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Information on EC 3.2.1.54 - cyclomaltodextrinase
for references in articles please use BRENDA:EC3.2.1.54
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EC Tree 3 Hydrolases
3.2 Glycosylases
3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
3.2.1.54 cyclomaltodextrinase
IUBMB Comments
Also hydrolyses linear maltodextrin.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 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
showSynonyms
cdase, cyclomaltodextrinase, tva ii, cyclodextrinase, maltodextrin glucosidase, alpha-amylase ii, cdase i-5, ra.04, tk1770, env cda13a, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AfCda13
alpha-amylase
alpha-amylase II
CD-/pullulan-hydrolyzing enzyme
CD-ase
-
-
-
-
CDA
CDase
CDase I-5
cyclodextrinase
cycloheptaglucanase
cyclohexaglucanase
cyclomaltodextrin dextrin-hydrolase
-
-
-
-
Cyclomaltodextrin hydrolase, decycling
-
-
-
-
cyclomaltodextrinase
CymH
EC 3.2.1.12
-
-
formerly
-
LLCD
neopullulanase
PFTA
thermophilic CDase
TK1770
TVA II
CDase
CDase
-
-
-
-
cyclodextrinase
-
-
-
-
cycloheptaglucanase
-
-
-
-
cyclohexaglucanase
-
-
-
-
additional information
-
the enzyme belongs to the alpha-amylase family of enzymes
additional information
-
the enzyme belongs to the alpha-amylase family of enzymes
additional information
-
the enzyme belongs to the alpha-amylase family of enzymes
additional information
-
the enzyme belongs to the alpha-amylase family of enzymes
additional information
-
the enzyme belongs to the alpha-amylase family of enzymes
additional information
enzyme belongs to the glycosylhydrolase family 13
additional information
-
the enzyme belongs to the alpha-amylase family of enzymes
additional information
-
the enzyme belongs to the alpha-amylase family of enzymes
-
additional information
-
the enzyme belongs to the alpha-amylase family of enzymes
additional information
-
the enzyme belongs to the alpha-amylase family of enzymes
additional information
-
the enzyme belongs to the alpha-amylase family of enzymes
-
additional information
-
the enzyme belongs to the alpha-amylase family of enzymes
additional information
-
the enzyme belongs to the alpha-amylase family of enzymes
additional information
-
cf. EC 3.2.1.1, alpha-amylase, the enzyme belongs to glycoside hydrolase family 13
additional information
-
the enzyme belongs to the alpha-amylase family of enzymes
additional information
-
the enzyme belongs to the alpha-amylase family of enzymes
-
additional information
-
the enzyme belongs to the alpha-amylase family of enzymes
additional information
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
the enzyme belongs to the alpha-amylase family of enzymes
-
additional information
-
the enzyme belongs to the alpha-amylase family of enzymes
additional information
-
the enzyme belongs to the alpha-amylase family of enzymes
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cyclomaltodextrin + H2O = linear maltodextrin
-
-
-
-
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, 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
active site structure
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
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
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
PFTA is a bifunctional enzyme showing alpha-amylase as well as cyclodextrin-hydrolyzing activity
-
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
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, 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
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
-
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
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
hydrolysis of O-glycosyl bond
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
starch degradation III, starch degradation IV
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SYSTEMATIC NAME
IUBMB Comments
cyclomaltodextrin dextrin-hydrolase (decyclizing)
Also hydrolyses linear maltodextrin.
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CAS REGISTRY NUMBER
COMMENTARY
37288-41-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl-alpha-D-maltohexaoside + H2O
4-nitrophenol + maltohexaose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-D-maltopentaoside + H2O
4-nitrophenol + alpha-D-maltopentaoside
-
Substrates: -
Products: -
Products: -
?
acarbose + H2O
acarviosine-glucose + alpha-D-glucose
-
Substrates: -
Products: -
Products: -
?
alpha-cyclodextrin + H2O
maltohexaose
-
Substrates: highest activity. The enzyme shows strongest preference towards alpha-and beta-cyclodextrin
Products: -
Products: -
?
amylose + H2O
maltose + glucose
-
Substrates: CDase I-5 shows high preference towards amylose
Products: major hydrolysis products
Products: major hydrolysis products
?
beta-cyclodextrin + H2O
D-glucose + ?
Substrates: beta-cyclodextrin is the most active substrate
Products: -
Products: -
?
beta-cyclodextrin + H2O
maltoheptaose
-
Substrates: strongest preference towards alpha-and beta-cyclodextrin
Products: -
Products: -
?
beta-cyclodextrin + H2O
maltose + maltotriose + maltotetraose + maltopentaose + maltoheptaose + glucose
beta-cyclodextrin + H2O
panose + maltoheptaose
-
Substrates: cyclomaltodextrinase activity
Products: -
Products: -
?
branched cyclodextrins + H2O
glucose + maltose
-
Substrates: -
Products: -
Products: -
?
cyclodextrin + H2O
panose + maltoheptaose
-
Substrates: cyclomaltodextrinase activity, hydrolysis of alpha-1,4-glucosidic linkages
Products: -
Products: -
?
cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
dextrin + H2O
?
-
Substrates: 29% of the activity with beta-cyclodextrin
Products: -
Products: -
?
G1-alpha-cyclodextrin + H2O
D-glucose + maltose
-
Substrates: 24% of the activity with beta-cyclodextrin
Products: main products
Products: main products
?
G2-alpha-cyclodextrin + H2O
D-glucose + maltose
-
Substrates: 19% of the activity with beta-cyclodextrin
Products: main products
Products: main products
?
G2-beta-cyclodextrin + H2O
D-glucose + maltose
-
Substrates: 30% of the activity with beta-cyclodextrin
Products: main products
Products: main products
?
gamma-cyclodextrin + H2O
D-glucose + ?
Substrates: hydrolyzing activity is about 20% compared to the activity with beta-cyclodextrin
Products: -
Products: -
?
gamma-cyclodextrin + H2O
glucose + maltose + maltotriose + maltotetraose + maltopentaose + maltohexaose + maltoheptaose + maltooctaose
gamma-cyclodextrin + H2O
maltotriose + maltotetraose
-
Substrates: main products: maltotriose and maltotetraose
Products: -
Products: -
?
linear maltoheptaose + H2O
alpha-D-glucose + maltose
-
Substrates: -
Products: -
Products: -
?
linear maltohexaose + H2O
alpha-D-glucose + maltose
-
Substrates: -
Products: -
Products: -
?
linear maltooctaose + H2O
alpha-D-glucose + maltose
-
Substrates: -
Products: -
Products: -
?
maltodextrin + H2O
D-glucose + maltose
WP_000471779.1, Q819G8
Substrates: about 30% of the activity with alpha-cyclodextrin
Products: -
Products: -
?
maltoheptaose + H2O
maltose + D-glucose + ?
-
Substrates: 24% of the activity with gamma-cyclodextrin
Products: -
Products: -
?
maltoheptaose + H2O
maltotetraose + maltotriose
-
Substrates: -
Products: -
Products: -
?
maltohexaose + H2O
?
-
Substrates: 33% of the activity with beta-cyclodextrin
Products: -
Products: -
?
maltohexaose + H2O
maltose + D-glucose + ?
-
Substrates: 14% of the activity with gamma-cyclodextrin
Products: -
Products: -
?
maltooligosaccharides + H2O
maltotriose + maltotetraose
-
Substrates: alpha-amylase activity
Products: main products
Products: main products
?
maltopentaose + H2O
?
-
Substrates: 18% of the activity with beta-cyclodextrin
Products: -
Products: -
?
maltopentaose + H2O
D-glucose + maltose + ?
-
Substrates: 22% of the activity with beta-cyclodextrin
Products: -
Products: -
?
maltopentaose + H2O
maltose + D-glucose + ?
-
Substrates: 11% of the activity with gamma-cyclodextrin
Products: -
Products: -
?
maltotetraose + H2O
?
-
Substrates: 12% of the activity with beta-cyclodextrin
Products: -
Products: -
?
maltotetraose + H2O
maltose + 2 D-glucose
-
Substrates: 6% of the activity with gamma-cyclodextrin
Products: -
Products: -
?
p-nitrophenyl-D-maltopentaoside + H2O
p-nitrophenol + maltopentaose
-
Substrates: -
Products: -
Products: -
?
pullulan + H2O
branched pullulan tetrasaccharide
-
Substrates: substrate is a linear polysaccharide composed of maltotriose units linked by alpha-1,6-bonds, low activity
Products: main products
Products: main products
?
pullulan + H2O
D-glucose + ?
Substrates: hydrolyzing activity is about 20% compared to the activity with beta-cyclodextrin
Products: -
Products: -
?
pullulan + H2O
glucose + panose + isopanose + large saccharides containing alpha 1,6-glucosidic bonds
pullulan + H2O
panose + ?
-
Substrates: cyclomaltodextrinase activity, hydrolysis of alpha-1,4-glucosidic linkages
Products: -
Products: -
?
pullulan + H2O
panose + maltoheptaose
-
Substrates: cyclomaltodextrinase activity
Products: -
Products: -
?
starch + H2O
D-glucose + maltose
WP_000471779.1, Q819G8
Substrates: about 40% of the activity with alpha-cyclodextrin
Products: -
Products: -
?
starch + H2O
maltooligosaccharides
-
Substrates: alpha-amylase activity, preferred substrate, hydrolysis of alpha-1,4-glucosidic linkages
Products: -
Products: -
?
starch + H2O
maltotriose + maltotetraose
-
Substrates: alpha-amylase activity, preferred substrate
Products: main products
Products: main products
?
6-O-alpha-D-glucosyl-alpha-cyclodextrin + H2O
isomaltooligosaccharides
Substrates: branched cyclodextrin
Products: -
Products: -
?
6-O-alpha-D-glucosyl-alpha-cyclodextrin + H2O
isomaltooligosaccharides
Substrates: branched cyclodextrin
Products: -
Products: -
?
6-O-alpha-D-glucosyl-beta-cyclodextrin + H2O
isomaltooligosaccharides
Substrates: branched cyclodextrin
Products: -
Products: -
?
6-O-alpha-D-glucosyl-beta-cyclodextrin + H2O
isomaltooligosaccharides
Substrates: branched cyclodextrin
Products: -
Products: -
?
6-O-alpha-D-maltosyl-beta-cyclodextrin + H2O
isomaltooligosaccharides
Substrates: branched cyclodextrin
Products: -
Products: -
?
6-O-alpha-D-maltosyl-beta-cyclodextrin + H2O
isomaltooligosaccharides
Substrates: branched cyclodextrin
Products: -
Products: -
?
acarbose + H2O
?
-
Substrates: pseudotetrasaccharide inhibitor of glucosidases and alpha-amylases, binding the active sites of the enzyme
Products: -
Products: -
?
acarbose + H2O
?
-
Substrates: substrate is a pseudotetrasaccharide and potent inhibitor of glucosidases
Products: -
Products: -
?
acarbose + H2O
?
-
Substrates: pseudotetrasaccharide inhibitor of glucosidases and alpha-amylases, binding the active sites of the enzyme
Products: -
Products: -
?
acarbose + H2O
?
-
Substrates: the substrate is a potent inhibitor of alpha-amylases, cyclomaltodextrinase activity
Products: -
Products: -
?
acarbose + H2O
?
-
Substrates: substrate is a pseudotetrasaccharide and potent inhibitor of glucosidases
Products: -
Products: -
?
alpha-cyclodextrin
maltotriose + maltose + glucose
-
Substrates: -
Products: -
Products: -
?
alpha-cyclodextrin
maltotriose + maltose + glucose
-
Substrates: -
Products: -
Products: -
?
alpha-cyclodextrin + H2O
?
Substrates: -
Products: -
Products: -
?
alpha-cyclodextrin + H2O
?
Substrates: -
Products: -
Products: -
?
alpha-cyclodextrin + H2O
?
Substrates: higher affinity for alpha-cyclodextrin followed by beta-cyclodextrin and then gamma-cyclodextrin
Products: -
Products: -
?
alpha-cyclodextrin + H2O
?
Substrates: higher affinity for alpha-cyclodextrin followed by beta-cyclodextrin and then gamma-cyclodextrin
Products: -
Products: -
?
alpha-cyclodextrin + H2O
?
-
Substrates: cyclomaltodextrinase activity
Products: -
Products: -
?
alpha-cyclodextrin + H2O
D-glucose + maltose
Substrates: preferred substrate. As compared with the dimer protein, the monomeric enzyme retains only 23% of the specific activity
Products: + maltotriose + maltotetraose + maltoheptaose at lower amounts
Products: + maltotriose + maltotetraose + maltoheptaose at lower amounts
?
alpha-cyclodextrin + H2O
D-glucose + maltose
-
Substrates: -
Products: -
Products: -
?
alpha-cyclodextrin + H2O
D-glucose + maltose
-
Substrates: 57% of the activity with beta-cyclodextrin
Products: + less amounts of maltotriose and maltotetraose
Products: + less amounts of maltotriose and maltotetraose
?
alpha-cyclodextrin + H2O
D-glucose + maltose
-
Substrates: 53% of the activity with beta-cyclodextrin
Products: main products
Products: main products
?
alpha-cyclodextrin + H2O
D-glucose + maltose
-
Substrates: 57% of the activity with beta-cyclodextrin
Products: + less amounts of maltotriose and maltotetraose
Products: + less amounts of maltotriose and maltotetraose
?
alpha-cyclodextrin + H2O
D-glucose + maltose
-
Substrates: 53% of the activity with beta-cyclodextrin
Products: main products
Products: main products
?
alpha-cyclodextrin + H2O
glucose + maltose + maltotriose
-
Substrates: -
Products: -
Products: -
?
alpha-cyclodextrin + H2O
glucose + maltose + maltotriose
-
Substrates: -
Products: -
Products: -
?
alpha-cyclodextrin + H2O
glucose + maltose + maltotriose
-
Substrates: -
Products: -
Products: -
?
alpha-cyclodextrin + H2O
glucose + maltose + maltotriose
-
Substrates: -
Products: -
Products: -
?
alpha-cyclodextrin + H2O
isomaltooligosaccharides
Substrates: -
Products: -
Products: -
?
alpha-cyclodextrin + H2O
isomaltooligosaccharides
Substrates: -
Products: mainly D-glucose and maltose
Products: mainly D-glucose and maltose
?
alpha-cyclodextrin + H2O
isomaltooligosaccharides
Substrates: -
Products: -
Products: -
?
alpha-cyclodextrin + H2O
isomaltooligosaccharides
Substrates: -
Products: mainly D-glucose and maltose
Products: mainly D-glucose and maltose
?
alpha-cyclodextrin + H2O
linear maltodextrins
-
Substrates: -
Products: -
Products: -
?
alpha-cyclodextrin + H2O
linear maltodextrins
-
Substrates: -
Products: -
Products: -
?
alpha-cyclodextrin + H2O
maltooligosaccharides
-
Substrates: -
Products: maltohexaose, maltoheptaose, maltooctaose
Products: maltohexaose, maltoheptaose, maltooctaose
?
alpha-cyclodextrin + H2O
maltooligosaccharides
-
Substrates: -
Products: maltohexaose, maltoheptaose, maltooctaose
Products: maltohexaose, maltoheptaose, maltooctaose
?
alpha-cyclodextrin + H2O
maltooligosaccharides
-
Substrates: -
Products: maltohexaose, maltoheptaose, maltooctaose
Products: maltohexaose, maltoheptaose, maltooctaose
?
alpha-cyclodextrin + H2O
maltose + ?
WP_000471779.1, Q819G8
Substrates: the purified enzyme shows substrate preference in the order of alpha-cyclodextrin > beta-cyclodextrin > starch > maltodextrin > gamma-cyclodextrin and hydrolyzes them mainly to maltose
Products: -
Products: -
?
alpha-cyclodextrin + H2O
maltose + ?
Bacillus cereus ATCC 14,579
WP_000471779.1
Substrates: the purified enzyme shows substrate preference in the order of alpha-cyclodextrin > beta-cyclodextrin > starch > maltodextrin > gamma-cyclodextrin and hydrolyzes them mainly to maltose
Products: -
Products: -
?
alpha-cyclodextrin + H2O
maltose + ?
Substrates: -
Products: -
Products: -
?
alpha-cyclodextrin + H2O
maltose + ?
Substrates: -
Products: -
Products: -
?
alpha-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: -
Products: -
Products: -
?
alpha-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: -
Products: -
Products: -
?
alpha-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: -
Products: -
Products: -
?
alpha-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: -
Products: -
Products: -
?
alpha-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: -
Products: -
Products: -
?
alpha-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: -
Products: -
Products: -
?
alpha-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: 65% of the activity with gamma-cyclodextrin
Products: -
Products: -
?
alpha-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: -
Products: -
Products: -
?
alpha-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: -
Products: -
Products: -
?
alpha-cyclodextrin + H2O
maltose + glucose
-
Substrates: -
Products: in an approximate molar ratio of 2 to 1, the intermediate products are analysed using a pulsed amperometric detector for on-line measurements and real-time sampling
Products: in an approximate molar ratio of 2 to 1, the intermediate products are analysed using a pulsed amperometric detector for on-line measurements and real-time sampling
?
alpha-cyclodextrin + H2O
maltose + glucose
Substrates: glucose and maltose are the main products
Products: -
Products: -
?
alpha-cyclodextrin + H2O
maltose + glucose
Substrates: glucose and maltose are the main products
Products: -
Products: -
?
alpha-cyclodextrin + H2O
maltose + glucose
-
Substrates: -
Products: in an approximate molar ratio of 2 to 1, the intermediate products are analysed using a pulsed amperometric detector for on-line measurements and real-time sampling
Products: in an approximate molar ratio of 2 to 1, the intermediate products are analysed using a pulsed amperometric detector for on-line measurements and real-time sampling
?
alpha-cyclodextrin + H2O
maltose + maltotriose
-
Substrates: -
Products: -
Products: -
?
alpha-cyclodextrin + H2O
maltose + maltotriose
-
Substrates: -
Products: -
Products: -
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: -
Products: -
Products: -
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: -
Products: -
Products: -
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: -
Products: -
Products: -
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
Substrates: -
Products: -
Products: -
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: -
Products: -
Products: -
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: -
Products: -
Products: -
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: -
Products: -
Products: -
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: 55% of the activity with beta-cyclomaltodextrin
Products: -
Products: -
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
amylopectin + H2O
maltose + ?
-
Substrates: -
Products: degraded slowly by cleavage of maltose units from the nonreducing ends
Products: degraded slowly by cleavage of maltose units from the nonreducing ends
?
amylopectin + H2O
maltose + ?
-
Substrates: -
Products: -
Products: -
?
amylopectin + H2O
maltose + ?
-
Substrates: -
Products: -
Products: -
?
amylopectin + H2O
maltose + ?
-
Substrates: rate of hydrolysis less than 5% of the rate of alpha-cyclodextrin hydrolysis
Products: -
Products: -
?
amylose + H2O
?
-
Substrates: less than 5% of the rate of alpha-cyclodextrin hydrolysis
Products: -
Products: -
?
amylose + H2O
?
-
Substrates: 53% hydrolysis
Products: -
Products: -
?
amylose + H2O
?
-
Substrates: 53% hydrolysis
Products: -
Products: -
?
beta-cyclodextrin + H2O
?
Substrates: -
Products: -
Products: -
?
beta-cyclodextrin + H2O
?
Substrates: -
Products: -
Products: -
?
beta-cyclodextrin + H2O
?
-
Substrates: -
Products: -
Products: -
?
beta-cyclodextrin + H2O
?
Substrates: higher affinity for alpha-cyclodextrin followed by beta-cyclodextrin and then gamma-cyclodextrin
Products: -
Products: -
?
beta-cyclodextrin + H2O
?
Substrates: higher affinity for alpha-cyclodextrin followed by beta-cyclodextrin and then gamma-cyclodextrin
Products: -
Products: -
?
beta-cyclodextrin + H2O
?
-
Substrates: best substrate
Products: -
Products: -
?
beta-cyclodextrin + H2O
?
-
Substrates: wild-type enzyme and mutant enzymes G415E, H414N/G415E and H414N hydrolyze beta-cyclodextrin intp maltoheptaose as the major product plus several small maltooligosaccharides
Products: -
Products: -
?
beta-cyclodextrin + H2O
?
Substrates: 80% compared to activity with alpha-cyclodextrin
Products: -
Products: -
?
beta-cyclodextrin + H2O
D-glucose + maltose
Substrates: -
Products: + maltotriose + maltotetraose + maltoheptaose at lower amounts
Products: + maltotriose + maltotetraose + maltoheptaose at lower amounts
?
beta-cyclodextrin + H2O
D-glucose + maltose
WP_000471779.1, Q819G8
Substrates: about 50% of the activity with alpha-cyclodextrin
Products: -
Products: -
?
beta-cyclodextrin + H2O
D-glucose + maltose
-
Substrates: preferred substrate
Products: -
Products: -
?
beta-cyclodextrin + H2O
D-glucose + maltose
Substrates: 100% activity
Products: -
Products: -
?
beta-cyclodextrin + H2O
D-glucose + maltose
Substrates: 100% activity
Products: -
Products: -
?
beta-cyclodextrin + H2O
D-glucose + maltose
-
Substrates: -
Products: + less amounts of maltotriose and maltotetraose
Products: + less amounts of maltotriose and maltotetraose
?
beta-cyclodextrin + H2O
D-glucose + maltose
-
Substrates: -
Products: main products
Products: main products
?
beta-cyclodextrin + H2O
D-glucose + maltose
-
Substrates: -
Products: + less amounts of maltotriose and maltotetraose
Products: + less amounts of maltotriose and maltotetraose
?
beta-cyclodextrin + H2O
D-glucose + maltose
-
Substrates: -
Products: main products
Products: main products
?
beta-cyclodextrin + H2O
glucose + maltose + long chain linear oligomers
-
Substrates: -
Products: -
Products: -
?
beta-cyclodextrin + H2O
glucose + maltose + long chain linear oligomers
-
Substrates: -
Products: -
Products: -
?
beta-cyclodextrin + H2O
glucose + maltose + maltotriose + maltotetraose
-
Substrates: -
Products: -
Products: -
?
beta-cyclodextrin + H2O
glucose + maltose + maltotriose + maltotetraose
-
Substrates: -
Products: -
Products: -
?
beta-cyclodextrin + H2O
glucose + maltose + maltotriose + maltotetraose
-
Substrates: -
Products: -
Products: -
?
beta-cyclodextrin + H2O
maltoheptaose + ?
Substrates: -
Products: -
Products: -
?
beta-cyclodextrin + H2O
maltoheptaose + ?
Substrates: -
Products: -
Products: -
?
beta-cyclodextrin + H2O
maltooligosaccharides
-
Substrates: -
Products: maltohexaose, maltoheptaose, maltooctaose
Products: maltohexaose, maltoheptaose, maltooctaose
?
beta-cyclodextrin + H2O
maltooligosaccharides
-
Substrates: -
Products: maltohexaose, maltoheptaose, maltooctaose
Products: maltohexaose, maltoheptaose, maltooctaose
?
beta-cyclodextrin + H2O
maltooligosaccharides
-
Substrates: -
Products: G1 to G7, maltoheptaose as major product
Products: G1 to G7, maltoheptaose as major product
?
beta-cyclodextrin + H2O
maltooligosaccharides
-
Substrates: -
Products: maltohexaose, maltoheptaose, maltooctaose
Products: maltohexaose, maltoheptaose, maltooctaose
?
beta-cyclodextrin + H2O
maltose + ?
WP_000471779.1, Q819G8
Substrates: the purified enzyme shows substrate preference in the order of alpha-cyclodextrin > beta-cyclodextrin > starch > maltodextrin > gamma-cyclodextrin and hydrolyzes them mainly to maltose
Products: -
Products: -
?
beta-cyclodextrin + H2O
maltose + ?
Bacillus cereus ATCC 14,579
WP_000471779.1
Substrates: the purified enzyme shows substrate preference in the order of alpha-cyclodextrin > beta-cyclodextrin > starch > maltodextrin > gamma-cyclodextrin and hydrolyzes them mainly to maltose
Products: -
Products: -
?
beta-cyclodextrin + H2O
maltose + ?
Substrates: 61% compared to activity with alpha-cyclodextrin
Products: -
Products: -
?
beta-cyclodextrin + H2O
maltose + ?
Substrates: 61% compared to activity with alpha-cyclodextrin
Products: -
Products: -
?
beta-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: -
Products: in an approximate molar ratio of 2 to 1
Products: in an approximate molar ratio of 2 to 1
?
beta-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: -
Products: in an approximate molar ratio of 2 to 1
Products: in an approximate molar ratio of 2 to 1
?
beta-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: -
Products: in an approximate molar ratio of 2 to 1
Products: in an approximate molar ratio of 2 to 1
?
beta-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: -
Products: in an approximate molar ratio of 2 to 1
Products: in an approximate molar ratio of 2 to 1
?
beta-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: -
Products: -
Products: -
?
beta-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: -
Products: in an approximate molar ratio of 2 to 1
Products: in an approximate molar ratio of 2 to 1
?
beta-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: -
Products: in an approximate molar ratio of 2 to 1
Products: in an approximate molar ratio of 2 to 1
?
beta-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: 78% of the activity with gamma-cyclodextrin
Products: -
Products: -
?
beta-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: -
Products: in an approximate molar ratio of 2 to 1
Products: in an approximate molar ratio of 2 to 1
?
beta-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: -
Products: in an approximate molar ratio of 2 to 1
Products: in an approximate molar ratio of 2 to 1
?
beta-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: -
Products: in an approximate molar ratio of 2 to 1
Products: in an approximate molar ratio of 2 to 1
?
beta-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: -
Products: in an approximate molar ratio of 2 to 1
Products: in an approximate molar ratio of 2 to 1
?
beta-cyclodextrin + H2O
maltose + glucose
-
Substrates: -
Products: in an approximate molar ratio of 2 to 1
Products: in an approximate molar ratio of 2 to 1
?
beta-cyclodextrin + H2O
maltose + glucose
Substrates: glucose and maltose are the main products. About 75% of the activity as compared to alpha-cyclodextrin
Products: -
Products: -
?
beta-cyclodextrin + H2O
maltose + glucose
Substrates: glucose and maltose are the main products. About 75% of the activity as compared to alpha-cyclodextrin
Products: -
Products: -
?
beta-cyclodextrin + H2O
maltose + glucose
-
Substrates: -
Products: in an approximate molar ratio of 2 to 1
Products: in an approximate molar ratio of 2 to 1
?
beta-cyclodextrin + H2O
maltose + glucose
-
Substrates: -
Products: -
Products: -
?
beta-cyclodextrin + H2O
maltose + maltotriose
-
Substrates: -
Products: -
Products: -
?
beta-cyclodextrin + H2O
maltose + maltotriose
-
Substrates: -
Products: -
Products: -
?
beta-cyclodextrin + H2O
maltose + maltotriose + maltotetraose + maltopentaose + maltoheptaose + glucose
-
Substrates: -
Products: -
Products: -
?
beta-cyclodextrin + H2O
maltose + maltotriose + maltotetraose + maltopentaose + maltoheptaose + glucose
-
Substrates: -
Products: -
Products: -
?
beta-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
beta-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: -
Products: -
Products: -
?
beta-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
beta-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
beta-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
Substrates: -
Products: -
Products: -
?
beta-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
beta-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
beta-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
beta-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
beta-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: -
Products: -
Products: -
?
beta-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
beta-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
beta-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: best substrate
Products: -
Products: -
?
beta-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
beta-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
beta-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
beta-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
cyclodextrin + H2O
glucose + ?
-
Substrates: alpha and beta
Products: -
Products: -
?
cyclomaltodextrin + H2O
linear maltodextrin
-
Substrates: -
Products: -
Products: -
?
cyclomaltodextrin + H2O
linear maltodextrin
-
Substrates: no avtivity with activity with starch, pullulan, amylose, amylopectin, or oligosaccharides as substrates
Products: -
Products: -
?
cyclomaltodextrin + H2O
linear maltodextrin
-
Substrates: no avtivity with activity with starch, pullulan, amylose, amylopectin, or oligosaccharides as substrates
Products: -
Products: -
?
cyclomaltodextrin + H2O
linear maltodextrin
-
Substrates: -
Products: -
Products: -
?
cyclomaltodextrin + H2O
linear maltodextrin
-
Substrates: -
Products: -
Products: -
?
cyclomaltodextrin + H2O
linear maltodextrin
-
Substrates: -
Products: -
Products: -
?
cyclomaltodextrin + H2O
linear maltodextrin
-
Substrates: -
Products: -
Products: -
?
cyclomaltodextrin + H2O
linear maltodextrin
Substrates: -
Products: -
Products: -
?
cyclomaltodextrin + H2O
linear maltodextrin
-
Substrates: -
Products: -
Products: -
?
cyclomaltodextrin + H2O
linear maltodextrin
-
Substrates: -
Products: -
Products: -
?
cyclomaltodextrin + H2O
linear maltodextrin
-
Substrates: -
Products: -
Products: -
?
cyclomaltodextrin + H2O
maltodextrin
-
Substrates: -
Products: -
Products: -
?
cyclomaltodextrin + H2O
maltodextrin
-
Substrates: -
Products: -
Products: -
?
cyclomaltodextrin + H2O
maltodextrin
-
Substrates: -
Products: -
Products: -
?
cyclomaltodextrin + H2O
maltodextrin
-
Substrates: -
Products: -
Products: -
?
cyclomaltodextrin + H2O
maltodextrin
-
Substrates: -
Products: linear, glucose only
Products: linear, glucose only
?
cyclomaltodextrin + H2O
maltodextrin
-
Substrates: -
Products: linear, glucose only
Products: linear, glucose only
?
cyclomaltodextrin + H2O
maltodextrin
-
Substrates: -
Products: -
Products: -
?
cyclomaltodextrin + H2O
maltodextrin
-
Substrates: -
Products: -
Products: -
?
cyclomaltodextrin + H2O
maltodextrin
-
Substrates: alpha-, beta- and gamma
Products: -
Products: -
?
cyclomaltodextrin + H2O
maltodextrin
-
Substrates: -
Products: -
Products: -
?
cyclomaltodextrin + H2O
maltodextrin
-
Substrates: -
Products: maltooligosaccharides
Products: maltooligosaccharides
?
cyclomaltodextrin + H2O
maltodextrin
-
Substrates: opening the ring of the cyclic dextrins forming a linear molecule with corresponding number of glucose units
Products: -
Products: -
ir
cyclomaltodextrin + H2O
maltodextrin
-
Substrates: -
Products: -
Products: -
ir
cyclomaltodextrin + H2O
maltodextrin
-
Substrates: opening the ring of the cyclic dextrins forming a linear molecule with corresponding number of glucose units
Products: -
Products: -
ir
cyclomaltodextrin + H2O
maltodextrin
-
Substrates: -
Products: series of maltooligomers
Products: series of maltooligomers
?
cyclomaltodextrin + H2O
maltodextrin
-
Substrates: -
Products: series of maltooligomers
Products: series of maltooligomers
?
cyclomaltodextrin + H2O
maltodextrin
-
Substrates: -
Products: -
Products: -
?
cyclomaltodextrin + H2O
maltodextrin
-
Substrates: alpha-cyclodextrin 100% hydrolysis, beta-cyclodextrin 67% hydrolysis, gamma-cyclodextrin 8%
Products: -
Products: -
?
cyclomaltodextrin + H2O
maltodextrin
-
Substrates: alpha-cyclodextrin 100% hydrolysis, beta-cyclodextrin 67% hydrolysis, gamma-cyclodextrin 8%
Products: -
Products: -
?
cyclomaltodextrin + H2O
maltodextrin
-
Substrates: -
Products: -
Products: -
?
cyclomaltodextrin + H2O
maltooligosaccharide
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
cyclomaltodextrin + H2O
maltooligosaccharide
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
cyclomaltodextrins + H2O
linear maltodextrins
-
Substrates: -
Products: -
Products: -
?
cyclomaltodextrins + H2O
linear maltodextrins
-
Substrates: -
Products: -
Products: -
?
cyclomaltodextrins + H2O
linear maltodextrins
-
Substrates: -
Products: -
Products: -
?
G1-beta-cyclodextrin + H2O
D-glucose + maltose
-
Substrates: 32% of the activity with beta-cyclodextrin
Products: main products
Products: main products
?
G1-beta-cyclodextrin + H2O
D-glucose + maltose
-
Substrates: 32% of the activity with beta-cyclodextrin
Products: main products
Products: main products
?
gamma-cyclodextrin + H2O
?
Substrates: -
Products: -
Products: -
?
gamma-cyclodextrin + H2O
?
Substrates: -
Products: -
Products: -
?
gamma-cyclodextrin + H2O
?
Substrates: higher affinity for alpha-cyclodextrin followed by beta-cyclodextrin and then gamma-cyclodextrin
Products: -
Products: -
?
gamma-cyclodextrin + H2O
?
Substrates: higher affinity for alpha-cyclodextrin followed by beta-cyclodextrin and then gamma-cyclodextrin
Products: -
Products: -
?
gamma-cyclodextrin + H2O
?
-
Substrates: cyclomaltodextrinase activity
Products: -
Products: -
?
gamma-cyclodextrin + H2O
?
Substrates: 73% compared to activity with alpha-cyclodextrin
Products: -
Products: -
?
gamma-cyclodextrin + H2O
D-glucose + maltose
WP_000471779.1, Q819G8
Substrates: about 15% of the activity with alpha-cyclodextrin
Products: -
Products: -
?
gamma-cyclodextrin + H2O
D-glucose + maltose
-
Substrates: 72% of the activity with beta-cyclodextrin
Products: + less amounts of maltotriose and maltotetraose
Products: + less amounts of maltotriose and maltotetraose
?
gamma-cyclodextrin + H2O
D-glucose + maltose
-
Substrates: 59% of the activity with beta-cyclodextrin
Products: main products
Products: main products
?
gamma-cyclodextrin + H2O
D-glucose + maltose
-
Substrates: 72% of the activity with beta-cyclodextrin
Products: + less amounts of maltotriose and maltotetraose
Products: + less amounts of maltotriose and maltotetraose
?
gamma-cyclodextrin + H2O
D-glucose + maltose
-
Substrates: 59% of the activity with beta-cyclodextrin
Products: main products
Products: main products
?
gamma-cyclodextrin + H2O
glucose + maltose + maltotriose + maltotetraose + maltopentaose + maltohexaose + maltoheptaose + maltooctaose
-
Substrates: -
Products: -
Products: -
?
gamma-cyclodextrin + H2O
glucose + maltose + maltotriose + maltotetraose + maltopentaose + maltohexaose + maltoheptaose + maltooctaose
-
Substrates: -
Products: -
Products: -
?
gamma-cyclodextrin + H2O
maltooctaose + ?
Substrates: cyclodextrinase rapidly hydrolyzes only gamma-cyclodextrinase, whereas it slowly hydrolyzes alpha- and beta-cyclodextrinase, maltooctaose, amylose, amylopectin and soluble starch. The hydrolysis activities toward these substrates are less than 4% of that toward gamma-cyclodextrinase. Pullulan and glycogen are hardly hydrolyzed. Cyclodextrinase is a CDase that has high specificity for only gamma-cyclodextrinase
Products: -
Products: -
?
gamma-cyclodextrin + H2O
maltooctaose + ?
Evansella clarkii 7364
Substrates: cyclodextrinase rapidly hydrolyzes only gamma-cyclodextrinase, whereas it slowly hydrolyzes alpha- and beta-cyclodextrinase, maltooctaose, amylose, amylopectin and soluble starch. The hydrolysis activities toward these substrates are less than 4% of that toward gamma-cyclodextrinase. Pullulan and glycogen are hardly hydrolyzed. Cyclodextrinase is a CDase that has high specificity for only gamma-cyclodextrinase
Products: -
Products: -
?
gamma-cyclodextrin + H2O
maltooligosaccharides
-
Substrates: preferred substrate
Products: maltohexaose, maltoheptaose, maltooctaose
Products: maltohexaose, maltoheptaose, maltooctaose
?
gamma-cyclodextrin + H2O
maltooligosaccharides
-
Substrates: preferred substrate
Products: maltohexaose, maltoheptaose, maltooctaose
Products: maltohexaose, maltoheptaose, maltooctaose
?
gamma-cyclodextrin + H2O
maltooligosaccharides
-
Substrates: preferred substrate
Products: maltohexaose, maltoheptaose, maltooctaose
Products: maltohexaose, maltoheptaose, maltooctaose
?
gamma-cyclodextrin + H2O
maltose + ?
WP_000471779.1, Q819G8
Substrates: the purified enzyme shows substrate preference in the order of alpha-cyclodextrin > beta-cyclodextrin > starch > maltodextrin > gamma-cyclodextrin and hydrolyzes them mainly to maltose
Products: -
Products: -
?
gamma-cyclodextrin + H2O
maltose + ?
Bacillus cereus ATCC 14,579
WP_000471779.1
Substrates: the purified enzyme shows substrate preference in the order of alpha-cyclodextrin > beta-cyclodextrin > starch > maltodextrin > gamma-cyclodextrin and hydrolyzes them mainly to maltose
Products: -
Products: -
?
gamma-cyclodextrin + H2O
maltose + ?
Substrates: 30% compared to activity with alpha-cyclodextrin
Products: -
Products: -
?
gamma-cyclodextrin + H2O
maltose + ?
Substrates: 30% compared to activity with alpha-cyclodextrin
Products: -
Products: -
?
gamma-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: -
Products: in an approximate molar ratio of 2 to 1
Products: in an approximate molar ratio of 2 to 1
?
gamma-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: -
Products: in an approximate molar ratio of 2 to 1
Products: in an approximate molar ratio of 2 to 1
?
gamma-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: -
Products: in an approximate molar ratio of 2 to 1
Products: in an approximate molar ratio of 2 to 1
?
gamma-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: -
Products: in an approximate molar ratio of 2 to 1
Products: in an approximate molar ratio of 2 to 1
?
gamma-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: -
Products: -
Products: -
?
gamma-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: -
Products: in an approximate molar ratio of 2 to 1
Products: in an approximate molar ratio of 2 to 1
?
gamma-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: -
Products: in an approximate molar ratio of 2 to 1
Products: in an approximate molar ratio of 2 to 1
?
gamma-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: -
Products: -
Products: -
?
gamma-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: during the initial stage of the reaction, only one alpha-1,4-glycosidic linkage of every gamma-cyclodexrtrin is cleaved, and then the linear maltooctaose is formed. Until almost all gamma-cyclodextrin has disappeared, maltooctaose is not further hydrolyzed. Selective degradation of gamma-cyclodextrin is preferred by the enzyme in the presence of maltooctaose. After all rings are opened at one single glycosidic linkage of cyclodextrins, the corresponding maltooligosaccharides started to be hydrolyzed into smaller maltooligosaccharides. The final hydrolysis products are maltose and glucose
Products: -
Products: -
?
gamma-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: -
Products: in an approximate molar ratio of 2 to 1
Products: in an approximate molar ratio of 2 to 1
?
gamma-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: -
Products: in an approximate molar ratio of 2 to 1
Products: in an approximate molar ratio of 2 to 1
?
gamma-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: -
Products: in an approximate molar ratio of 2 to 1
Products: in an approximate molar ratio of 2 to 1
?
gamma-cyclodextrin + H2O
maltose + D-glucose
-
Substrates: -
Products: in an approximate molar ratio of 2 to 1
Products: in an approximate molar ratio of 2 to 1
?
gamma-cyclodextrin + H2O
maltose + glucose
-
Substrates: -
Products: in an approximate molar ratio of 2 to 1
Products: in an approximate molar ratio of 2 to 1
?
gamma-cyclodextrin + H2O
maltose + glucose
Substrates: glucose and maltose are the main products. About 60% of the activity as compared to alpha-cyclodextrin
Products: -
Products: -
?
gamma-cyclodextrin + H2O
maltose + glucose
Substrates: glucose and maltose are the main products. About 60% of the activity as compared to alpha-cyclodextrin
Products: -
Products: -
?
gamma-cyclodextrin + H2O
maltose + glucose
-
Substrates: -
Products: in an approximate molar ratio of 2 to 1
Products: in an approximate molar ratio of 2 to 1
?
gamma-cyclodextrin + H2O
maltose + maltotriose
-
Substrates: -
Products: -
Products: -
?
gamma-cyclodextrin + H2O
maltose + maltotriose
-
Substrates: -
Products: -
Products: -
?
gamma-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
gamma-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: -
Products: -
Products: -
?
gamma-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
gamma-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
gamma-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
Substrates: -
Products: -
Products: -
?
gamma-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
gamma-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
gamma-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
gamma-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
gamma-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: -
Products: -
Products: -
?
gamma-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
gamma-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
gamma-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: 33% of the activity with beta-cyclomaltodextrin
Products: -
Products: -
?
gamma-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
gamma-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
gamma-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
gamma-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
Substrates: composed of 6 to 8 D-glucopyranosyl residues
Products: -
Products: -
?
glucosyl-alpha-cyclodextrin + H2O
6,3-O-alpha-D-glucosylmaltohexaose
-
Substrates: branched alpha-cyclodextrin, synonym 6-O-alpha-D-glucosylmaltohexaose
Products: -
Products: -
?
glucosyl-alpha-cyclodextrin + H2O
6,3-O-alpha-D-glucosylmaltohexaose
-
Substrates: branched alpha-cyclodextrin, synonym 6-O-alpha-D-glucosylmaltohexaose
Products: -
Products: -
?
glucosyl-beta-cyclodextrin + H2O
6,4-O-alpha-D-glucosylmaltoheptaose
-
Substrates: branched beta-cyclodextrin, synonym 6-O-alpha D-glucosylmaltoheptaose
Products: -
Products: -
?
glucosyl-beta-cyclodextrin + H2O
6,4-O-alpha-D-glucosylmaltoheptaose
-
Substrates: -
Products: -
Products: -
?
glucosyl-beta-cyclodextrin + H2O
6,4-O-alpha-D-glucosylmaltoheptaose
-
Substrates: branched beta-cyclodextrin, synonym 6-O-alpha D-glucosylmaltoheptaose
Products: -
Products: -
?
glycogen + H2O
?
Substrates: less than 5% of the activity as compared to alpha-cyclodextrin
Products: -
Products: -
?
glycogen + H2O
?
Substrates: less than 5% of the activity as compared to alpha-cyclodextrin
Products: -
Products: -
?
glycogen + H2O
?
-
Substrates: relative rate of hydrolysis 0,1%
Products: -
Products: -
?
isopanose + H2O
?
-
Substrates: cyclomaltodextrinase activity, hydrolysis of alpha-1,6-glucosidic linkages
Products: -
Products: -
?
linear maltodextrins + H2O
alpha-D-glucose + maltose
-
Substrates: -
Products: -
Products: -
?
linear maltodextrins + H2O
alpha-D-glucose + maltose
-
Substrates: -
Products: -
Products: -
?
linear maltodextrins + H2O
alpha-D-glucose + maltose
-
Substrates: -
Products: -
Products: -
?
linear maltodextrins + H2O
alpha-D-glucose + maltose
-
Substrates: -
Products: -
Products: -
?
linear maltodextrins + H2O
alpha-D-glucose + maltose
-
Substrates: -
Products: -
Products: -
?
linear maltodextrins + H2O
alpha-D-glucose + maltose
-
Substrates: -
Products: -
Products: -
?
linear maltodextrins + H2O
alpha-D-glucose + maltose
-
Substrates: -
Products: -
Products: -
?
linear maltodextrins + H2O
alpha-D-glucose + maltose
-
Substrates: with a small glucose unit, low activity
Products: -
Products: -
?
linear maltodextrins + H2O
alpha-D-glucose + maltose
-
Substrates: -
Products: -
Products: -
?
linear maltodextrins + H2O
alpha-D-glucose + maltose
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
Substrates: -
Products: -
Products: -
?
maltodextrin + H2O
?
Substrates: 62% activity compared to beta-cyclodextrin
Products: -
Products: -
?
maltodextrin + H2O
?
Substrates: 62% activity compared to beta-cyclodextrin
Products: -
Products: -
?
maltodextrin + H2O
maltose + ?
WP_000471779.1, Q819G8
Substrates: the purified enzyme shows substrate preference in the order of alpha-cyclodextrin > beta-cyclodextrin > starch > maltodextrin > gamma-cyclodextrin and hydrolyzes them mainly to maltose
Products: -
Products: -
?
maltodextrin + H2O
maltose + ?
Bacillus cereus ATCC 14,579
WP_000471779.1
Substrates: the purified enzyme shows substrate preference in the order of alpha-cyclodextrin > beta-cyclodextrin > starch > maltodextrin > gamma-cyclodextrin and hydrolyzes them mainly to maltose
Products: -
Products: -
?
maltodextrins + H2O
maltose + glucose
-
Substrates: linear, enzyme degrades the linear molecules by splitting off maltose units from the nonreducing end of the chain
Products: -
Products: -
?
maltodextrins + H2O
maltose + glucose
-
Substrates: 6 to 8 membered maltooligosaccharides
Products: -
Products: -
?
maltodextrins + H2O
maltose + glucose
-
Substrates: linear, enzyme degrades the linear molecules by splitting off maltose units from the nonreducing end of the chain
Products: -
Products: -
?
maltodextrins + H2O
maltose + glucose
-
Substrates: linear, enzyme degrades the linear molecules by splitting off maltose units from the nonreducing end of the chain
Products: -
Products: -
?
maltodextrins + H2O
maltose + glucose
-
Substrates: linear, enzyme degrades the linear molecules by splitting off maltose units from the nonreducing end of the chain
Products: -
Products: -
?
maltodextrins + H2O
maltose + glucose
-
Substrates: linear, enzyme degrades the linear molecules by splitting off maltose units from the nonreducing end of the chain
Products: -
Products: -
?
maltodextrins + H2O
maltose + glucose
-
Substrates: linear, enzyme degrades the linear molecules by splitting off maltose units from the nonreducing end of the chain
Products: -
Products: -
?
maltodextrins + H2O
maltose + glucose
-
Substrates: linear, enzyme degrades the linear molecules by splitting off maltose units from the nonreducing end of the chain
Products: -
Products: -
?
maltoheptaose + H2O
?
-
Substrates: 41% of the activity with beta-cyclodextrin
Products: -
Products: -
?
maltoheptaose + H2O
D-glucose + maltose + ?
-
Substrates: -
Products: -
Products: -
?
maltoheptaose + H2O
D-glucose + maltose + ?
Substrates: -
Products: -
Products: -
?
maltoheptaose + H2O
D-glucose + maltose + ?
Substrates: -
Products: -
Products: -
?
maltoheptaose + H2O
D-glucose + maltose + ?
-
Substrates: -
Products: -
Products: -
?
maltoheptaose + H2O
D-glucose + maltose + ?
-
Substrates: 43% of the activity with beta-cyclodextrin
Products: -
Products: -
?
maltoheptaose + H2O
D-glucose + maltose + ?
-
Substrates: 43% of the activity with beta-cyclodextrin
Products: -
Products: -
?
maltoheptaose + H2O
D-glucose + maltose + ?
-
Substrates: -
Products: -
Products: -
?
maltohexaose + H2O
D-glucose + maltose + ?
-
Substrates: 35% of the activity with beta-cyclodextrin
Products: -
Products: -
?
maltohexaose + H2O
D-glucose + maltose + ?
-
Substrates: 35% of the activity with beta-cyclodextrin
Products: -
Products: -
?
maltohexaose + H2O
maltotetraose + maltose
-
Substrates: -
Products: -
Products: -
?
maltohexaose + H2O
maltotetraose + maltose
-
Substrates: -
Products: -
Products: -
?
maltohexaose + H2O
maltotetraose + maltose
-
Substrates: -
Products: -
Products: -
?
maltohexaose + H2O
maltotetraose + maltose
-
Substrates: -
Products: -
Products: -
?
maltohexaose + H2O
maltotetraose + maltose
-
Substrates: -
Products: -
Products: -
?
maltooctaose + H2O
maltohexaose + maltose
Substrates: -
Products: small amounts of maltotriose, maltotetraose and maltopentaose are also observed
Products: small amounts of maltotriose, maltotetraose and maltopentaose are also observed
?
maltooctaose + H2O
maltohexaose + maltose
Evansella clarkii 7364
Substrates: -
Products: small amounts of maltotriose, maltotetraose and maltopentaose are also observed
Products: small amounts of maltotriose, maltotetraose and maltopentaose are also observed
?
maltooligosaccharides + H2O
D-glucose + ?
-
Substrates: -
Products: -
Products: -
?
maltooligosaccharides + H2O
D-glucose + ?
-
Substrates: -
Products: -
Products: -
?
maltooligosaccharides + H2O
D-glucose + ?
-
Substrates: -
Products: -
Products: -
?
maltooligosaccharides + H2O
D-glucose + ?
-
Substrates: -
Products: -
Products: -
?
maltopentaose + H2O
maltose + maltotriose
-
Substrates: -
Products: -
Products: -
?
maltopentaose + H2O
maltose + maltotriose
-
Substrates: -
Products: -
Products: -
?
maltopentaose + H2O
maltose + maltotriose
-
Substrates: -
Products: -
Products: -
?
maltopentaose + H2O
maltose + maltotriose
-
Substrates: -
Products: -
Products: -
?
maltopentaose + H2O
maltose + maltotriose
-
Substrates: -
Products: -
Products: -
?
maltosyl-alpha-cyclodextrin + H2O
6,3-O-alpha-D-maltosylmaltohexaose
-
Substrates: branched alpha-cyclodextrin, synonym 6-O-alpha-D-maltosylcyclomaltohexaose
Products: -
Products: -
?
maltosyl-alpha-cyclodextrin + H2O
6,3-O-alpha-D-maltosylmaltohexaose
-
Substrates: -
Products: -
Products: -
?
maltosyl-alpha-cyclodextrin + H2O
6,3-O-alpha-D-maltosylmaltohexaose
-
Substrates: branched alpha-cyclodextrin, synonym 6-O-alpha-D-maltosylcyclomaltohexaose
Products: -
Products: -
?
maltosyl-beta-cyclodextrin
6,4-O-alpha-D-maltosylmaltoheptaose
-
Substrates: branched beta-cyclodextrin, synonym 6-O-alpha-D-maltosylcyclomaltoheptaose
Products: -
Products: -
?
maltosyl-beta-cyclodextrin
6,4-O-alpha-D-maltosylmaltoheptaose
-
Substrates: -
Products: -
Products: -
?
maltosyl-beta-cyclodextrin
6,4-O-alpha-D-maltosylmaltoheptaose
-
Substrates: branched beta-cyclodextrin, synonym 6-O-alpha-D-maltosylcyclomaltoheptaose
Products: -
Products: -
?
maltotetraose + H2O
2 D-glucose + maltose
Substrates: -
Products: -
Products: -
?
maltotetraose + H2O
2 D-glucose + maltose
Substrates: -
Products: -
Products: -
?
maltotetraose + H2O
2 D-glucose + maltose
-
Substrates: 14% of the activity with beta-cyclodextrin
Products: -
Products: -
?
maltotetraose + H2O
2 maltose
-
Substrates: -
Products: -
Products: -
?
maltotriose + H2O
?
-
Substrates: 11% of the activity with beta-cyclodextrin
Products: -
Products: -
?
maltotriose + H2O
?
-
Substrates: slowly
Products: -
Products: -
?
maltotriose + H2O
?
-
Substrates: slowly
Products: -
Products: -
?
maltotriose + H2O
maltose + D-glucose
-
Substrates: 11% of the activity with beta-cyclodextrin
Products: -
Products: -
?
maltotriose + H2O
maltose + D-glucose
-
Substrates: 5.3% of the activity with gamma-cyclodextrin
Products: -
Products: -
?
pullulan + H2O
glucose + panose + isopanose + large saccharides containing alpha 1,6-glucosidic bonds
-
Substrates: -
Products: -
Products: -
?
pullulan + H2O
glucose + panose + isopanose + large saccharides containing alpha 1,6-glucosidic bonds
-
Substrates: -
Products: -
Products: -
?
pullulan + H2O
glucose + panose + isopanose + large saccharides containing alpha 1,6-glucosidic bonds
-
Substrates: -
Products: -
Products: -
?
pullulan + H2O
glucose + panose + isopanose + large saccharides containing alpha 1,6-glucosidic bonds
-
Substrates: -
Products: -
Products: -
?
pullulan + H2O
glucose + panose + isopanose + large saccharides containing alpha 1,6-glucosidic bonds
-
Substrates: -
Products: -
Products: -
?
pullulan + H2O
glucose + panose + isopanose + large saccharides containing alpha 1,6-glucosidic bonds
-
Substrates: -
Products: -
Products: -
?
pullulan + H2O
glucose + panose + isopanose + large saccharides containing alpha 1,6-glucosidic bonds
-
Substrates: rate of hydrolysis less than 5% of the rate of alpha-cyclodextrin hydrolysis
Products: -
Products: -
?
pullulan + H2O
panose + maltose
-
Substrates: substrate is a linear polysaccharide composed of maltotriose units linked by alpha-1,6-bonds, low activity
Products: main products
Products: main products
?
pullulan + H2O
panose + maltose
-
Substrates: substrate is a linear polysaccharide composed of maltotriose units linked by alpha-1,6-bonds, low activity
Products: main products
Products: main products
?
pullulan + H2O
panose + maltose
-
Substrates: substrate is a linear polysaccharide composed of maltotriose units linked by alpha-1,6-bonds, low activity
Products: main products
Products: main products
?
pullulan + H2O
panose + maltose
-
Substrates: substrate is a linear polysaccharide composed of maltotriose units linked by alpha-1,6-bonds, low activity
Products: main products
Products: main products
?
pullulan + H2O
panose + maltose
-
Substrates: substrate is a linear polysaccharide composed of maltotriose units linked by alpha-1,6-bonds, low activity
Products: main products
Products: main products
?
pullulan + H2O
panose + maltose
-
Substrates: substrate is a linear polysaccharide composed of maltotriose units linked by alpha-1,6-bonds, low activity
Products: main products
Products: main products
?
pullulan + H2O
panose + maltose
-
Substrates: substrate is a linear polysaccharide composed of maltotriose units linked by alpha-1,6-bonds, low activity
Products: main products
Products: main products
?
pullulan + H2O
panose + maltose + glucose
-
Substrates: -
Products: -
Products: -
?
pullulan + H2O
panose + maltose + glucose
-
Substrates: -
Products: -
Products: -
?
pullulan + H2O
panose + maltose + glucose
-
Substrates: -
Products: -
Products: -
?
pullulan + H2O
panose + maltose + glucose
-
Substrates: -
Products: -
Products: -
?
starch + H2O
?
Substrates: less than 5% of the activity as compared to alpha-cyclodextrin
Products: -
Products: -
?
starch + H2O
?
Substrates: less than 5% of the activity as compared to alpha-cyclodextrin
Products: -
Products: -
?
starch + H2O
?
Substrates: 8% activity compared to beta-cyclodextrin
Products: -
Products: -
?
starch + H2O
?
Substrates: 8% activity compared to beta-cyclodextrin
Products: -
Products: -
?
starch + H2O
alpha-D-glucose + maltose
-
Substrates: no formation of cyclodextrins as products
Products: -
Products: -
?
starch + H2O
alpha-D-glucose + maltose
-
Substrates: -
Products: -
Products: -
?
starch + H2O
alpha-D-glucose + maltose
-
Substrates: soluble starch, no formation of cyclodextrins as products
Products: -
Products: -
?
starch + H2O
alpha-D-glucose + maltose
-
Substrates: soluble starch, no formation of cyclodextrins as products
Products: -
Products: -
?
starch + H2O
alpha-D-glucose + maltose
-
Substrates: soluble starch, no formation of cyclodextrins as products
Products: -
Products: -
?
starch + H2O
alpha-D-glucose + maltose
-
Substrates: no formation of cyclodextrins as products
Products: -
Products: -
?
starch + H2O
alpha-D-glucose + maltose
-
Substrates: no formation of cyclodextrins as products
Products: -
Products: -
?
starch + H2O
alpha-D-glucose + maltose
-
Substrates: no formation of cyclodextrins as products
Products: -
Products: -
?
starch + H2O
alpha-D-glucose + maltose
-
Substrates: no formation of cyclodextrins as products
Products: -
Products: -
?
starch + H2O
alpha-D-glucose + maltose
-
Substrates: soluble starch, no formation of cyclodextrins as products
Products: -
Products: -
?
starch + H2O
alpha-D-glucose + maltose
-
Substrates: soluble starch, no formation of cyclodextrins as products
Products: -
Products: -
?
starch + H2O
alpha-D-glucose + maltose
-
Substrates: soluble starch, no formation of cyclodextrins as products
Products: -
Products: -
?
starch + H2O
glucose + maltose
-
Substrates: -
Products: -
Products: -
?
starch + H2O
glucose + maltose
-
Substrates: -
Products: -
Products: -
?
starch + H2O
glucose + maltose
-
Substrates: 10%
Products: degraded slowly by cleavage of maltose units from the nonreducing ends
Products: degraded slowly by cleavage of maltose units from the nonreducing ends
?
starch + H2O
glucose + maltose
-
Substrates: -
Products: glucose minor early product, + maltotriose + maltotetraose
Products: glucose minor early product, + maltotriose + maltotetraose
?
starch + H2O
glucose + maltose
-
Substrates: -
Products: -
Products: -
?
starch + H2O
glucose + maltose
-
Substrates: -
Products: -
Products: -
?
starch + H2O
glucose + maltose
-
Substrates: -
Products: -
Products: -
?
starch + H2O
glucose + maltose
-
Substrates: 50% hydrolysis
Products: -
Products: -
?
starch + H2O
glucose + maltose
-
Substrates: 50% hydrolysis
Products: -
Products: -
?
starch + H2O
maltose + ?
WP_000471779.1, Q819G8
Substrates: the purified enzyme shows substrate preference in the order of alpha-cyclodextrin > beta-cyclodextrin > starch > maltodextrin > gamma-cyclodextrin and hydrolyzes them mainly to maltose
Products: -
Products: -
?
starch + H2O
maltose + ?
Bacillus cereus ATCC 14,579
WP_000471779.1
Substrates: the purified enzyme shows substrate preference in the order of alpha-cyclodextrin > beta-cyclodextrin > starch > maltodextrin > gamma-cyclodextrin and hydrolyzes them mainly to maltose
Products: -
Products: -
?
cyclomaltodextrin + H2O
linear maltodextrin
additional information
-
Substrates: -
Products: -
Products: -
?
maltooligosaccharides + H2O
D-glucose + ?
additional information
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological role of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: broad specificity, cleavage of alpha-1,4- and alpha-1,6-glycosidic bonds, the cyclomaltodextrins are the preferred substrates, substrate ring size effects the activity, the enzyme also shows transglucosylation activity transferring cleavage products to the sugar moiety of various acceptor molecules resulting in a series of branched oligosaccharides, part of the cyclomaltodextrin binding site is located between the third and fourth conserved regions
Products: -
Products: -
?
additional information
?
-
WP_000471779.1
Substrates: no hydrolyis of maltose, pullulan, and glycogen
Products: -
Products: -
-
additional information
?
-
Substrates: no hydrolyis of maltose, pullulan, and glycogen
Products: -
Products: -
-
additional information
?
-
WP_000471779.1
Substrates: substrate preference in decreasing order: alpha-cyclodextrin > beta-cyclodextrin > starch > maltodextrin > gamma-cyclodextrin, substrates are mainly hydrolyzed to maltose. No substrates are: maltose, pullulan, and glycogen. In addition, the enzyme enzyme can transfer the sugars released from cyclodextrins and maltotriose to acceptor molecules
Products: -
Products: -
-
additional information
?
-
Substrates: substrate preference in decreasing order: alpha-cyclodextrin > beta-cyclodextrin > starch > maltodextrin > gamma-cyclodextrin, substrates are mainly hydrolyzed to maltose. No substrates are: maltose, pullulan, and glycogen. In addition, the enzyme enzyme can transfer the sugars released from cyclodextrins and maltotriose to acceptor molecules
Products: -
Products: -
-
additional information
?
-
-
Substrates: physiological role of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: broad specificity, cleavage of mainly alpha-1,4- and also alpha-1,6-glycosidic bonds in strain I-5, the cyclomaltodextrins are the preferred substrates, substrate ring size effects the activity, the enzyme also shows very high transglucosylation activity transferring cleavage products to the sugar moiety of various acceptor molecules resulting in a series of branched oligosaccharides with alpha-1,3-, alpha1,4-, and alpha1,6-glycosidic bonds in strain I-5, substrate specificities and cleavage activities are different between different Bacillus strains, overview, part of the cyclomaltodextrin binding site is located between the third and fourth conserved regions
Products: -
Products: -
?
additional information
?
-
-
Substrates: neopullulanases, cyclomaltodextrinases and maltogenic amylases display similar biochemical properties and share almost the same 3D structures, enzymes should be classified under the same name and enzyme code, cyclodextrins are the most preferred substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological role of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological role of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological role of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: broad substrate specificity, cleavage of alpha-1,4- and alpha-1,6-glycosidic bonds, the cyclomaltodextrins and linear maltodextrins are the preferred substrates, substrate ring size effects the activity, the enzyme also shows very high transglucosylation activity transferring cleavage products to the sugar moiety of various acceptor molecules resulting in a series of branched oligosaccharides in alpha-1,4- and alpha1,6-glycosidic bonds
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological role of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: broad specificity, cleavage of alpha-1,4-glycosidic bonds, linear maltodextrins are the preferred substrates before cyclomaltodextrins, soluble starch, and pullulan, substrate ring size effects the activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological role of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: slowly: short chain amylose
Products: -
Products: -
?
additional information
?
-
-
Substrates: hydrolyses by detaching one maltose unit, recognizes maltose residues at non-reducing end of various maltosides and hydrolyzes (1, 4)-, (1, 2)-, (1, 3)-and (1, 6)-alpha-D-glucosidic linkages and the glucosidic linkages between D-glucose and phenol, D-glucose and D-glucitol, and D-glucose and D-fructose adjacent to the maltose molecule
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological role of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: broad specificity, cleavage of alpha-1,4- and alpha-1,6-glycosidic bonds, the cyclomaltodextrins are the preferred substrates, substrate ring size effects the activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological role of the enzyme, starch utilization pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: part of the cyclomaltodextrin binding site is located between the third and fourth conserved regions
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological role of the enzyme, starch utilization pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: part of the cyclomaltodextrin binding site is located between the third and fourth conserved regions
Products: -
Products: -
?
additional information
?
-
-
Substrates: poor activity with starch, acarbose, and pullulan, about 80fold lower compared to beta-cyclodextrin
Products: -
Products: -
?
additional information
?
-
-
Substrates: poor activity with starch, acarbose, and pullulan, about 80fold lower compared to beta-cyclodextrin
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological role of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: broad specificity, cleavage of alpha-1,4-glycosidic bonds, the cyclomaltodextrins are the preferred substrates, substrate ring size effects the activity, substrate specificity is different between different the strains, overview, part of the cyclomaltodextrin binding site is located between the third and fourth conserved regions
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with maltose
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with maltose
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological role of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: broad specificity, cleavage of alpha-1,4- and alpha-1,6-glycosidic bonds, the cyclomaltodextrins are the preferred substrates, substrate ring size effects the activity, the enzyme also shows transglucosylation activity transferring cleavage products to the sugar moiety of various acceptor molecules resulting in a series of branched oligosaccharides
Products: -
Products: -
?
additional information
?
-
-
Substrates: inducible enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme hardly reacts with potato soluble starch, pullulan, amylose, amylopectin
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity, hydrolytic pattern, PFTA is a bifunctional enzyme showing alpha-amylase as well as cyclodextrin-hydrolyzing activity, but no transglycosylation activity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity of the bifunctional enzyme, the enzyme hydrolyzes alpha-1,4-glucosidic linkages and alpha-1,6-glucosidic linkages, and performs transglycosylation reactions, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological role of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: broad substrate specificity, cleavage of alpha-1,4-glycosidic bonds, the cyclomaltodextrins are the preferred substrates, substrate ring size effects the activity, part of the cyclomaltodextrin binding site is located between the third and fourth conserved regions
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological role of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: not: maltose
Products: -
Products: -
?
additional information
?
-
-
Substrates: not: maltose
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with pullulan and maltose, soluble starch is a poor substrate
Products: -
Products: -
?
additional information
?
-
Substrates: substrate specificity, overview. The enzyme preferentially hydrolyzes alpha-cyclodextrin, and at the initial stage catalyzes a ring-opening reaction by cleaving one alpha-1,4-glycosidic linkage of the cyclodextrin ring to produce the corresponding single maltooligosaccharide. A long substrate is preferred over smaller substrates. The enzyme can hydrolyze branched cyclodextrins to yield significant amounts of isomaltooligosaccharides (panose and 6-alpha-maltosylmaltose) in addition to glucose and maltose. No activity with pullulan and maltose, poor activity with soluble starch, amylopactin, and amylose, product analysis by thin layer chromatography, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological role of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: broad specificity, cleavage of alpha-1,4-glycosidic bonds, the linear maltodextrins are the preferred substrates, substrate ring size effects the activity
Products: -
Products: -
?
additional information
?
-
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
Substrates: physiological role of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological role of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: broad specificity, cleavage of alpha-1,4-glycosidic bonds, the cyclomaltodextrins are the preferred substrates, substrate ring size effects the activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological role of the enzyme
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
cyclomaltodextrin + H2O
linear maltodextrin
Substrates: -
Products: -
Products: -
?
alpha-cyclodextrin + H2O
isomaltooligosaccharides
Substrates: -
Products: -
Products: -
?
alpha-cyclodextrin + H2O
isomaltooligosaccharides
Substrates: -
Products: -
Products: -
?
cyclomaltodextrins + H2O
linear maltodextrins
-
Substrates: -
Products: -
Products: -
?
cyclomaltodextrins + H2O
linear maltodextrins
-
Substrates: -
Products: -
Products: -
?
cyclomaltodextrins + H2O
linear maltodextrins
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological role of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological role of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological role of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological role of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological role of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological role of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological role of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological role of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological role of the enzyme, starch utilization pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological role of the enzyme, starch utilization pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological role of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological role of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: inducible enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological role of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological role of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological role of the enzyme
Products: -
Products: -
?
additional information
?
-
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
Substrates: physiological role of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological role of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: physiological role of the enzyme
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
K+
Mg2+
Na+
Ca2+
Ca2+
-
activated and stabilized by Ca2+, relative activity 128.7%
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
PMSF
10 mM, activity decreases by about 50%
Ba2+
WP_000471779.1, Q819G8
5 mM, about 20% loss of activity, substrate: soluble starch; 5 mM, about 80% of initial activity
Ca2+
5 mM, activity decreases by about 66%
Ca2+
WP_000471779.1, Q819G8
5 mM, about 40% loss of activity, substrate: soluble starch; 5 mM, about 65% of initial activity
Co2+
5 mM, activity decreases by about 91%
Co2+
WP_000471779.1, Q819G8
5 mM, complete loss of activity, substrate: soluble starch; 5 mM, no residual activity
Cu2+
WP_000471779.1, Q819G8
5 mM, complete loss of activity, substrate: soluble starch; 5 mM, no residual activity
EDTA
WP_000471779.1, Q819G8
5 mM, about 20% loss of activity, substrate: soluble starch; 5 mM, about 85% of initial activity
Li+
WP_000471779.1, Q819G8
5 mM, about 50% loss of activity, substrate: soluble starch; 5 mM, about 50% of initial activity
Mg2+
5 mM, activity decreases by about 31%
Mg2+
WP_000471779.1, Q819G8
5 mM, about 20% of initial activity; 5 mM, about 80% loss of activity, substrate: soluble starch
Mn2+
WP_000471779.1, Q819G8
5 mM, about 15% of initial activity; 5 mM, about 90% loss of activity, substrate: soluble starch
N-bromosuccinimide
-
0.1 mM, relative activity 8%, 1.0 mM, relative activity 4.6%
Na+
WP_000471779.1, Q819G8
5 mM, about 50% of initial activity; 5 mM, about 60% loss of activity, substrate: soluble starch
Ni2+
WP_000471779.1, Q819G8
5 mM, about 5% of initial activity; 5 mM, about 95% loss of activity, substrate: soluble starch
Zn2+
WP_000471779.1, Q819G8
5 mM, about 10% of initial activity; 5 mM, about 90% loss of activity, substrate: soluble starch
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
5 mM, 24% increase in enzyme activity
EGTA
-
increases activity about 2.3fold, relative activity 236.3%
K+
5 mM, enzyme activity increases by about 49%
Na+
5 mM, enzyme activity increases by about 34%
PMSF
5 mM, 28% increase in enzyme activity
Zn2+
5 mM, enzyme activity increases by about 16%
dithiothreitol
5 mM, 95% increase in enzyme activity
EDTA
5 mM, 34% increase in enzyme activity
EDTA
-
5 mM EDTA, activity increases more than 2fold, relative activity 237.2%
EDTA
-
at 5 mM for isoenzyme ag1B* and ag1B(1Met), no activity against ag1B(2Met)
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Atherosclerosis
Neutral/alkaline and acid ceramidase activities are actively released by murine endothelial cells.
Carcinoma, Hepatocellular
Pharmacological inhibition or small interfering RNA targeting acid ceramidase sensitizes hepatoma cells to chemotherapy and reduces tumor growth in vivo.
Cystic Fibrosis
Expression of intestinal and lung alkaline sphingomyelinase and neutral ceramidase in cystic fibrosis f508del transgenic mice.
Glioma
Antineoplastic effects in rats of 5-fluorocytosine in combination with cytosine deaminase capsules.
Liver Neoplasms
Pharmacological inhibition or small interfering RNA targeting acid ceramidase sensitizes hepatoma cells to chemotherapy and reduces tumor growth in vivo.
Neoplasms
Antineoplastic effects in rats of 5-fluorocytosine in combination with cytosine deaminase capsules.
Neoplasms
Generation of 5-fluorouracil from 5-fluorocytosine by monoclonal antibody-cytosine deaminase conjugates.
Neoplasms
Pharmacological inhibition or small interfering RNA targeting acid ceramidase sensitizes hepatoma cells to chemotherapy and reduces tumor growth in vivo.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
alpha-cyclodextrin
-
Km-value: 4.47 mg/ml, pH 6.0, 95°C
additional information
alpha-cyclodextrin
Km-value: 3.99 mg/ml, pH 7.0, 65°C, wild-type enzyme
additional information
alpha-cyclodextrin
Km-value: 4.22 mg/ml, pH 7.0, 65°C, mutant enzyme H403R
additional information
alpha-cyclodextrin
Km-value: 3.99 mg/ml, pH 7.0, 25°C, wild-type enzyme
additional information
alpha-cyclodextrin
Km-value: 4.35 mg/ml, pH 7.0, 25°C, mutant enzyme A123V
additional information
alpha-cyclodextrin
Km-value: 4.12 mg/ml, pH 7.0, 25°C, mutant enzyme C127Q
additional information
alpha-cyclodextrin
Km-value: 4.71 mg/ml, pH 7.0, 25°C, mutant enzyme A123V/C127Q
additional information
alpha-cyclodextrin
Km-value: 3.99 mg/ml, pH 7.0, 65°C
additional information
beta-cyclodextrin
KM-value is 2.94 mg/ml at pH 7.5 and 65°C
additional information
beta-cyclodextrin
-
Km-value: 11.61 mg/ml, pH 6.0, 95°C
additional information
beta-cyclodextrin
Km-value: 3.45 mg/ml, pH 7.0, 65°C, wild-type enzyme
additional information
beta-cyclodextrin
Km-value: 4.61 mg/ml, pH 7.0, 65°C, mutant enzyme H403R
additional information
beta-cyclodextrin
Km-value: 3.45 mg/ml, pH 7.0, 25°C, wild-type enzyme
additional information
beta-cyclodextrin
Km-value: 4.07 mg/ml, pH 7.0, 25°C, mutant enzyme A123V
additional information
beta-cyclodextrin
Km-value: 3.81 mg/ml, pH 7.0, 25°C, mutant enzyme C127Q
additional information
beta-cyclodextrin
Km-value: 4.3 mg/ml, pH 7.0, 25°C, mutant enzyme A123V/C127Q
additional information
beta-cyclodextrin
Km-value: 3.45 mg/ml, pH 7.0, 65°C
additional information
gamma-cyclodextrin
-
Km-value: 52.14 mg/ml, pH 6.0, 95°C
additional information
gamma-cyclodextrin
Km-value: 2.98 mg/ml, pH 7.0, 65°C, wild-type enzyme
additional information
gamma-cyclodextrin
Km-value: 2.53 mg/ml, pH 7.0, 65°C, mutant enzyme H403R
additional information
gamma-cyclodextrin
Km-value: 2.98 mg/ml, pH 7.0, 25°C, wild-type enzyme
additional information
gamma-cyclodextrin
Km-value: 3.65 mg/ml, pH 7.0, 25°C, mutant enzyme A123V
additional information
gamma-cyclodextrin
Km-value: 3.19 mg/ml, pH 7.0, 25°C, mutant enzyme C127Q
additional information
gamma-cyclodextrin
Km-value: 3.9 mg/ml, pH 7.0, 25°C, mutant enzyme A123V/C127Q
additional information
gamma-cyclodextrin
Km-value: 2.98 mg/ml, pH 7.0, 65°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
373
alpha-cyclodextrin
pH 7.0, 25°C, mutant enzyme A123V/C127Q
410
alpha-cyclodextrin
pH 7.0, 25°C, mutant enzyme A123V
483
alpha-cyclodextrin
pH 7.0, 65°C, mutant enzyme H403R
498
alpha-cyclodextrin
pH 7.0, 25°C, mutant enzyme C127Q
580
alpha-cyclodextrin
pH 7.0, 65°C, wild-type enzyme
580
alpha-cyclodextrin
pH 7.0, 65°C
305
beta-cyclodextrin
pH 7.0, 25°C, mutant enzyme A123V/C127Q
329
beta-cyclodextrin
pH 7.0, 25°C, mutant enzyme A123V
349
beta-cyclodextrin
pH 7.0, 25°C, mutant enzyme C127Q
382
beta-cyclodextrin
pH 7.0, 65°C, wild-type enzyme
447
beta-cyclodextrin
pH 7.0, 65°C, mutant enzyme H403R
231
gamma-cyclodextrin
pH 7.0, 25°C, mutant enzyme A123V/C127Q
254
gamma-cyclodextrin
pH 7.0, 25°C, mutant enzyme A123V
291
gamma-cyclodextrin
pH 7.0, 25°C, mutant enzyme C127Q
308
gamma-cyclodextrin
pH 7.0, 65°C, wild-type enzyme
308
gamma-cyclodextrin
pH 7.0, 65°C
414
gamma-cyclodextrin
pH 7.0, 65°C, mutant enzyme H403R
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
alpha-cyclodextrin
-
kcat/Km: 0.308 mg/ml*s, pH 6.0, 95°C
additional information
alpha-cyclodextrin
kcat/Km-value: 145 mg/ml*s, pH 7.0, 65°C, wild-type enzyme
additional information
alpha-cyclodextrin
kcat/Km-value: 114 mg/ml*s, pH 7.0, 65°C, mutant enzyme H403R
additional information
alpha-cyclodextrin
kcat/Km-value: 145.36 mg/ml*s, pH 7.0, 65°C
additional information
beta-cyclodextrin
-
kcat/Km: 0.1 mg/ml*s, pH 6.0, 95°C
additional information
beta-cyclodextrin
kcat/Km-value: 111 mg/ml*s, pH 7.0, 65°C, wild-type enzyme
additional information
beta-cyclodextrin
kcat/Km-value: 97 mg/ml*s, pH 7.0, 65°C, mutant enzyme H403R
additional information
beta-cyclodextrin
kcat/Km-value: 110.72 mg/ml*s, pH 7.0, 65°C
additional information
gamma-cyclodextrin
-
kcat/Km: 0.016 mg/ml*s, pH 6.0, 95°C
additional information
gamma-cyclodextrin
kcat/Km-value: 103 mg/ml*s, pH 7.0, 65°C, wild-type enzyme
additional information
gamma-cyclodextrin
kcat/Km-value: 164 mg/ml*s, pH 7.0, 65°C, mutant enzyme H403R
additional information
gamma-cyclodextrin
kcat/Km-value: 103.36 mg/ml*s, pH 7.0, 65°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
14.8
176.4
177
-
95°C, pH 5.5, crude recombinant enzyme in Escherichia coli cell extract, substrate is gamma-cyclodextrin
22.4
-
isoenzyme aglB(1Met) after purification, beta-cyclodextrin as substrate
22.8
-
isoenzyme aglB* after purification, beta-cyclodextrin as substrate
3.1
-
isoenzyme aglB(2Met) after purification, beta-cyclodextrin as substrate
535.1
-
95°C, pH 5.5, purified recombinant enzyme, substrate is gamma-cyclodextrin
additional information
additional information
Cda rapidly hydrolyzes only gamma-cyclodextrinase, whereas it slowly hydrolyzes alpha- and beta-cyclodextrinase, maltooctaose, amylose, amylopectin and soluble starch. The hydrolysis activities toward these substrates are less than 4% of that toward gamma-cyclodextrinase. Pullulan and glycogen are hardly hydrolyzed. Cda is a CDase that has high specificity for only gamma-cyclodextrinase
80
additional information
-
potato starch as substrate, maltose, kejibiose, nigeriose, iso-maltose, iso-maltotriose, trehalose and p-nitrophenyl ?-D-glucopyranoside are not used as substrates
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
5.5
5.9
6 - 6.5
6 - 7
6.2
6.5
6.5 - 7
WP_000471779.1, Q819G8
phosphate buffer, no activity detected in 50 mM Tris-HCl buffer at pH 7
7.5
6
carbohydrate-binding module 34 truncated enzyme
6
substrate: alpha-cyclodextrin, phosphate buffer
7
wild-type enzyme and mutant enzyme H403R
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 10
pH 3.0: about 85% of maximal activity, pH 10.0: about 85% of maximal activity
4 - 7
4.5 - 8
pH 4.5: about 60% of maximal activity, pH 8.0: about 60% of maximal activity, carbohydrate-binding module 34 truncated enzyme
5 - 6.5
-
pH 5.0: about 80% of maximal activity, pH 6.5: about 50% of maximal activity
5 - 7
5 - 8
6 - 7
WP_000471779.1, Q819G8
pH 6.0: about 50% of maximal activity, pH 7.0: about 95% of maximal activity, less than 5% activity at pH 7.5, substrate: soluble starch
6 - 8.5
6.5 - 8.5
-
pH 6.5: about 50% of maximal activity, pH 8.5: about 35% of maximal activity, substrate: cyclomaltoheptaose
additional information
5 - 7
pH 5.0: about 75% of maximal activity, pH 7.0: about 80% of maximal activity
5 - 7
pH 5.0: about 30% of maximal activity, pH 7.0: about 50% of maximal activity
5 - 8
-
about 87% activity at pH 5.0, 100% activity at pH 6.0, about 75% activity at pH 7.0, about 50% activity at pH 8.0
6 - 8.5
pH 6.0: about 45% of maximal activity, pH 8.5: about 55% of maximal activity, wild-type enzyme
6 - 8.5
pH 6.0: about 15% of maximal activity, pH 8.5: about 75% of maximal activity, mutant enzyme H403Ry
6 - 8.5
pH 6.0: about 30% of maximal activity, pH 8.5: about 30% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
40
42
45
50
55
60
65
70
85
90
95
42
-
crude enzyme, incubation at 37°C and higher for longer than 24 h, significant loss of activity
50
-
pullulan, optimum temperature variable depending on the substrate
55
carbohydrate-binding module 34 truncated enzyme
55
-
crude enzyme, incubation at 4-55°C for 48 h, little loss of activity
65
wild-type enzyme and mutant enzyme H403R
85
-
recombinant enzyme, substrates cyclomaltodextrins, starch, and acarbose
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 70
30 - 55
30 - 60
-
30°C: about 45% of maximal activity, 60°C: about 80% of maximal activity, substrate: cyclomaltoheptaose
35 - 40
WP_000471779.1, Q819G8
35°C: about 50% of maximal activity, 40°C: about 30% of maximal activity, substrate: soluble starch
35 - 60
35°C: about 80% of maximal activity, 60°C: about 90% of maximal activity, carbohydrate-binding module 34 truncated enzyme
40 - 75
40°C: about 40% of maximal activity, 75°C: about 45% of maximal activity
45 - 65
45°C: about 50% of maximal activity, 65°C: about 55% of maximal activity
45 - 70
50 - 90
50°C: about 55% of maximal activity, 90°C: about 80% of maximal activity
52 - 60
-
52°C: about 50% of maximal activity, 60°C: about 30% of maximal activitry
70 - 100
75 - 100
75°C: about 50% of maximal activity, 100°C: about 80% of maximal activity
80 - 105
-
80°C: about 50% of maximal activity, 105°C: about 50% of maximal activity
20 - 70
-
20°C: about 65% of maximal activity, 70°C: about 40% of maximal activity
45 - 70
45°C: about 50% of maximal activity, 70°C: about 70% of maximal activitry
45 - 70
45°C: about 55% of maximal activity, 70°C: about 70% of maximal activity
45 - 70
45°C: about 55% of maximal activity, 70°C: about 75% of maximal activity
70 - 100
-
70°C: about 60% of maximal activity, 95°C: about 70% of maximal activity, 100°C: about 20% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from a Paralvinella sp. polychaete worm collected from an active deep-sea hydrothermal vent sulfide chimney, gene CL1_0884 or tccd
UniProt
brenda
Env Cda13A can be classified into the neopullulanase subfamily consisting of neopullulanases, cyclomaltodextrinases and maltogenic amylases
-
-
brenda
bifunctional enzyme with combined activities of alpha-amylase and CD-/pullulan-degrading enzyme
-
-
brenda
bifunctional enzyme with combined activities of alpha-amylase and CD-/pullulan-degrading enzyme
-
-
brenda
strain I-5 and the alkalophilic enzyme-containing strain
-
-
brenda
isolated from a Paralvinella sp. polychaete worm collected from an active deep-sea hydrothermal vent sulfide chimney, gene CL1_0884 or tccd
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
recombinant enzyme is produced in Escherichia coli primarily in
brenda
-
recombinant enzyme is produced in Escherichia coli primarily in
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
evolution
cyclomaltodextrinase is a member of the glycoside hydrolase family 13, GH13. The N-terminal extra domain of these enzymes is known to be composed of all of the substrate-binding components in a monomeric unit, which is generally provided by the dimeric N-domain position in bacterial enzymes
evolution
in the phylogenetic tree, carbohydrate-binding module 34 of the cyclomaltodextrinase from Geobacillus thermopakistaniensis groups together with counterparts from genera Bacillus, Thermus and Geobacillus. The nearest homolog is an enzyme from Bacillus sp. WPD616, followed by Thermus sp. IM6501. The evolutionary tree shows close relatedness among most of the Bacilli
evolution
-
cyclomaltodextrinase is a member of the glycoside hydrolase family 13, GH13. The N-terminal extra domain of these enzymes is known to be composed of all of the substrate-binding components in a monomeric unit, which is generally provided by the dimeric N-domain position in bacterial enzymes
-
evolution
-
the enzyme belongs to the cyclodextrinase family of enzymes
-
evolution
-
in the phylogenetic tree, carbohydrate-binding module 34 of the cyclomaltodextrinase from Geobacillus thermopakistaniensis groups together with counterparts from genera Bacillus, Thermus and Geobacillus. The nearest homolog is an enzyme from Bacillus sp. WPD616, followed by Thermus sp. IM6501. The evolutionary tree shows close relatedness among most of the Bacilli
-
malfunction
truncation of the carbohydrate-binding module 34 leads to an overall decrease in binding affinity and reversed the order of substrate preference
malfunction
-
truncation of the carbohydrate-binding module 34 leads to an overall decrease in binding affinity and reversed the order of substrate preference
-
physiological function
the characteristic of the enzyme hydrolyzing beta-cyclodextrin at a relatively low temperature and nonneutral pH should play an important role in the survival of Thermococcus kodakarensis KOD1 under low temperature conditions (65°C)
physiological function
WP_000471779.1, Q819G8
the enzyme is likely to be involved in the maltodextrin metabolism in Bacillus cereus
physiological function
Bacillus cereus ATCC 14,579
-
the enzyme is likely to be involved in the maltodextrin metabolism in Bacillus cereus
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CDAS_GEOTM
Geobacillus thermopakistaniensis (strain MAS1)
588
0
68157
Swiss-Prot
-
CDAS_THEP3
Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E)
574
0
68066
Swiss-Prot
-
AGLB_THEMA
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
473
0
55181
Swiss-Prot
-
A0A0Y0H9K3_9BACL
587
0
68837
TrEMBL
-
I3ZTQ5_THECF
Thermococcus cleftensis (strain DSM 27260 / KACC 17922 / CL1)
644
0
75478
TrEMBL
-
Q5BLZ6_9BACL
586
0
69016
TrEMBL
other Location (Reliability: 1)
Q5JJ59_THEKO
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
656
0
76349
TrEMBL
-
Q819G8_BACCR
Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711)
586
0
68241
TrEMBL
Secretory Pathway (Reliability: 2)
Q8TZP8_PYRFU
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
645
0
76084
TrEMBL
-
B2IUW9_NOSP7
Nostoc punctiforme (strain ATCC 29133 / PCC 73102)
488
0
55582
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
148000
55000
61000
62000
65000
66000
67000
68030
-
denatured protein estimated by SDS-PAGE, native enzyme determined by gel filtration
69000
71000
72000
75956
1 * 65000, recombinant His6-tagged enzyme, SDS-PAGE and gel filtration, 1 * 75956, sequence calculation
76084
67000
-
2 * 67000, molecular weight estimated to be 126000 by gel filtration, 67000 by SDS-PAGE
71000
-
2 * 71000, at pH 6.5, the enzyme exiosts mainly as dimer, SDS-PAGE
71000
2 * 71000, at pH 6.5, the enzyme exiosts mainly as dimer, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
dodecamer
-
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
-
additional information
-
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
-
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, 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, 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, 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
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
10 mg/ml purified recombinant enzyme in 10 mM HEPES, pH 7.5 and 1 mM 2-mercaptoethanol, hanging drop vapour diffusion method by addition of equal amount of 0.002 ml of precipitant solution containing 50% PEG 200, and 0.1 M HEPES, pH 7.0, equilibration against 1 ml, 22°C, X-ray diffraction structure determination and analysis at 3.3 A resolution
-
6 mg/ml purified recombinant enzyme as native and selenomethionine derivatives in 50 mM HEPES, pH 7.5, 3.8 M NaCl, and 3 mM DTT with the SeM-enzyme derivative, equal volumes of protein and reservoir solution, hanging drop vapour diffusion method, 2 days, 15% glycerol for cryoprotection, multiwavelength anomalous X-ray diffraction 3D-structure determination and analysis at 2.1 A resolution
mutant E340Q alpha-cyclodextrin complex, 0.1 M HEPES, 3.8 M NaCl, 3 mM CaCl2, pH 7.5, vapor diffusion, hanging drop, temperature 20°C, X-ray diffraction structure determination and analysis at 2.65 A resolution, space group H 3 2, T79P contact mutant, 0.1 M Tris, 17% PEG1500, pH 8.75, vapor diffusion, hanging drop, temperature 20°C, X-ray diffraction structure determination and analysis at 1.71 A resolution, space group P 21 21 2, mutant T49P, E340Q alpha-cyclodextrin complex, 0.1 M Tris, 17% PEG1500, pH 8.75, vapor diffusion, hanging drop, temperature 20°C, X-ray diffraction structure determination and analysis at 1.65 A resolution, space group P 21 21 2, mutant T49P, E340Q beta-cyclodextrin complex, resolution 1.69 A, mutant T49P, E340Q gamma-cyclodextrin complex, resolution 1.77 A
sitting drop method at 18°C. The structure studies supporting the proposition that cyclodextrin-hydrolyzing amylases from hyperthermophilic microorganisms contain all of the structural components required for substrate binding within a single monomer, distinguishing PFTA from the classical bacterial cyclodextrin-hydrolyzing enzymes of the GH13 family
purified recombinant TVAII mutant enzyme D325N complexed with alpha-panosylpanose, hanging drop vapour diffusion method, 0.0015 ml of 20 mg/ml protein in 5 m Tris-HCl, pH 7.5, is mixed with 0.0015 ml of reservoir solution containing 1% w/v PEG 6000, 5 mM CaCl2, and 40 mM MES-NaOH, pH 6.1, soaking of crystals in cryoprotection solution containing 20% v/v 2-methyl-2,4-pentanediol, 20% w/v PEG 6000, and 2.5 mM CaCl2, X-ray diffraction structure determination and analysis at 2.2 A resolution, modelling
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A123V
increase in Tm-value as compared to wild-type enzyme. kcat/Km is 1.5fold lower than the kcat/Km value for alpha-cyclodextrin for the wild-type enzyme
A123V/C127Q
increase in Tm-value as compared to wild-type enzyme. kcat/Km is 1.8fold lower than the kcat/Km value alpha-cyclodextrin for the wild-type enzyme
C127Q
increase in Tm-value as compared to wild-type enzyme. kcat/Km is 1.2fold lower than the kcat/Km value for alpha-cyclodextrin for the wild-type enzyme
H403R
H49V/H539V
-
the mutant enzyme dissociates into dimers faster than the wild-type enzyme at both pH 6.0 and 7.0
H49V/H89V/H539V
-
the mutant enzyme dissociates into dimers faster than the wild-type enzyme at both pH 6.0 and 7.0
I388E
-
mutant from strain I-5, decreased hydrophobicity, between the third and the fourth conserved region resulting in decreased cyclomaltodextrin degrading activity
V380T
-
mutant from strain I-5, decreased hydrophobicity, between the third and the fourth conserved region resulting in decreased cyclomaltodextrin degrading activity
H49V/H539V
-
the mutant enzyme dissociates into dimers faster than the wild-type enzyme at both pH 6.0 and 7.0
-
H49V/H89V/H539V
-
the mutant enzyme dissociates into dimers faster than the wild-type enzyme at both pH 6.0 and 7.0
-
E340Q
The active center mutant E340Q yields as much purified protein as the wild-type, and shows a residual, though very low, activity for alpha-cyclomaltodextrinase as derived from the crystal structure analysis
R464A
Arg464 is suggested to chaperone the substrates to the active center of the same enzyme subunit
R464S
Arg464 is suggested to chaperone the substrates to the active center of the same enzyme subunit
T49P
molucular weight 132000, mutant T49P, which causes the dissociation of the tetrameric wild-type FspCMD to the tight dimers, reduces the activity to less than 50% with a particularly strong reduction for beta-cyclomaltodextrinase and gamma-cyclomaltodextrinase
G415E
H414N
-
the hydrolysis of beta-cyclodextrins decreases 10fold. Substrate preference is similar to that of the wild-type enzyme
H414N/G415E
-
the hydrolysis of beta-cyclodextrins decreases 8fold. Mutant enzyme exhibits strongly enhanced alpha-(1,4)-transglycosylation activity, resulting in the production of a series of maltooligosaccharides that are longer than the initial substrates
Y374A
-
site-directed mutagenesis, the mutant shows reduced activity, and altered substrate specificity and kinetics compared to the wild-type enzyme
Y374A
-
site-directed mutagenesis, the mutant shows reduced activity, and altered substrate specificity and kinetics compared to the wild-type enzyme
-
additional information
H403R
the optimum values of pH and temperature in mutant enzyme is the same as wild-type enzyme. The activity at optimum points increases in H403R variant. The H403R variant has slightly improved catalytic efficiency for gamma-CD. The same value of activation parameters for both protein variants indicates that mutation does not alter the mechanism of catalysis during enzyme-substrate formation
H403R
-
the optimum values of pH and temperature in mutant enzyme is the same as wild-type enzyme. The activity at optimum points increases in H403R variant. The H403R variant has slightly improved catalytic efficiency for gamma-CD. The same value of activation parameters for both protein variants indicates that mutation does not alter the mechanism of catalysis during enzyme-substrate formation
-
G415E
-
the hydrolysis of beta-cyclodextrins decreases 80fold. Substrate preference is similar to that of the wild-type enzyme
G415E
the mutant enzyme reveals considerable differences in substrate preference relative to the wild-type enzyme. Increased substrate selectivity of the mutant enzyme for the beta-cyclodextrin substrate, whereas the mutant shows no difference in activity for the maltoheptaose substrate
additional information
-
construction of a mutant enzyme lacking the C-terminal domain, expression as insoluble protein in Escherichia coli
additional information
the double mutant T49P-G523R does not show a clear monomer mass
additional information
thermostability of carbohydrate-binding module 34 truncated enzyme decreases to about 50% and 22% after 5 h incubation at 60°C and 65°C, respectively, whereas the full length enzyme retains nearly all of its activity when incubated at the same temperatures and for the same duration of time
additional information
-
thermostability of carbohydrate-binding module 34 truncated enzyme decreases to about 50% and 22% after 5 h incubation at 60°C and 65°C, respectively, whereas the full length enzyme retains nearly all of its activity when incubated at the same temperatures and for the same duration of time
-
additional information
-
single mutants of the catalytic residues Asp325, Glu354, and Asp421 are catalytically inactive
additional information
-
single mutants of the catalytic residues Asp325, Glu354, and Asp421 are catalytically inactive
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
6.5 - 8
the enzyme remains 100% active when incubated at pH values 6.5 and 8.0 after 24 h of incubation, and is 60% active when incubated at pH 7.0 for 24 h
6.8
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
25 - 50
the enzyme remains stable after 30 min incubation at 45°C and loses all its activity when incubated for 30 min at 50°C. The temperature at which the enzyme loses 50% of its activity with 2 mM calcium is 48.5°C. The enzyme remains 60% active after 24 h at 25 or 40°C but is 20% active at 0°C
40
42
-
MalZ loses its native conformation and undergoes aggregation during incubation at 42°C., thermoprotection is achieved by proline, glycerol, dimethylsulfoxide or trimethylamine-N-oxide
57
-
complete loss of activity after 20 min without calcium, completely stable after 120 min in presence of 1 mM calcium
60
60 - 70
-
enzyme half-life 402 min at 60°C, 180 min at 65°C, 75 min at 70°C
65
70
75
75 - 95
-
the enzyme retains more than 90% activity after 8 h at 75-85°C. At 95°C, the enzyme shows about 77%, 45%, 30% and less than 20% activity after 1 h, 2 h, 4 h and 8 h, respectively
85
90
93
purified enzyme, melting temperature, differential scanning calorimetry and differential scanning fluorimetry analysis
95
additional information
100
-
purified recombinant enzyme, sodium acetate buffer, pH 5.0, loss of 65% activity within 60 min
60
half-life: 20 min. Thermal inactivation is not significantly affected by addition of calcium
60
5 h, full length enzyme retains nearly all of its activity, carbohydrate-binding module 34 truncated enzyme decreases to about 50% of its activity
60
-
half-life: 4 min, in absence of calcium. 50% loss of activity after 120 min in presence of 1 mM calcium
65
60 min, the enzyme retains 70% of its initial activity
65
100 min, the enzyme retains 50% of its initial activity
65
5 h, full length enzyme retains nearly all of its activity, carbohydrate-binding module 34 truncated enzyme decreases to 22% of its activity
65
-
incubation for 1 h led to a 15% loss of activity
70
30 min, the enzyme retains 50% of its initial activity
70
half-life: 90 min, 360 min (in presence of EDTA)
75
5 min, complete loss of activity
85
-
purified recombinant enzyme, sodium acetate buffer, pH 5.0, completely stable for 120 min
90
-
purified recombinant enzyme, sodium acetate buffer, pH 5.0, loss of 15-20% activity within 120 min
90
180 min, the enzyme retains about 40% of its initial activity. 30 min, the enzyme retains about 60% of its initial activity
90
-
half-inactivation time of AglB(2Met) at 90°C is 5 min, for AglB* and AglB(1Met) 3 h
95
-
purified recombinant enzyme, sodium acetate buffer, pH 5.0, loss of 25% activity within 120 min
additional information
EDTA enhances the thermostability
60 - 80
additional information
-
half-life at 60°, 65°, 70° and 80°C is 600, 480, 30 and 12 min, respectively, independent on the pH and the presence of Ca2+
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
denaturation and unfolding induced with 2 M guanidine hydrochloride pH 7.0 or 25 mM glycine phosphate buffer, pH 2 for 4 h at 25°C, chaperons GroEL, GroES assist in vivo and in vitro folding of the enzyme, a trans folding mechanism for GroEL/GroES-assisted refolding of MalZ is proposed
-
EDTA induces structural changes in the enzyme in terms of chirality, and enhances the thermostability of the enzyme
more than 90% of the enzyme activity remains in the pH range of 8.0-10.0 and at 4°C in the absence of CaCl2 after pH and temperature treatments, respectively. Cda is efficiently stabilized by CaCl2. In the presence of CaCl2. Cda is stable in the pH range of 7.0-10.5 and at temperatures below 30°C.
pH 7.0, 8 M urea and 20 mM dithiothreitol, glycerol, dimethylsulfoxide, trimethylamine-N-oxide, trehalose and proline act as chemical chaperones in the refolding of the denatured MalZ, GroEL, GroES and ATP-mediated refolding of urea
-
stable in the presence of up to 2% Triton X-100, completely inactivated in the presence of SDS at concentrations higher than 50 mM
additional information
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
urea
-
chemical chaperones inhibit denaturation induced by chaotropic agents such as urea
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by Q-sepharose column, DEAE-Sepharose column, Bioprep SE 1000/17 and UNO S1 column chromatography
-
gene encoding enzyme cloned in Escherichia coli, expressed and purified 12fold from Escherichia coli
-
gene encoding enzyme cloned in Escherichia coli, expressed and purified from Escherichia coli
-
of the recombinant protein
purified 40fold, highly purified, not completely free from contaminations
-
recombinant enzyme from Escherichia coli by ammonium sulfate precipitation and Sepharose Q chromatography
-
recombinant His-tagged enzyme 3.0fold from Escherichia coli by heat treatment and nickel affinity chromatography
-
recombinant His6-tagged enzyme from Escherichia coli strain BL21-CodonPlus(DE3)-RP by nickel affinity chromatography and dialysis
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
CDase I-5 gene, pBR322, expression in Escherichia coli MC1061
-
DNA and amino acid sequence determination and analysis, expression as native and selenomethionine derivatives in Eschrichia coli BL21(DE3) and B834 (DE3), respectively
DNA and amino acid sequence determination and analysis, recombinant expression of N-terminally His6-tagged dimeric enzyme in Escherichia coli
-
DNA sequence determination and analysis, expression in Escherichia coli
-
expression in Escherichia coli
expression in Escherichia coli BL21 (DE3)
expression in Escherichia coli BL21 CodonPlus (DE3)
expression in Escherichia coli BL21(DE3). Synergistic effect of glycine-Ca2+ supplementation and deletion of genes related to LPS synthesis (lpxM) on the extracellular secretion of recombinant enzyme (CDase)
expression of wild-type and mutant enzymes in Escherichia coli strain MC1061
-
gene cgtB, DNA and amino acid sequence determination and analysis, expression in Escherichia coli BL21(DE3)
-
gene CL1_0884, DNA and amino acid sequence determination and analysis, sequence comparisons and genetic structure, phylogenetic analysis, expression of His6-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3)-RP
gene Tpen_1458, DNA and amino acid sequence determination and analysis, phylogenetic tree, expression as His-tagged enzyme in Escherichia coli strain MC1061
-
optimized expression in Escherichia coli by using a soluble fusion-tag and by tuning of inducer concentration
-
overexpression in Escherichia coli, three expression vectors are constructed, aglB gene linked to an upstream 90-bp 30-terminal region of the malG gene with the stop codon overlapping with the start codon of aglB, aglB with two tandem potential start codons and ag1B with only one start codon
-
PTFA, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3) and MC1061
-
expression in Escherichia coli BL21 (DE3)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
biotechnology
food industry
industry
synthesis
additional information
analysis
-
synthesis of radiolabeled linear and cyclic maltodextrins as tools for metabolism investigation
analysis
-
synthesis of radiolabeled linear and cyclic maltodextrins as tools for metabolism investigation
-
biotechnology
-
Archaeoglobus fulgidus utilizes an unusual pathway of starch degradation involving cyclodextrins as intermediates, extracellular cyclodextrins are transported into the cell and linearized via a CDase
biotechnology
-
chemical or molecular operones can be used in refolding of various aggregate-prone proteins of commercial and medical importance after overexpression in Escherichia coli
biotechnology
-
Archaeoglobus fulgidus utilizes an unusual pathway of starch degradation involving cyclodextrins as intermediates, extracellular cyclodextrins are transported into the cell and linearized via a CDase
-
food industry
the extremely thermostable enzyme might be of potential value in the production of isomaltooligosaccharides in the food industry
food industry
-
cyclodextrinase can hardly modify starch, but replaces the excess cyclodextrins produced by beta-cyclodextrin glycosyltransferase with malto-oligosaccharides which is beneficial to the human body and food properties. There is an apparent synergistic effect between cyclodextrinase and beta-cyclodextrin glycosyltransferase, resulting in a reaction efficiency improvement
food industry
one-pot production of maltoheptaose from starch by sequential addition of cyclodextrin glucotransferase and cyclomaltodextrinase. Maltoheptaose (i.e. amyloheptaose) is one of the maltodextrin mixtures widely used in foods, cosmetics, and pharmaceutical industries. The one-pot cascade reaction converts 30 g/l of soluble starch to 5.4 g/l of maltoheptaose in 1 h reaction time with a conversion rate of 16%
food industry
the enzyme is able to prepare higher yield of maltoheptaose through conversion of beta-cyclodextrin in the food industry
food industry
-
one-pot production of maltoheptaose from starch by sequential addition of cyclodextrin glucotransferase and cyclomaltodextrinase. Maltoheptaose (i.e. amyloheptaose) is one of the maltodextrin mixtures widely used in foods, cosmetics, and pharmaceutical industries. The one-pot cascade reaction converts 30 g/l of soluble starch to 5.4 g/l of maltoheptaose in 1 h reaction time with a conversion rate of 16%
-
food industry
-
the extremely thermostable enzyme might be of potential value in the production of isomaltooligosaccharides in the food industry
-
industry
one-pot production of maltoheptaose from starch by sequential addition of cyclodextrin glucotransferase and cyclomaltodextrinase. Maltoheptaose (i.e. amyloheptaose) is one of the maltodextrin mixtures widely used in foods, cosmetics, and pharmaceutical industries. The one-pot cascade reaction converts 30 g/l of soluble starch to 5.4 g/l of maltoheptaose in 1 h reaction time with a conversion rate of 16%
industry
-
one-pot production of maltoheptaose from starch by sequential addition of cyclodextrin glucotransferase and cyclomaltodextrinase. Maltoheptaose (i.e. amyloheptaose) is one of the maltodextrin mixtures widely used in foods, cosmetics, and pharmaceutical industries. The one-pot cascade reaction converts 30 g/l of soluble starch to 5.4 g/l of maltoheptaose in 1 h reaction time with a conversion rate of 16%
-
synthesis
-
CDase I-5 is applied to modify the starch structure to produce low-amylose starch products by incubating rice starch with this enzyme. The amylose content of rice starch decreases from 28.5 to 9% while the amylopectin content remains almost constant with no significant change in side chain length distribution
synthesis
the G415E mutant is an excellent candidate for the industrial production of specific-length maltooligosaccharides from cyclodextrins
synthesis
-
application of cyclodextrinase in non-complexant production of gamma-cyclodextrin
additional information
-
neopullulanases, cyclomaltodextrinases and maltogenic amylases display similar biochemical properties and share almost the same 3D structures, enzymes should be classified under the same name and enzyme code, cyclodextrins are the most preferred substrates
additional information
-
neopullulanases, cyclomaltodextrinases and maltogenic amylases display similar biochemical properties and share almost the same 3D structures, enzymes should be classified under the same name and enzyme code, cyclodextrins are the most preferred substrates
additional information
-
neopullulanases, cyclomaltodextrinases and maltogenic amylases display similar biochemical properties and share almost the same 3D structures, enzymes should be classified under the same name and enzyme code, cyclodextrins are the most preferred substrates
additional information
-
neopullulanases, cyclomaltodextrinases and maltogenic amylases display similar biochemical properties and share almost the same 3D structures, enzymes should be classified under the same name and enzyme code, cyclodextrins are the most preferred substrates
additional information
-
neopullulanases, cyclomaltodextrinases and maltogenic amylases display similar biochemical properties and share almost the same 3D structures, enzymes should be classified under the same name and enzyme code, cyclodextrins are the most preferred substrates
additional information
-
neopullulanases, cyclomaltodextrinases and maltogenic amylases display similar biochemical properties and share almost the same 3D structures, enzymes should be classified under the same name and enzyme code, cyclodextrins are the most preferred substrates
additional information
-
neopullulanases, cyclomaltodextrinases and maltogenic amylases display similar biochemical properties and share almost the same 3D structures, enzymes should be classified under the same name and enzyme code, cyclodextrins are the most preferred substrates
additional information
-
neopullulanases, cyclomaltodextrinases and maltogenic amylases display similar biochemical properties and share almost the same 3D structures, enzymes should be classified under the same name and enzyme code, cyclodextrins are the most preferred substrates
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kitahata, S.; Taniguchi, M.; Beltran, S.D.; Sugimoto, T.; Okada, S.
Purification and some properties of cyclodextrinase from Bacillus coagulans
Agric. Biol. Chem.
47
1441-1447
1983
Heyndrickxia coagulans
-
brenda
DePinto, J.A.; Campbell, L.L.
Purification and properties of the cyclodextrinase of Bacillus macerans
Biochemistry
7
121-125
1968
Paenibacillus macerans, Paenibacillus macerans ATCC 8514
brenda
DePinto, J.A.; Campbell, L.L.
Pattern of action of the amylase and the cyclodextrinase of Bacillus macerans
Arch. Biochem. Biophys.
125
253-258
1968
Paenibacillus macerans, Paenibacillus macerans ATCC 8514
brenda
Antenucci, R.N.; Palmer, J.K.
Enzymatic degradation of alpha- and beta-cyclodextrins by bacteroides of the human colon
J. Agric. Food Chem.
32
1316-1321
1984
Parabacteroides distasonis, Bacteroides ovatus, Bacteroides ovatus 3524, Parabacteroides distasonis C18-7
-
brenda
Kitahata, S.; Okada, S.
Hydrolytic action on various maltosides by an enzyme from Bacillus coagulans
Carbohydr. Res.
137
217-225
1985
Heyndrickxia coagulans
-
brenda
Badal, C.S.; Zeikus, J.G.
Characterization of thermostable cyclodextrinase from Clostridium thermohydrosulfuricum 39E
Appl. Environ. Microbiol.
9
2941-2943
1990
Thermoanaerobacter thermohydrosulfuricus, Thermoanaerobacter thermohydrosulfuricus 39E
-
brenda
Yoshida, A.; Iwasaki, Y.; Akiba, T.; Horikoshi, K.
Purification and properties of cyclomaltodextrinase from alkalophilic Bacillus sp.
J. Ferment. Bioeng.
71
226-229
1991
Niallia circulans
-
brenda
Oguma, T.; Kikuchi, M.; Mizusawa, K.
Hydrolysis of branched cyclodextrins by a cyclodextrin-hydrolyzing enzyme from Bacillus sphaericus E-244
FEBS Lett.
290
13-16
1991
Lysinibacillus sphaericus, Lysinibacillus sphaericus E-244
brenda
Bradley, M.K.; Lindsay, J.A.
Reclassification of a thermostable alpha-glucosidase from Bacillus subtilis H-17 as a cyclomaltodextrinase
Enzyme Microb. Technol.
14
194-196
1992
Bacillus subtilis
-
brenda
Podkovyrov, S.M.; Zeikus, J.G.
Structure of the gene encoding cyclomaltodextrinase from Clostridium thermohydrosulfuricum 39E and characterization of the enzyme purified from Escherichia coli
J. Bacteriol.
8
5400-5405
1992
Thermoanaerobacter thermohydrosulfuricus, Thermoanaerobacter thermohydrosulfuricus 39E
brenda
Bender, H.
Purification and characterization of a cyclodextrin-degrading enzyme from Flavobacterium sp.
Appl. Microbiol. Biotechnol.
39
714-719
1993
Flavobacterium sp.
-
brenda
Galvin, N.M.; Kelly, C.T.; Fogarty, W.M.
Purification and properties of the cyclodextrinase of Bacillus sphaericus ATCC 7055
Appl. Microbiol. Biotechnol.
42
46-50
1994
Lysinibacillus sphaericus
-
brenda
Bender, H.
Purification and characterization of a soluble, cytoplasmic decycling maltodextrinase from a Lactobacillus species, strain 26X, isolated from kitchen waste water
Appl. Microbiol. Biotechnol.
43
838-843
1995
Lactobacillus sp.
-
brenda
Zhong, W.; Zheng, Z.S.; Jun, Y.S.
Purification and properties of cyclodextrinase from Bacillus stearothermophilus HY-1
Appl. Biochem. Biotechnol.
59
63-75
1996
Geobacillus stearothermophilus, Geobacillus stearothermophilus HY-1
-
brenda
Feederle, R.; Pajatsch, M.; Kremmer, E.; Bck, A.
Metabolism of cyclodextrins by Klebsiella oxytoca M5a1: purification and characterisation of a cytoplasmically located cyclodextrinase
Arch. Microbiol.
165
206-212
1996
Klebsiella oxytoca, Klebsiella oxytoca M5a1
brenda
Pajatsch,M.; Bck, A.; Boos, W.
Enzymatic preparation of radiolabeled linear maltodextrins and cyclodextrins of high specific activity from [14C]maltose using amylomaltase, cyclodextrin glucosyltransferase and cyclodextrinase
Carbohydr. Res.
307
375-379
1998
Klebsiella oxytoca, Klebsiella oxytoca M5a1
brenda
Kim, T.J.; Shin, J.H.; Oh, J.H.; Kim, M.J.; Lee, S.B.; Ryu, S.; Kwon, K.; Kim, J.W.; Choi, E.H.; Robyt, J.F.; Park, K.H.
Analysis of the gene encoding cyclomaltodextrinase from alkalophilic Bacillus sp. I-5 and cgaracterization of enzymatic properties
Arch. Biochem. Biophys.
353
221-227
1998
Bacillus sp. (in: firmicutes), Bacillus sp. (in: firmicutes) I-5
brenda
Matzke, J.; Herrmann, A.; Schneider, E.; Bakker, E.P.
Gene cloning, nucleotide sequence and biochemical properties of a cytoplasmic cyclomaltodextrinase (neopullunase) from Alicyclobacillus acidocaldarius, reclassification of a group of enzymes
FEMS Microbiol. Lett.
183
55-61
2000
Alicyclobacillus acidocaldarius, Alicyclobacillus acidocaldarius ATCC 27009
brenda
Kim, M.J.; Park, W.S.; Lee, H.S.; Kim, T.J.; Shin, J.H.; Yoo, S.H.; Cheong, T.K.; Ryu, S.; Kim, J.C.; Kim, K.W.; Moon, T.W.; Robyt, J.F.; Park, K.H.
Kinetics and inhibition of cyclomaltodextrinase from alkalophilic Bacillus sp. I-5
Arch. Biochem. Biophys.
373
110-115
2000
Bacillus sp. (in: firmicutes), Bacillus sp. (in: firmicutes) I-5
brenda
Yang, S.J.; Wang, Z.; Zhang, S.Z.
Purification and properties of cyclodextrinase from Bacillus stearothermophilus HY-1
Ann. N. Y. Acad. Sci.
799
425-428
1996
Geobacillus stearothermophilus, Geobacillus stearothermophilus HY-1
-
brenda
Lee, H.S.; Kim, M.S.; Cho, H.S.; Kim, J.I.; Kim, T.J.; Choi, J.H.; Park, C.; Oh, B.H.; Park, K.H.
Cyclomaltodextrinase, neopullulanase, and maltogenic amylase are nearly indistinguishable from each other
J. Biol. Chem.
277
21891-21897
2002
Bacillus sp. (in: firmicutes)
brenda
Park, K.H.; Kim, T.J.; Cheong, T.K.; Kim, J.W.; Oh, B.H.; Svensson, B.
Structure, specificity and function of cyclomaltodextrinase, a multispecific enzyme of the alpha-amylase family
Biochim. Biophys. Acta
1478
165-185
2000
Alicyclobacillus acidocaldarius, Bacillus sp. (in: firmicutes), Bacteroides ovatus, Escherichia coli, Flavobacterium sp., Geobacillus stearothermophilus, Geobacillus stearothermophilus K-12481, Heyndrickxia coagulans, Klebsiella oxytoca, Klebsiella oxytoca M5a1, Lysinibacillus sphaericus, Paenibacillus macerans, Thermoanaerobacter ethanolicus, Thermoanaerobacter ethanolicus 39E, Thermotoga maritima, Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589, Xanthomonas campestris, Xanthomonas campestris K-11151
brenda
Fritzsche, H.B.; Schwede, T.; Schulz, G.E.
Covalent and three-dimensional structure of the cyclodextrinase from Flavobacterium sp. no. 92
Eur. J. Biochem.
270
2332-2341
2003
Flavobacterium sp. (Q8KKG0)
brenda
Hashimoto, Y.; Yamamoto, T.; Fujiwara, S.; Takagi, M.; Imanaka, T.
Extracellular synthesis, specific recognition, and intracellular degradation of cyclomaltodextrins by the hyperthermophilic archaeon Thermococcus sp. strain B1001
J. Bacteriol.
183
5050-5057
2001
Thermococcus sp.
brenda
Yang, S.J.; Lee, H.S.; Park, C.S.; Kim, Y.R.; Moon, T.W.; Park, K.H.
Enzymatic analysis of an amylolytic enzyme from the hyperthermophilic archaeon Pyrococcus furiosus reveals its novel catalytic properties as both an alpha-amylase and a cyclodextrin-hydrolyzing enzyme
Appl. Environ. Microbiol.
70
5988-5995
2004
Pyrococcus furiosus
brenda
Kaulpiboon, J.; Pongsawasdi, P.
Purification and characterization of cyclodextrinase from Paenibacillus sp. A11
Enzyme Microb. Technol.
36
168-175
2005
Paenibacillus sp., Paenibacillus sp. A11
-
brenda
Mizuno, M.; Tonozuka, T.; Uechi, A.; Ohtaki, A.; Ichikawa, K.; Kamitori, S.; Nishikawa, A.; Sakano, Y.
The crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVA II) complexed with transglycosylated product
Eur. J. Biochem.
271
2530-2538
2004
Thermoactinomyces vulgaris, Thermoactinomyces vulgaris R-47
brenda
Lee, H.S.; Kim, J.S.; Shim, K.; Kim, J.W.; Inouye, K.; Oneda, H.; Kim, Y.W.; Cheong, K.A.; Cha, H.; Woo, E.J.; Auh, J.H.; Lee, S.J.; Kim, J.W.; Park, K.H.
Dissociation/association properties of a dodecameric cyclomaltodextrinase. Effects of pH and salt concentration on the oligomeric state
FEBS J.
273
109-121
2006
Bacillus sp. (in: firmicutes), Bacillus sp. (in: firmicutes) I-5
brenda
Auh, J.H.; Chae, H.Y.; Kim, Y.R.; Shim, K.H.; Yoo, S.H.; Park, K.H.
Modification of rice starch by selective degradation of amylose using alkalophilic Bacillus cyclomaltodextrinase
J. Agric. Food Chem.
54
2314-2319
2006
Bacillus sp. (in: firmicutes)
brenda
Kaulpiboon, J.; Pongsawasdi, P.
Expression of cyclodextrinase gene from Paenibacillus sp. A11 in Escherichia coli and characterization of the purified cyclodextrinase
J. Biochem. Mol. Biol.
37
408-415
2004
Paenibacillus sp., Paenibacillus sp. A11
brenda
Turner, P.; Labes, A.; Fridjonsson, O.H.; Hreggvidson, G.O.; Schoenheit, P.; Kristjansson, J.K.; Holst, O.; Karlsson, E.N.
Two novel cyclodextrin-degrading enzymes isolated from thermophilic bacteria have similar domain structures but differ in oligomeric state and activity profile
J. Biosci. Bioeng.
100
380-390
2005
Anoxybacillus flavithermus (Q5BLZ6), Laceyella sacchari
brenda
Turner, P.; Holst, O.; Karlsson, E.N.
Optimized expression of soluble cyclomaltodextrinase of thermophilic origin in Escherichia coli by using a soluble fusion-tag and by tuning of inducer concentration
Protein Expr. Purif.
39
54-60
2005
Anoxybacillus flavithermus
brenda
Nilsson, C.; Nilsson, F.; Turner, P.; Sixtensson, M.; Nordberg Karlsson, E.; Holst, O.; Cohen, A.; Gorton, L.
Characterisation of two novel cyclodextrinases using on-line microdialysis sampling with high-performance anion exchange chromatography
Anal. Bioanal. Chem.
385
1421-1429
2006
Anoxybacillus flavithermus, Laceyella sacchari
brenda
Ferrer, M.; Beloqui, A.; Golyshina, O.V.; Plou, F.J.; Neef, A.; Chernikova, T.N.; Fernandez-Arrojo, L.; Ghazi, I.; Ballesteros, A.; Elborough, K.; Timmis, K.N.; Golyshin, P.N.
Biochemical and structural features of a novel cyclodextrinase from cow rumen metagenome
Biotechnol. J.
2
207-213
2007
More
brenda
Paul, S.; Singh, C.; Mishra, S.; Chaudhuri, T.K.
The 69 kDa Escherichia coli maltodextrin glucosidase does not get encapsulated underneath GroES and folds through trans mechanism during GroEL/GroES-assisted folding
FASEB J.
21
2874-2885
2007
Escherichia coli
brenda
Paul, S.; Punam, S.; Chaudhuri, T.K.
Chaperone-assisted refolding of Escherichia coli maltodextrin glucosidase
FEBS J.
274
6000-6010
2007
Escherichia coli
brenda
Tang, K.; Utairungsee, T.; Kanokratana, P.; Sriprang, R.; Champreda, V.; Eurwilaichitr, L.; Tanapongpipat, S.
Characterization of a novel cyclomaltodextrinase expressed from environmental DNA isolated from Bor Khleung hot spring in Thailand
FEMS Microbiol. Lett.
260
91-99
2006
unidentified
brenda
Park, K.
Function and tertiary- and quaternary-structure of cyclodextrin-hydrolyzing enzymes (CDase), a group of multisubstrate specific enzymes belonging to the alpha -amylase family
J. Appl. Glycosci.
53
35-44
2006
Bacillus licheniformis, Bacillus sp. I-5, Bacillus thermoalkalophilus, Geobacillus stearothermophilus, Nostoc punctiforme, Pyrococcus furiosus, Thermoplasma volcanium, Thermotoga maritima, Thermus
-
brenda
Labes, A.; Schoenheit, P.
Unusual starch degradation pathway via cyclodextrins in the hyperthermophilic sulfate-reducing archaeon Archaeoglobus fulgidus strain 7324
J. Bacteriol.
189
8901-8913
2007
Archaeoglobus fulgidus, Archaeoglobus fulgidus 7324
brenda
Lunina, N.A.; Agafonova, E.V.; Chekanovskaya, L.A.; Dvortsov, I.A.; Berezina, O.V.; Shedova, E.N.; Kostrov, S.V.; Velikodvorskaya, G.A.
Co-expression of the Thermotoga neapolitana aglB gene with an upstream 3-coding fragment of the malG gene improves enzymatic characteristics of recombinant AglB cyclomaltodextrinase
Protein Expr. Purif.
54
18-23
2007
Thermotoga neapolitana
brenda
Nakagawa, Y.; Saburi, W.; Takada, M.; Hatada, Y.; Horikoshi, K.
Gene cloning and enzymatic characteristics of a novel gamma-cyclodextrin-specific cyclodextrinase from alkalophilic Bacillus clarkii 7364
Biochim. Biophys. Acta
1784
2004-2011
2008
Evansella clarkii (B9A1J7), Evansella clarkii 7364 (B9A1J7)
brenda
Buedenbender, S.; Schulz, G.E.
Structural base for enzymatic cyclodextrin hydrolysis
J. Mol. Biol.
385
606-617
2009
Flavobacterium sp. 92 (Q8KKG0)
brenda
Li, X.; Li, D.; Yin, Y.; Park, K.H.
Characterization of a recombinant amylolytic enzyme of hyperthermophilic archaeon Thermofilum pendens with extremely thermostable maltogenic amylase activity
Appl. Microbiol. Biotechnol.
85
1821-1830
2010
Thermofilum pendens
brenda
Yang, S.J.; Min, B.C.; Kim, Y.W.; Jang, S.M.; Lee, B.H.; Park, K.H.
Changes in the catalytic properties of Pyrococcus furiosus thermostable amylase by mutagenesis of the substrate binding sites
Appl. Environ. Microbiol.
73
5607-5612
2007
Pyrococcus furiosus
brenda
Park, J.T.; Song, H.N.; Jung, T.Y.; Lee, M.H.; Park, S.G.; Woo, E.J.; Park, K.H.
A novel domain arrangement in a monomeric cyclodextrin-hydrolyzing enzyme from the hyperthermophile Pyrococcus furiosus
Biochim. Biophys. Acta
1834
380-386
2013
Pyrococcus furiosus (Q8TZP8)
brenda
Sun, Y.; Lv, X.; Li, Z.; Wang, J.; Jia, B.; Liu, J.
Recombinant cyclodextrinase from Thermococcus kodakarensis KOD1: expression, purification, and enzymatic characterization
Archaea
2015
397924
2015
Thermococcus kodakarensis (Q5JJ59)
brenda
Lee, J.E.; Kim, I.H.; Jung, J.H.; Seo, D.H.; Kang, S.G.; Holden, J.F.; Cha, J.; Park, C.S.
Molecular cloning and enzymatic characterization of cyclomaltodextrinase from hyperthermophilic archaeon Thermococcus sp. CL1
J. Microbiol. Biotechnol.
23
1060-1069
2013
Thermococcus sp. (I3ZTQ5), Thermococcus sp. CL1 (I3ZTQ5)
brenda
Jang, M.; Kang, H.; Jeong, C.; Park, J.; Yi, A.; Kang, J.; Lee, S.; Kim, T.
Enzymatic characterization of Lactococcus lactis subsp. lactis cyclomaltodextrinase expressed in E. coli
Korean J. Microbiol. Biotechnol.
41
391-397
2013
Lactococcus lactis, Lactococcus lactis KCTC 3769
-
brenda
Ali, R.; Shafiq, M.I.
Sequence, structure, and binding analysis of cyclodextrinase (TK1770) from T. kodakarensis (KOD1) using an in silico approach
Archaea
2015
179196
2015
Thermococcus kodakarensis (Q5JJ59), Thermococcus kodakarensis
brenda
Ji, H.; Bai, Y.; Li, X.; Wang, J.; Xu, X.; Jin, Z.
Preparation of malto-oligosaccharides with specific degree of polymerization by a novel cyclodextrinase from Palaeococcus pacificus
Carbohydr. Polym.
210
64-72
2019
Palaeococcus pacificus
brenda
Santos, F.C.D.; Barbosa-Tessmann, I.P.
Recombinant expression, purification, and characterization of a cyclodextrinase from Massilia timonae
Protein Expr. Purif.
154
74-84
2019
Massilia timonae (K9DE84), Massilia timonae, Massilia timonae CCUG 45783 (K9DE84)
brenda
Ji, H.; Bai, Y.; Li, X.; Zheng, D.; Shen, Y.; Jin, Z.
Structural and property characterization of corn starch modified by cyclodextrin glycosyltransferase and specific cyclodextrinase
Carbohydr. Polym.
237
116137
2020
Palaeococcus pacificus
brenda
Aroob, I.; Javed, M.; Ahmad, N.; Aslam, M.; Rashid, N.
Investigating the role of carbohydrate-binding module 34 in cyclomaltodextrinase from Geobacillus thermopakistaniensis structural and functional analyses
3 Biotech
12
25
2022
Geobacillus thermopakistaniensis (A0A7U9P668), Geobacillus thermopakistaniensis MAS1 (A0A7U9P668)
brenda
Park, B.R.; MubarakAli, D.; Kim, J.W.
Identification of a novel cyclomaltodextrinase annotated as a neopullulanase in the genome of Bacillus cereus
Arch. Microbiol.
205
86
2023
Bacillus cereus (WP_000471779.1), Bacillus cereus (Q819G8), Bacillus cereus ATCC 14,579 (WP_000471779.1)
brenda
Aroob, I.; Shaeer, A.; Ahmad, N.; Aslam, M.; Rashid, N.
Ethylenediaminetetraacetic acid enhances structural stability and thermotolerance of recombinant cyclomaltodextrinase from Geobacillus thermopakistaniensis at higher temperatures
Biologia
79
291-298
2024
Geobacillus thermopakistaniensis (A0A7U9P668), Geobacillus thermopakistaniensis MAS1 (A0A7U9P668)
-
brenda
Ji, H.; Wang, Y.; Bai, Y.; Li, X.; Qiu, L.; Jin, Z.
Application of cyclodextrinase in non-complexant production of gamma-cyclodextrin
Biotechnol. Prog.
36
e2930
2020
Palaeococcus pacificus
brenda
Aroob, I.; Ahmad, N.; Aslam, M.; Shaeer, A.; Rashid, N.
A highly active gamma-cyclodextrin preferring cyclomaltodextrinase from Geobacillus thermopakistaniensis
Carbohydr. Res.
481
1-8
2019
Geobacillus thermopakistaniensis (A0A7U9P668), Geobacillus thermopakistaniensis MAS1 (A0A7U9P668)
brenda
Mirzaee, Z.; Jafarian, V.; Shirdel, S.A.; Khalifeh, K.
Structural and functional consequences of replacement of His403 with Arg near the catalytic site of Anoxybacillus flavithermus cyclomaltodextrinase
Enzyme Microb. Technol.
131
109421
2019
Anoxybacillus flavithermus subsp. flavithermus (A0A0Y0H9K3), Anoxybacillus flavithermus subsp. flavithermus ZNU.NGA (A0A0Y0H9K3)
brenda
Abdalla, M.; Jiang, B.; Hassanin, H.A.M.; Zheng, L.; Chen, J.
One-pot production of maltoheptaose (DP7) from starch by sequential addition of cyclodextrin glucotransferase and cyclomaltodextrinase
Enzyme Microb. Technol.
149
109847
2021
Lysinibacillus sphaericus (Q08341), Lysinibacillus sphaericus E-244 (Q08341)
brenda
Zheng, L.; Jiang, B.; Chen, J.; Zhou, L.; Zhang, T.
Strategies for efficient extracellular secretion of recombinant cyclomaltodextrinase by Escherichia coli
Food Biosci.
50
102203
2022
Lysinibacillus sphaericus (Q08341), Lysinibacillus sphaericus E-244 (Q08341)
-
brenda
Wang, L.; Wu, Q.; Zhang, K.; Chen, S.; Yan, Z.; Wu, J.
Cyclodextrinase from Thermococcus sp expressed in Bacillus subtilis and its application in the preparation of maltoheptaose
Microb. Cell Fact.
19
157
2020
Thermococcus sp. B1001 (Q9HHC8)
brenda
Mehrvand, J.; Hayati Roodbari, N.; Hassani, L.; Jafarian, V.; Khalifeh, K.
An evolution-based designing and characterization of mutants of cyclomaltodextrinase molecular modeling and spectroscopic studies
Spectrochim. Acta A. Mol. Biomol. Spectrosc.
230
118055
2020
Anoxybacillus flavithermus (A0A0Y0H9K3)
brenda
Aliakbari, N.; Mirzaee, Z.; Jafarian, V.; Khalifeh, K.; Salehi, M.
Genetic and biochemical characterization of a novel thermostable cyclomaltodextrinase from Anoxybacillus flavithermus
Starch
71
180033
2019
Anoxybacillus flavithermus subsp. flavithermus (A0A0Y0H9K3), Anoxybacillus flavithermus subsp. flavithermus ZNU.NGA (A0A0Y0H9K3)
-
brenda
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