3.2.1.54: cyclomaltodextrinase
This is an abbreviated version!
For detailed information about cyclomaltodextrinase, go to the full flat file.
Word Map on EC 3.2.1.54
-
3.2.1.54
-
starch
-
cyclodextrins
-
maltose
-
maltodextrins
-
ceramidase
-
neopullulanase
-
transglycosylation
-
thermoactinomyces
-
alpha-amylases
-
maltogenic
-
maltotriose
-
glucanotransferase
-
amylolytic
-
acarbose
-
amylases
-
maltoheptaose
-
malto-oligosaccharides
-
cgtases
-
cyclomaltodextrins
-
maltotetraose
-
panose
-
beta-cd
-
alkalophilic
-
amylomaltase
-
alpha-cd
-
anoxybacillus
-
biotechnology
-
synthesis
-
food industry
-
analysis
- 3.2.1.54
- starch
- cyclodextrins
- maltose
- maltodextrins
- ceramidase
- neopullulanase
-
transglycosylation
-
thermoactinomyces
- alpha-amylases
-
maltogenic
- maltotriose
-
glucanotransferase
-
amylolytic
- acarbose
- amylases
- maltoheptaose
- malto-oligosaccharides
- cgtases
- cyclomaltodextrins
- maltotetraose
- panose
- beta-cd
-
alkalophilic
- amylomaltase
-
alpha-cd
- anoxybacillus
- biotechnology
- synthesis
- food industry
- analysis
Reaction
Synonyms
AfCda13, AglB, alpha-amylase, alpha-amylase II, CD-/pullulan-hydrolyzing enzyme, CD-ase, CD-degrading enzyme, CD-hydrolyzing amylase, CDA, CDase, CDase I-5, CMD, cyclodextrinase, cycloheptaglucanase, cyclohexaglucanase, cyclomaltodextrin dextrin-hydrolase, Cyclomaltodextrin hydrolase, decycling, cyclomaltodextrinase, CymH, cytoplasmic decycling maltodextrinase, EC 3.2.1.12, Env cda13A, FspCMD, H-17 CDase, H-17 thermostable CDase, LLCD, LsCda13, Lsp26X-Mdase, maltodextrin glucosidase, More, neopullulanase, PFTA, RA.04, thermophilic CDase, TK1770, TVA II
ECTree
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Substrates Products
Substrates Products on EC 3.2.1.54 - cyclomaltodextrinase
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REACTION DIAGRAM
4-nitrophenyl-alpha-D-maltopentaoside + H2O
4-nitrophenol + alpha-D-maltopentaoside
-
-
-
-
?
6-O-alpha-D-glucosyl-alpha-cyclodextrin + H2O
isomaltooligosaccharides
branched cyclodextrin
-
-
?
6-O-alpha-D-glucosyl-beta-cyclodextrin + H2O
isomaltooligosaccharides
branched cyclodextrin
-
-
?
6-O-alpha-D-maltosyl-beta-cyclodextrin + H2O
isomaltooligosaccharides
branched cyclodextrin
-
-
?
alpha-cyclodextrin + H2O
maltohexaose
-
highest activity. The enzyme shows strongest preference towards alpha-and beta-cyclodextrin
-
-
?
amylose + H2O
maltose + glucose
-
CDase I-5 shows high preference towards amylose
major hydrolysis products
-
?
beta-cyclodextrin + H2O
D-glucose + ?
beta-cyclodextrin is the most active substrate
-
-
?
beta-cyclodextrin + H2O
maltoheptaose
-
strongest preference towards alpha-and beta-cyclodextrin
-
-
?
beta-cyclodextrin + H2O
maltose + maltotriose + maltotetraose + maltopentaose + maltoheptaose + glucose
beta-cyclodextrin + H2O
panose + maltoheptaose
-
cyclomaltodextrinase activity
-
-
?
cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
G1-alpha-cyclodextrin + H2O
D-glucose + maltose
-
24% of the activity with beta-cyclodextrin
main products
-
?
G1-beta-cyclodextrin + H2O
D-glucose + maltose
-
32% of the activity with beta-cyclodextrin
main products
-
?
G2-alpha-cyclodextrin + H2O
D-glucose + maltose
-
19% of the activity with beta-cyclodextrin
main products
-
?
G2-beta-cyclodextrin + H2O
D-glucose + maltose
-
30% of the activity with beta-cyclodextrin
main products
-
?
gamma-cyclodextrin + H2O
D-glucose + ?
hydrolyzing activity is about 20% compared to the activity with beta-cyclodextrin
-
-
?
gamma-cyclodextrin + H2O
glucose + maltose + maltotriose + maltotetraose + maltopentaose + maltohexaose + maltoheptaose + maltooctaose
glycogen + H2O
?
-
relative rate of hydrolysis 0,1%
-
-
?
maltohexaose + H2O
maltose + D-glucose + ?
-
14% of the activity with gamma-cyclodextrin
-
-
?
maltooligosaccharides + H2O
maltotriose + maltotetraose
-
alpha-amylase activity
main products
-
?
maltopentaose + H2O
maltose + D-glucose + ?
-
11% of the activity with gamma-cyclodextrin
-
-
?
p-nitrophenyl-D-maltopentaoside + H2O
p-nitrophenol + maltopentaose
-
-
-
-
?
pullulan + H2O
branched pullulan tetrasaccharide
-
substrate is a linear polysaccharide composed of maltotriose units linked by alpha-1,6-bonds, low activity
main products
-
?
pullulan + H2O
D-glucose + ?
hydrolyzing activity is about 20% compared to the activity with beta-cyclodextrin
-
-
?
pullulan + H2O
glucose + panose + isopanose + large saccharides containing alpha 1,6-glucosidic bonds
pullulan + H2O
panose + maltoheptaose
-
cyclomaltodextrinase activity
-
-
?
starch + H2O
maltotriose + maltotetraose
-
alpha-amylase activity, preferred substrate
main products
-
?
4-nitrophenol + maltohexaose
-
-
-
?
4-nitrophenyl-alpha-D-maltohexaoside + H2O
4-nitrophenol + maltohexaose
-
-
-
?
?
-
pseudotetrasaccharide inhibitor of glucosidases and alpha-amylases, binding the active sites of the enzyme
-
-
?
acarbose + H2O
?
-
substrate is a pseudotetrasaccharide and potent inhibitor of glucosidases
-
-
?
acarbose + H2O
?
-
pseudotetrasaccharide inhibitor of glucosidases and alpha-amylases, binding the active sites of the enzyme
-
-
?
acarbose + H2O
?
-
the substrate is a potent inhibitor of alpha-amylases, cyclomaltodextrinase activity
-
-
?
acarbose + H2O
?
-
substrate is a pseudotetrasaccharide and potent inhibitor of glucosidases
-
-
?
acarbose + H2O
?
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
substrate is a pseudotetrasaccharide and potent inhibitor of glucosidases
-
-
?
maltotriose + maltose + glucose
-
-
-
?
alpha-cyclodextrin
maltotriose + maltose + glucose
-
-
-
?
D-glucose + maltose
preferred substrate. As compared with the dimer protein, the monomeric enzyme retains only 23% of the specific activity
+ maltotriose + maltotetraose + maltoheptaose at lower amounts
-
?
alpha-cyclodextrin + H2O
D-glucose + maltose
-
53% of the activity with beta-cyclodextrin
main products
-
?
alpha-cyclodextrin + H2O
D-glucose + maltose
-
57% of the activity with beta-cyclodextrin
+ less amounts of maltotriose and maltotetraose
-
?
alpha-cyclodextrin + H2O
glucose + maltose + maltotriose
-
-
-
?
alpha-cyclodextrin + H2O
glucose + maltose + maltotriose
-
-
-
?
isomaltooligosaccharides
-
mainly D-glucose and maltose
-
?
alpha-cyclodextrin + H2O
isomaltooligosaccharides
-
mainly D-glucose and maltose
-
?
alpha-cyclodextrin + H2O
linear maltodextrins
-
-
-
?
maltooligosaccharides
-
-
maltohexaose, maltoheptaose, maltooctaose
-
?
alpha-cyclodextrin + H2O
maltooligosaccharides
-
-
maltohexaose, maltoheptaose, maltooctaose
-
?
alpha-cyclodextrin + H2O
maltooligosaccharides
-
-
maltohexaose, maltoheptaose, maltooctaose
-
?
alpha-cyclodextrin + H2O
maltose + D-glucose
-
-
-
-
?
alpha-cyclodextrin + H2O
maltose + D-glucose
-
65% of the activity with gamma-cyclodextrin
-
-
?
alpha-cyclodextrin + H2O
maltose + D-glucose
-
65% of the activity with gamma-cyclodextrin
-
-
?
maltose + glucose
-
-
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
-
-
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-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
-
-
-
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
-
-
-
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
-
-
-
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
-
-
-
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
55% of the activity with beta-cyclomaltodextrin
-
-
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
55% of the activity with beta-cyclomaltodextrin
-
-
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
alpha-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
maltose + ?
-
-
degraded slowly by cleavage of maltose units from the nonreducing ends
?
amylopectin + H2O
maltose + ?
-
rate of hydrolysis less than 5% of the rate of alpha-cyclodextrin hydrolysis
-
-
?
amylose + H2O
?
-
less than 5% of the rate of alpha-cyclodextrin hydrolysis
-
-
?
beta-cyclodextrin + H2O
?
-
wild-type enzyme and mutant enzymes G415E, H414N/G415E and H414N hydrolyze beta-cyclodextrin intp maltoheptaose as the major product plus several small maltooligosaccharides
-
-
?
D-glucose + maltose
-
+ maltotriose + maltotetraose + maltoheptaose at lower amounts
-
?
beta-cyclodextrin + H2O
D-glucose + maltose
-
-
+ less amounts of maltotriose and maltotetraose
-
?
glucose + maltose + long chain linear oligomers
-
-
-
?
beta-cyclodextrin + H2O
glucose + maltose + long chain linear oligomers
-
-
-
-
?
beta-cyclodextrin + H2O
glucose + maltose + long chain linear oligomers
-
-
-
?
beta-cyclodextrin + H2O
glucose + maltose + long chain linear oligomers
-
-
-
-
?
glucose + maltose + maltotriose + maltotetraose
-
-
-
?
beta-cyclodextrin + H2O
glucose + maltose + maltotriose + maltotetraose
-
-
-
?
beta-cyclodextrin + H2O
glucose + maltose + maltotriose + maltotetraose
-
-
-
?
maltooligosaccharides
-
-
maltohexaose, maltoheptaose, maltooctaose
-
?
beta-cyclodextrin + H2O
maltooligosaccharides
-
-
maltohexaose, maltoheptaose, maltooctaose
-
?
beta-cyclodextrin + H2O
maltooligosaccharides
-
-
G1 to G7, maltoheptaose as major product
-
?
beta-cyclodextrin + H2O
maltooligosaccharides
-
-
maltohexaose, maltoheptaose, maltooctaose
-
?
maltose + D-glucose
-
-
in an approximate molar ratio of 2 to 1
-
?
beta-cyclodextrin + H2O
maltose + D-glucose
-
-
in an approximate molar ratio of 2 to 1
-
?
beta-cyclodextrin + H2O
maltose + D-glucose
-
-
in an approximate molar ratio of 2 to 1
-
?
beta-cyclodextrin + H2O
maltose + D-glucose
-
-
in an approximate molar ratio of 2 to 1
-
?
beta-cyclodextrin + H2O
maltose + D-glucose
-
-
in an approximate molar ratio of 2 to 1
-
?
beta-cyclodextrin + H2O
maltose + D-glucose
-
-
in an approximate molar ratio of 2 to 1
-
?
beta-cyclodextrin + H2O
maltose + D-glucose
-
78% of the activity with gamma-cyclodextrin
-
-
?
beta-cyclodextrin + H2O
maltose + D-glucose
-
78% of the activity with gamma-cyclodextrin
-
-
?
beta-cyclodextrin + H2O
maltose + D-glucose
-
-
in an approximate molar ratio of 2 to 1
-
?
beta-cyclodextrin + H2O
maltose + D-glucose
-
-
in an approximate molar ratio of 2 to 1
-
?
beta-cyclodextrin + H2O
maltose + D-glucose
-
-
in an approximate molar ratio of 2 to 1
-
?
beta-cyclodextrin + H2O
maltose + D-glucose
-
-
in an approximate molar ratio of 2 to 1
-
?
maltose + glucose
-
-
in an approximate molar ratio of 2 to 1
-
?
beta-cyclodextrin + H2O
maltose + glucose
-
-
in an approximate molar ratio of 2 to 1
-
?
maltose + maltotriose + maltotetraose + maltopentaose + maltoheptaose + glucose
-
-
-
-
?
beta-cyclodextrin + H2O
maltose + maltotriose + maltotetraose + maltopentaose + maltoheptaose + glucose
-
-
-
?
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
beta-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
beta-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
beta-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
beta-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
beta-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
beta-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
beta-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
beta-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
beta-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
best substrate
-
-
?
beta-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
best substrate
-
-
?
beta-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
beta-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
beta-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
beta-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
beta-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
panose + maltoheptaose
-
cyclomaltodextrinase activity, hydrolysis of alpha-1,4-glucosidic linkages
-
-
?
cyclodextrin + H2O
panose + maltoheptaose
-
cyclomaltodextrinase activity, hydrolysis of alpha-1,4-glucosidic linkages
-
-
?
cyclomaltodextrin + H2O
linear maltodextrin
-
no avtivity with activity with starch, pullulan, amylose, amylopectin, or oligosaccharides as substrates
-
-
?
cyclomaltodextrin + H2O
linear maltodextrin
-
no avtivity with activity with starch, pullulan, amylose, amylopectin, or oligosaccharides as substrates
-
-
?
cyclomaltodextrin + H2O
maltodextrin
-
-
linear, glucose only
?
cyclomaltodextrin + H2O
maltodextrin
-
opening the ring of the cyclic dextrins forming a linear molecule with corresponding number of glucose units
-
-
ir
cyclomaltodextrin + H2O
maltodextrin
-
opening the ring of the cyclic dextrins forming a linear molecule with corresponding number of glucose units
-
-
ir
cyclomaltodextrin + H2O
maltodextrin
-
-
series of maltooligomers
?
cyclomaltodextrin + H2O
maltodextrin
-
-
series of maltooligomers
?
cyclomaltodextrin + H2O
maltodextrin
-
alpha-cyclodextrin 100% hydrolysis, beta-cyclodextrin 67% hydrolysis, gamma-cyclodextrin 8%
-
-
?
cyclomaltodextrin + H2O
maltodextrin
-
alpha-cyclodextrin 100% hydrolysis, beta-cyclodextrin 67% hydrolysis, gamma-cyclodextrin 8%
-
-
?
maltooligosaccharide
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
cyclomaltodextrin + H2O
maltooligosaccharide
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
cyclomaltodextrins + H2O
linear maltodextrins
-
-
-
?
D-glucose + maltose
-
59% of the activity with beta-cyclodextrin
main products
-
?
gamma-cyclodextrin + H2O
D-glucose + maltose
-
72% of the activity with beta-cyclodextrin
+ less amounts of maltotriose and maltotetraose
-
?
glucose + maltose + maltotriose + maltotetraose + maltopentaose + maltohexaose + maltoheptaose + maltooctaose
-
-
-
?
gamma-cyclodextrin + H2O
glucose + maltose + maltotriose + maltotetraose + maltopentaose + maltohexaose + maltoheptaose + maltooctaose
-
-
-
-
?
maltooctaose + ?
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
-
-
?
gamma-cyclodextrin + H2O
maltooctaose + ?
Evansella clarkii 7364
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
-
-
?
maltooligosaccharides
-
preferred substrate
maltohexaose, maltoheptaose, maltooctaose
-
?
gamma-cyclodextrin + H2O
maltooligosaccharides
-
preferred substrate
maltohexaose, maltoheptaose, maltooctaose
-
?
gamma-cyclodextrin + H2O
maltooligosaccharides
-
preferred substrate
maltohexaose, maltoheptaose, maltooctaose
-
?
maltose + D-glucose
-
-
in an approximate molar ratio of 2 to 1
-
?
gamma-cyclodextrin + H2O
maltose + D-glucose
-
-
in an approximate molar ratio of 2 to 1
-
?
gamma-cyclodextrin + H2O
maltose + D-glucose
-
-
in an approximate molar ratio of 2 to 1
-
?
gamma-cyclodextrin + H2O
maltose + D-glucose
-
-
in an approximate molar ratio of 2 to 1
-
?
gamma-cyclodextrin + H2O
maltose + D-glucose
-
-
in an approximate molar ratio of 2 to 1
-
?
gamma-cyclodextrin + H2O
maltose + D-glucose
-
-
in an approximate molar ratio of 2 to 1
-
?
gamma-cyclodextrin + H2O
maltose + D-glucose
-
-
-
-
?
gamma-cyclodextrin + H2O
maltose + D-glucose
-
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
-
-
?
gamma-cyclodextrin + H2O
maltose + D-glucose
-
-
in an approximate molar ratio of 2 to 1
-
?
gamma-cyclodextrin + H2O
maltose + D-glucose
-
-
in an approximate molar ratio of 2 to 1
-
?
gamma-cyclodextrin + H2O
maltose + D-glucose
-
-
in an approximate molar ratio of 2 to 1
-
?
gamma-cyclodextrin + H2O
maltose + D-glucose
-
-
in an approximate molar ratio of 2 to 1
-
?
maltose + glucose
-
-
in an approximate molar ratio of 2 to 1
-
?
gamma-cyclodextrin + H2O
maltose + glucose
-
-
in an approximate molar ratio of 2 to 1
-
?
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
gamma-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
-
-
-
?
gamma-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
gamma-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
gamma-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
gamma-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
gamma-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
gamma-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
gamma-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
gamma-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
gamma-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
33% of the activity with beta-cyclomaltodextrin
-
-
?
gamma-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
33% of the activity with beta-cyclomaltodextrin
-
-
?
gamma-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
gamma-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
gamma-cyclomaltodextrin + H2O
alpha-D-glucose + maltose
-
composed of 6 to 8 D-glucopyranosyl residues
-
-
?
6,3-O-alpha-D-glucosylmaltohexaose
-
branched alpha-cyclodextrin, synonym 6-O-alpha-D-glucosylmaltohexaose
-
?
glucosyl-alpha-cyclodextrin + H2O
6,3-O-alpha-D-glucosylmaltohexaose
-
branched alpha-cyclodextrin, synonym 6-O-alpha-D-glucosylmaltohexaose
-
?
6,4-O-alpha-D-glucosylmaltoheptaose
-
-
-
-
?
glucosyl-beta-cyclodextrin + H2O
6,4-O-alpha-D-glucosylmaltoheptaose
-
branched beta-cyclodextrin, synonym 6-O-alpha D-glucosylmaltoheptaose
-
?
glucosyl-beta-cyclodextrin + H2O
6,4-O-alpha-D-glucosylmaltoheptaose
-
branched beta-cyclodextrin, synonym 6-O-alpha D-glucosylmaltoheptaose
-
?
?
-
cyclomaltodextrinase activity, hydrolysis of alpha-1,6-glucosidic linkages
-
-
?
isopanose + H2O
?
-
cyclomaltodextrinase activity, hydrolysis of alpha-1,6-glucosidic linkages
-
-
?
linear maltodextrins + H2O
alpha-D-glucose + maltose
-
-
-
-
?
linear maltodextrins + H2O
alpha-D-glucose + maltose
-
-
-
-
?
linear maltodextrins + H2O
alpha-D-glucose + maltose
-
with a small glucose unit, low activity
-
-
?
linear maltodextrins + H2O
alpha-D-glucose + maltose
-
with a small glucose unit, low activity
-
-
?
?
62% activity compared to beta-cyclodextrin
-
-
?
maltodextrin + H2O
?
62% activity compared to beta-cyclodextrin
-
-
?
maltose + glucose
-
linear, enzyme degrades the linear molecules by splitting off maltose units from the nonreducing end of the chain
-
?
maltodextrins + H2O
maltose + glucose
-
6 to 8 membered maltooligosaccharides
-
-
?
maltodextrins + H2O
maltose + glucose
-
linear, enzyme degrades the linear molecules by splitting off maltose units from the nonreducing end of the chain
-
-
?
maltodextrins + H2O
maltose + glucose
-
linear, enzyme degrades the linear molecules by splitting off maltose units from the nonreducing end of the chain
-
-
?
maltodextrins + H2O
maltose + glucose
-
linear, enzyme degrades the linear molecules by splitting off maltose units from the nonreducing end of the chain
-
-
?
maltodextrins + H2O
maltose + glucose
-
linear, enzyme degrades the linear molecules by splitting off maltose units from the nonreducing end of the chain
-
-
?
maltodextrins + H2O
maltose + glucose
-
linear, enzyme degrades the linear molecules by splitting off maltose units from the nonreducing end of the chain
-
-
?
maltodextrins + H2O
maltose + glucose
-
linear, enzyme degrades the linear molecules by splitting off maltose units from the nonreducing end of the chain
-
-
?
maltoheptaose + H2O
D-glucose + maltose + ?
-
43% of the activity with beta-cyclodextrin
-
-
?
maltoheptaose + H2O
D-glucose + maltose + ?
-
43% of the activity with beta-cyclodextrin
-
-
?
maltoheptaose + H2O
D-glucose + maltose + ?
-
-
-
-
?
maltose + D-glucose + ?
-
24% of the activity with gamma-cyclodextrin
-
-
?
maltoheptaose + H2O
maltose + D-glucose + ?
-
24% of the activity with gamma-cyclodextrin
-
-
?
maltohexaose + H2O
?
-
33% of the activity with beta-cyclodextrin
-
-
?
D-glucose + maltose + ?
-
35% of the activity with beta-cyclodextrin
-
-
?
maltohexaose + H2O
D-glucose + maltose + ?
-
35% of the activity with beta-cyclodextrin
-
-
?
maltohexaose + H2O
maltotetraose + maltose
-
-
-
?
maltohexaose + maltose
-
small amounts of maltotriose, maltotetraose and maltopentaose are also observed
-
?
maltooctaose + H2O
maltohexaose + maltose
Evansella clarkii 7364
-
small amounts of maltotriose, maltotetraose and maltopentaose are also observed
-
?
maltopentaose + H2O
?
-
18% of the activity with beta-cyclodextrin
-
-
?
D-glucose + maltose + ?
-
22% of the activity with beta-cyclodextrin
-
-
?
maltopentaose + H2O
D-glucose + maltose + ?
-
22% of the activity with beta-cyclodextrin
-
-
?
6,3-O-alpha-D-maltosylmaltohexaose
-
-
-
-
?
maltosyl-alpha-cyclodextrin + H2O
6,3-O-alpha-D-maltosylmaltohexaose
-
branched alpha-cyclodextrin, synonym 6-O-alpha-D-maltosylcyclomaltohexaose
-
?
maltosyl-alpha-cyclodextrin + H2O
6,3-O-alpha-D-maltosylmaltohexaose
-
branched alpha-cyclodextrin, synonym 6-O-alpha-D-maltosylcyclomaltohexaose
-
?
6,4-O-alpha-D-maltosylmaltoheptaose
-
-
-
-
?
maltosyl-beta-cyclodextrin
6,4-O-alpha-D-maltosylmaltoheptaose
-
branched beta-cyclodextrin, synonym 6-O-alpha-D-maltosylcyclomaltoheptaose
-
?
maltosyl-beta-cyclodextrin
6,4-O-alpha-D-maltosylmaltoheptaose
-
branched beta-cyclodextrin, synonym 6-O-alpha-D-maltosylcyclomaltoheptaose
-
?
maltotetraose + H2O
2 D-glucose + maltose
-
14% of the activity with beta-cyclodextrin
-
-
?
maltotetraose + H2O
2 D-glucose + maltose
-
14% of the activity with beta-cyclodextrin
-
-
?
maltotetraose + H2O
?
-
12% of the activity with beta-cyclodextrin
-
-
?
maltose + 2 D-glucose
-
6% of the activity with gamma-cyclodextrin
-
-
?
maltotetraose + H2O
maltose + 2 D-glucose
-
6% of the activity with gamma-cyclodextrin
-
-
?
maltose + D-glucose
-
11% of the activity with beta-cyclodextrin
-
-
?
maltotriose + H2O
maltose + D-glucose
-
11% of the activity with beta-cyclodextrin
-
-
?
maltotriose + H2O
maltose + D-glucose
-
5.3% of the activity with gamma-cyclodextrin
-
-
?
maltotriose + H2O
maltose + D-glucose
-
5.3% of the activity with gamma-cyclodextrin
-
-
?
glucose + panose + isopanose + large saccharides containing alpha 1,6-glucosidic bonds
-
-
-
-
?
pullulan + H2O
glucose + panose + isopanose + large saccharides containing alpha 1,6-glucosidic bonds
-
-
-
-
?
pullulan + H2O
glucose + panose + isopanose + large saccharides containing alpha 1,6-glucosidic bonds
-
-
-
-
?
pullulan + H2O
glucose + panose + isopanose + large saccharides containing alpha 1,6-glucosidic bonds
-
-
-
?
pullulan + H2O
glucose + panose + isopanose + large saccharides containing alpha 1,6-glucosidic bonds
-
-
-
-
?
pullulan + H2O
glucose + panose + isopanose + large saccharides containing alpha 1,6-glucosidic bonds
-
-
-
-
?
pullulan + H2O
glucose + panose + isopanose + large saccharides containing alpha 1,6-glucosidic bonds
-
rate of hydrolysis less than 5% of the rate of alpha-cyclodextrin hydrolysis
-
-
?
panose + ?
-
cyclomaltodextrinase activity, hydrolysis of alpha-1,4-glucosidic linkages
-
-
?
pullulan + H2O
panose + ?
-
cyclomaltodextrinase activity, hydrolysis of alpha-1,4-glucosidic linkages
-
-
?
panose + maltose
-
substrate is a linear polysaccharide composed of maltotriose units linked by alpha-1,6-bonds, low activity
main products
-
?
pullulan + H2O
panose + maltose
-
substrate is a linear polysaccharide composed of maltotriose units linked by alpha-1,6-bonds, low activity
main products
-
?
pullulan + H2O
panose + maltose
-
substrate is a linear polysaccharide composed of maltotriose units linked by alpha-1,6-bonds, low activity
main products
-
?
pullulan + H2O
panose + maltose
-
substrate is a linear polysaccharide composed of maltotriose units linked by alpha-1,6-bonds, low activity
main products
-
?
pullulan + H2O
panose + maltose
-
substrate is a linear polysaccharide composed of maltotriose units linked by alpha-1,6-bonds, low activity
main products
-
?
pullulan + H2O
panose + maltose
-
substrate is a linear polysaccharide composed of maltotriose units linked by alpha-1,6-bonds, low activity
main products
-
?
pullulan + H2O
panose + maltose
-
substrate is a linear polysaccharide composed of maltotriose units linked by alpha-1,6-bonds, low activity
main products
-
?
pullulan + H2O
panose + maltose + glucose
-
-
-
?
starch + H2O
?
8% activity compared to beta-cyclodextrin
-
-
?
alpha-D-glucose + maltose
-
no formation of cyclodextrins as products
-
-
?
starch + H2O
alpha-D-glucose + maltose
-
soluble starch, no formation of cyclodextrins as products
-
-
?
starch + H2O
alpha-D-glucose + maltose
-
soluble starch, no formation of cyclodextrins as products
-
-
?
starch + H2O
alpha-D-glucose + maltose
-
soluble starch, no formation of cyclodextrins as products
-
-
?
starch + H2O
alpha-D-glucose + maltose
-
no formation of cyclodextrins as products
-
-
?
starch + H2O
alpha-D-glucose + maltose
-
no formation of cyclodextrins as products
-
-
?
starch + H2O
alpha-D-glucose + maltose
-
no formation of cyclodextrins as products
-
-
?
starch + H2O
alpha-D-glucose + maltose
-
soluble starch, no formation of cyclodextrins as products
-
-
?
starch + H2O
alpha-D-glucose + maltose
-
no formation of cyclodextrins as products
-
-
?
starch + H2O
alpha-D-glucose + maltose
-
soluble starch, no formation of cyclodextrins as products
-
-
?
starch + H2O
glucose + maltose
-
10%
degraded slowly by cleavage of maltose units from the nonreducing ends
?
starch + H2O
glucose + maltose
-
-
glucose minor early product, + maltotriose + maltotetraose
?
starch + H2O
glucose + maltose
-
50% hydrolysis
-
-
?
starch + H2O
glucose + maltose
-
50% hydrolysis
-
-
?
maltooligosaccharides
-
alpha-amylase activity, preferred substrate, hydrolysis of alpha-1,4-glucosidic linkages
-
-
?
starch + H2O
maltooligosaccharides
-
alpha-amylase activity, preferred substrate, hydrolysis of alpha-1,4-glucosidic linkages
-
-
?
additional information
?
-
-
physiological role of the enzyme
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
physiological role of the enzyme
-
-
?
additional information
?
-
-
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
-
-
?
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
?
-
-
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
-
-
?
additional information
?
-
-
physiological role of the enzyme
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
physiological role of the enzyme
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
physiological role of the enzyme, starch utilization pathway
-
-
?
additional information
?
-
-
part of the cyclomaltodextrin binding site is located between the third and fourth conserved regions
-
-
?
additional information
?
-
-
physiological role of the enzyme, starch utilization pathway
-
-
?
additional information
?
-
-
part of the cyclomaltodextrin binding site is located between the third and fourth conserved regions
-
-
?
additional information
?
-
-
poor activity with starch, acarbose, and pullulan, about 80fold lower compared to beta-cyclodextrin
-
-
?
additional information
?
-
-
poor activity with starch, acarbose, and pullulan, about 80fold lower compared to beta-cyclodextrin
-
-
?
additional information
?
-
-
physiological role of the enzyme
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme hardly reacts with potato soluble starch, pullulan, amylose, amylopectin
-
-
?
additional information
?
-
-
substrate specificity, hydrolytic pattern, PFTA is a bifunctional enzyme showing alpha-amylase as well as cyclodextrin-hydrolyzing activity, but no transglycosylation activity, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
physiological role of the enzyme
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
physiological role of the enzyme
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
no activity with pullulan and maltose, soluble starch is a poor substrate
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
no activity with pullulan and maltose, soluble starch is a poor substrate
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
broad specificity, cleavage of alpha-1,4-glycosidic bonds, the linear maltodextrins are the preferred substrates, substrate ring size effects the activity
-
-
?
additional information
?
-
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
physiological role of the enzyme
-
-
?
additional information
?
-
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
broad specificity, cleavage of alpha-1,4-glycosidic bonds, the linear maltodextrins are the preferred substrates, substrate ring size effects the activity
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
broad specificity, cleavage of alpha-1,4-glycosidic bonds, the cyclomaltodextrins are the preferred substrates, substrate ring size effects the activity
-
-
?
additional information
?
-
-
physiological role of the enzyme
-
-
?
additional information
?
-
-
broad specificity, cleavage of alpha-1,4-glycosidic bonds, the cyclomaltodextrins are the preferred substrates, substrate ring size effects the activity
-
-
?