextrin glucanotransferase, go to the full flat file.
Word Map on EC 2.4.1.19
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2.4.1.19
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cyclodextrins
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cgtases
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starch
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synthesis
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transglycosylation
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circulans
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cyclization
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glucosylated
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glucoamylase
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paenibacillus
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nutrition
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beta-cyclodextrins
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alkalophilic
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gamma-cyclodextrins
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beta-cds
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alpha-amylases
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maltooligosaccharides
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stearothermophilus
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disproportionation
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amylose
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maltodextrins
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gamma-cds
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industry
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starch-degrading
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maltohexaose
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starch-binding
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amylopectin
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amylolytic
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cyclomaltohexaose
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agriculture
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alpha-cd
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maltopentaose
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food industry
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pharmacology
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thermoanaerobacter
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maltotetraose
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maltotriose
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beta-amylase
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amyloglucosidase
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pullulanase
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alpha-1,4-glucans
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thermosulfurigenes
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acarbose
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thermoanaerobacterium
- 2.4.1.19
- cyclodextrins
- cgtases
- starch
- synthesis
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transglycosylation
- circulans
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cyclization
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glucosylated
- glucoamylase
- paenibacillus
- nutrition
- beta-cyclodextrins
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alkalophilic
- gamma-cyclodextrins
- beta-cds
- alpha-amylases
- maltooligosaccharides
- stearothermophilus
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disproportionation
- amylose
- maltodextrins
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gamma-cds
- industry
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starch-degrading
- maltohexaose
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starch-binding
- amylopectin
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amylolytic
- cyclomaltohexaose
- agriculture
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alpha-cd
- maltopentaose
- food industry
- pharmacology
- thermoanaerobacter
- maltotetraose
- maltotriose
- beta-amylase
- amyloglucosidase
- pullulanase
- alpha-1,4-glucans
- thermosulfurigenes
- acarbose
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thermoanaerobacterium
Reaction
Synonyms
1,4-alpha-D-glucopyranosyl transferase, Akrilex C cyclodextrin glycosyltransferase, alpha-1,4-glucan 4-glycosyltransferase, cyclizing, alpha-cgt, alpha-CGTase, alpha-cyclodextrin glucanotransferase, alpha-cyclodextrin glucosyltransferase, alpha-cyclodextrin glycosyltransferase, Bacillus macerans amylase, beta-CGTase, beta-cyclodextrin glucanotransferase, beta-cyclodextrin glucosyltransferase, beta-cyclodextrin glycosyltransferase, beta-cyclodextrinase, BMA, C-CGTase, CD glucanotransferase, CGT, CGT13, CGTase, cgtS, CGTse ET1, CGT_TK, cyclodextrin beta-glucanotransferase, cyclodextrin glucanotransferase, cyclodextrin glucosyltransferase, cyclodextrin glycosyl transferase, cyclodextrin glycosyltransferase, cyclodextrin-glycosyltransferase, cyclodextrinase, cyclomaltodextrin glucanyltransferase, cyclomaltodextrin glucotransferase, cyclomaltodextrin glycanotransferase, cyclomaltodextrin glycosyltransferase, gamma-CGTase, gamma-cyclodextrin glycosyltransferase, konchizaimu, M-CGTase, More, neutral-cyclodextrin glycosyltransferase, PFCGT, Toruzyme
ECTree
2.4.1.19 cyclomaltodextrin glucanotransferaseAdvanced search results
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results (Metals Ions
Metals Ions on EC 2.4.1.19 - cyclomaltodextrin glucanotransferase
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METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Ba2+
Ca2+
CaCl2
Co2+
Cu2+
Fe2+
FeCl2
K+
Mg2+
Mn2+
Na+
Zn2+
additional information
Ca2+
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the highest increase in beta-CGTase activity is 54.3% at 1 mM CaCl2 which is 5.6fold higher than that of the control. The highest increase in gamma-CGTase activity is 55.5% 1 mM CaCl2 which is 7.2fold higher than that of the control
Ca2+
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thermal stability is remarkably increased by addition of calcium ions
Ca2+
thermal stability is remarkably increased by addition of calcium ions
Ca2+
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thermal stability is remarkably increased by addition of calcium ions
Ca2+
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the enzyme has three Ca2+ binding sites. Ca2+ has a small contribution to the enzyme's thermostability
Ca2+
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synergistic promoting effects of glycine and Ca2+ on the extracellular secretion of the recombinant protein in Escherichia coli, optimal at 150 mM and 20 mM, respectively, overview
Ca2+
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the enzyme has two Ca2+ binding sites. Ca2+ has a small contribution to the enzyme's thermostability
Ca2+
thermal stability is remarkably increased by addition of calcium ions
Ca2+
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contains 2 mol Ca2+ per mol of enzyme, increases heat stability, denaturation temperature shifted from 70°C to 88°C
CaCl2
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5 mM, 20% activation of cross-linked enzyme crystals, 2% activation of soluble enzyme
FeCl2
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5 mM, 110% activation of cross-linked enzyme crystals, inhibition of soluble enzyme
Mg2+
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the highest increase in beta-CGTase activity is 46.4% at 2 mM MgSO4 which is 4.8fold higher than that of the control. The highest increase in gamma-CGTase activity is 45.9% at 3 mM MgSO4 which is 5.9fold higher than that of the control
Mg2+
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the enzymatic activity increases to 104.1% in the presence of 5 mM MgCl2
Mn2+
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the enzymatic activity increases to 104.1% in the presence of 5 mM MnCl2
additional information
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Ni2+ and Na+ ions have weak effects on the enzyme activity
additional information
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enzyme activity is not affected by Ca2+, Na+, K+, Fe3+, ICH2COOH, and SDS at low concentration
