Any feedback?
Information on EC 2.4.1.19 - cyclomaltodextrin glucanotransferase and Organism(s) Niallia circulans and UniProt Accession P43379
for references in articles please use BRENDA:EC2.4.1.19Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.4.1.19 cyclomaltodextrin glucanotransferaseIUBMB Comments
Cyclomaltodextrins (Schardinger dextrins) of various sizes (6,7,8, etc. glucose units) are formed reversibly from starch and similar substrates. Will also disproportionate linear maltodextrins without cyclizing (cf. EC 2.4.1.25, 4-alpha-glucanotransferase).
Specify your search results
Word Map
- 2.4.1.19
- cyclodextrins
- cgtases
- starch
- synthesis
-
transglycosylation
- circulans
-
cyclization
-
glucosylated
- glucoamylase
- paenibacillus
- nutrition
- beta-cyclodextrins
-
alkalophilic
- gamma-cyclodextrins
- beta-cds
- alpha-amylases
- maltooligosaccharides
- stearothermophilus
-
disproportionation
- amylose
- maltodextrins
-
gamma-cds
- industry
-
starch-degrading
- maltohexaose
-
starch-binding
- amylopectin
-
amylolytic
- cyclomaltohexaose
- agriculture
-
alpha-cd
- maltopentaose
- food industry
- pharmacology
- thermoanaerobacter
- maltotetraose
- maltotriose
- beta-amylase
- amyloglucosidase
- pullulanase
- alpha-1,4-glucans
- thermosulfurigenes
- acarbose
-
thermoanaerobacterium
The taxonomic range for the selected organisms is: Niallia circulans
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
cyclodextrin glycosyltransferase, cyclodextrin glucanotransferase, cyclomaltodextrin glucanotransferase, alpha-cgtase, beta-cgtase, toruzyme, cyclodextrin glucosyltransferase, alpha-cyclodextrin glycosyltransferase, cyclodextrin-glycosyltransferase, cyclodextrin glycosyl transferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-1,4-glucan 4-glycosyltransferase, cyclizing
-
-
-
-
alpha-cyclodextrin glucanotransferase
-
-
-
-
alpha-cyclodextrin glycosyltransferase
-
-
-
-
Bacillus macerans amylase
-
-
-
-
beta-cyclodextrin glucanotransferase
-
-
-
-
beta-cyclodextrin glycosyltransferase
BMA
-
-
-
-
CGTase
cyclodextrin glucanotransferase
cyclodextrin glycosyltransferase
cyclomaltodextrin glucotransferase
-
-
-
-
cyclomaltodextrin glycosyltransferase
gamma-cyclodextrin glycosyltransferase
-
-
-
-
konchizaimu
-
-
-
-
neutral-cyclodextrin glycosyltransferase
-
-
-
-
additional information
beta-cyclodextrin glycosyltransferase
-
-
-
-
CGTase
-
-
-
-
cyclodextrin glucanotransferase
-
-
-
-
cyclodextrin glycosyltransferase
-
-
-
-
cyclomaltodextrin glycosyltransferase
-
-
-
-
additional information
-
CGTase is a member of the glycoside hydrolase family 13, also known as the alpha-amylase family
additional information
-
CGTases are members of the largest family of glycoside hydrolases acting on starch and related alpha-glucans, glycoside hydrolase family 13
additional information
the enzyme is a member of the GH13 family, also known as the alpha-amylase family1
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
cyclization
-
-
-
-
hydrolysis
-
-
-
-
transglycosylation
-
-
-
-
hexosyl group transfer
hexosyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
(1->4)-alpha-D-glucan:(1->4)-alpha-D-glucan 4-alpha-D-[(1->4)-alpha-D-glucano]-transferase (cyclizing)
Cyclomaltodextrins (Schardinger dextrins) of various sizes (6,7,8, etc. glucose units) are formed reversibly from starch and similar substrates. Will also disproportionate linear maltodextrins without cyclizing (cf. EC 2.4.1.25, 4-alpha-glucanotransferase).
CAS REGISTRY NUMBER
COMMENTARY
9030-09-5
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
maltodextrin + glycosyl acceptor
beta-cyclodextrin + alpha-cyclodextrin + gamma-cyclodextrin
-
-
-
?
maltodextrin + glycosyl acceptor
beta-cyclodextrin + alpha-cylodextrin + gamma-cyclodextrin
-
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin + alpha-cyclodextrin + gamma-cyclodextrin
-
-
-
?
soluble starch + glycosyl acceptor
beta-cyclodextrin + alpha-cylodextrin + gamma-cyclodextrin
45.2% conversion yield
-
-
?
4,6-benzylidene-alpha-D-4-nitrophenylmaltoheptaose + D-glucose
4,6-benzylidene-maltopentaose + p-nitrophenyl-(alpha-1,4-glucopyranosyl)2-D-glucose
-
blocked p-nitrophenyl-(alpha-1,4-glucopyranosyl)6-D-glucose , weak cleavage
-
-
?
alpha-cyclodextrin + glycosyl acceptor
beta-cyclodextrin + maltooligosaccharide
-
-
-
-
r
amylopectin + glycosyl acceptor
cycloheptaamylose + cyclohexaamylose + exo-branched cyclohexaamylose
beta-cyclodextrin + D-glucose
?
-
E 192, rapid degradation of beta-cyclodextrin by increasing the coupling reaction
-
-
r
beta-cyclodextrin + L-ascorbic acid
2-O-alpha-D-glucopyranosyl-L-ascorbic acid
-
37% conversion rate
-
-
?
beta-cyclodextrin + salicin
?
-
E 192, rapid degradation of beta-cyclodextrin by increasing the coupling reaction
-
-
?
cycloamylose + D-glucose
?
-
E 192, rapid degradation of beta-cyclodextrin by increasing the coupling reaction
-
-
?
cycloamylose + salicin
?
-
E 192, rapid degradation of beta-cyclodextrin by increasing the coupling reaction
-
-
?
maltodextrin + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin + alpha-cyclodextrin
38% conversion
-
-
?
maltopentaose + glycosyl acceptor
beta-cyclodextrin
-
ATCC 21783
-
r
maltotetraose + glycosyl acceptor
beta-cyclodextrin
-
ATCC 21783
-
r
p-nitrophenyl-(alpha-1,4-glucopyranosyl)2-D-glucose + glycosyl acceptor
p-nitrophenyl-D-glucose + p-nitrophenyl-alpha-1,4-glucopyranosyl-D-glucose + ?
-
E 192
main product p-nitrophenyl-glucose when chain length of substrate is 4 glucose or less, p-nitrophenyl-alpha-1,4-glucopyranosyl-D-glucose when substrate chain length is 5 or more glucose residues
?
p-nitrophenyl-(alpha-1,4-glucopyranosyl)3-D-glucose + glycosyl acceptor
p-nitrophenyl alpha-D-glucoside + p-nitrophenyl-alpha-1,4-glucopyranosyl-D-glucose + p-nitrophenyl-(alpha-1,4-glucopyranosyl)2-D-glucose + ?
-
E 192
product proportions 48:31:21
?
p-nitrophenyl-(alpha-1,4-glucopyranosyl)6-D-glucose + glycosyl acceptor
p-nitrophenyl-glucose + p-nitrophenyl-alpha-1,4-glucopyranosyl-D-glucose + p-nitrophenyl-(glucose)3 + p-nitrophenyl-(alpha-1,4-glucopyranosyl)3-D-glucose + p-nitrophenyl-(alpha-1,4-glucopyranosyl)4-D-glucose + ?
-
E 192
product proportions 33:27:16:6:17
?
p-nitrophenyl-(alpha-1,4-glucopyranosyl)7-D-glucose + glycosyl acceptor
p-nitrophenyl-glucose + p-nitrophenyl-alpha-1,4-glucopyranosyl-D-glucose + p-nitrophenyl-(alpha-1,4-glucopyranosyl)2-D-glucose + p-nitrophenyl-(alpha-1,4-glucopyranosyl)3-D-glucose + p-nitrophenyl-(alpha-1,4-glucopyranosyl)4-D-glucose + p-nitrophenyl-(alpha-1,4-glucopyranosyl)5-D-glucose + ?
-
E 192
product proportions 16:51:12:13:4:4
?
p-nitrophenyl-(glucose)5 + glycosyl acceptor
p-nitrophenyl alpha-D-glucoside + p-nitrophenyl 4-O-alpha-D-glucopyranosyl-alpha-D-glucopyranoside + p-nitrophenyl-(alpha-1,4-D-glucopyranosyl)2-D-glucose + p-nitrophenyl-(alpha-1,4-D-glucopyranosyl)3-D-glucose
-
E 192
product proportions 32:50:12 6
?
p-nitrophenyl-(glucose)6 + glycosyl acceptor
p-nitrophenyl alpha-D-glucoside + p-nitrophenyl 4-O-alpha-D-glucopyranosyl-alpha-D-glucopyranoside + p-nitrophenyl-(alpha-1,4-glucopyranosyl)2-D-glucose + p-nitrophenyl-(alpha-1,4-glucopyranosyl)3-D-glucose + ?
-
E 192
product proportions 18:53:21:8
?
soluble potato starch
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
-
-
ratio for alpha- to beta- to gamma-cyclodextrin 1:1.3:0.5
-
?
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
soluble starch + glycosyl acceptor
beta-cyclodextrin + gamma-cyclodextrin
-
-
-
-
r
amylopectin + glycosyl acceptor
cycloheptaamylose + cyclohexaamylose + exo-branched cyclohexaamylose
-
-
-
-
r
amylopectin + glycosyl acceptor
cycloheptaamylose + cyclohexaamylose + exo-branched cyclohexaamylose
-
ATCC 21783
-
-
r
amylopectin + glycosyl acceptor
cycloheptaamylose + cyclohexaamylose + exo-branched cyclohexaamylose
-
C31
-
-
?
beta-cyclodextrin + maltose
alpha-cyclodextrin + maltooligosaccharide
-
-
-
-
r
beta-cyclodextrin + maltose
alpha-cyclodextrin + maltooligosaccharide
-
ATCC 21783
-
-
r
beta-cyclodextrin + maltotriose
alpha-cyclodextrin + maltooligosaccharide
-
-
-
-
r
beta-cyclodextrin + maltotriose
alpha-cyclodextrin + maltooligosaccharide
-
ATCC 21783
-
-
r
maltose + glycosyl acceptor
beta-cyclodextrin
-
E 192, poor substrate
-
r
maltotriose + glycosyl acceptor
beta-cyclodextrin
-
ATCC 21783
-
-
?
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
strain ATCC 21783, pH 4.5-4.7, producing ratio 23.5: 1.0: 1.0, pH 7.0 0.2: 6.0: 1.0, product ratio 2.0:5.0:1.0
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
21783, neutral CGTase, 0.4, 14 and 2.5%
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
-
strain 251, product proportions 9: 82: 9 with addition of tert-butanol, 15: 65: 20 without solvent
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
ATCC 21783
-
-
?
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
-
ATCC 21783
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin
-
-
-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta-cyclodextrin
-
C31
product ratio 1: 10.5
r
soluble starch + glycosyl acceptor
beta-cyclodextrin
-
E 192, waxy maize starch is the best substrate, wheat starch, corn starch, potato starch
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
-
-
r
soluble starch + glycosyl acceptor
cyclodextrins
-
-
beta-cyclodextrin is the main product
-
?
soluble starch + glycosyl acceptor
Schardinger beta-dextrin
-
ATCC 21783
-
-
?
soluble starch + glycosyl acceptor
Schardinger beta-dextrin
-
ATCC 21783
-
-
r
additional information
?
-
-
mannose, ribose, arabinose, mannitol or sorbitol are not acceptors
-
-
?
additional information
?
-
-
ATCC 21783 contains 3 types of enzymes, acid, neutral and alcaline
-
-
?
additional information
?
-
-
no reaction with p-nitrophenyl-glucose and p-nitrophenyl-alpha-1,4-glucopyranosyl-D-glucose, heptakis(2,6-di-O-methyl)-beta cyclodextrin is not transformed
-
-
?
additional information
?
-
beta-cyclodextrin-forming activity from partially hydrolyzed potato starch with an average degree of polymerization of 50. Disproportionation activity is determined using 4-nitrophenyl-beta-D-maltoheptaoside-4-6-O-ethylidene, i.e. pNPG7, as substrate
-
-
?
additional information
?
-
conversion of starch into beta- and gamma-cyclodextrins in a ratio 73:27
-
-
?
additional information
?
-
-
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
-
-
?
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzymes from Bacillus circulans strans produce beta-cyclodextrins, except for strain DF 9R that also produces alpha-cyclodextrins
-
-
?
additional information
?
-
CGTase catalyzes the formation of cyclomaltooligosaccharides, cyclic molecules formed by alpha-(1,4)-linked D-glucopyranosyl units with an apolar central cavity and a hydrophilic outer surface. alpha-, beta-Cyclizing and amylolytic activities withpotato starch as substrate, enzyme structure-function relationship, overview
-
-
?
additional information
?
-
-
formation of alpha-, beta-, and gamma-cyclodextrins from starch and matotriose
-
-
?
additional information
?
-
-
reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview. The enzyme from strain BC251 also shows hydrolytic activity on potato starch. Substrate binding structure of the strain BC251 enzyme, overview
-
-
?
additional information
?
-
-
substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites. Cyclodextrin glucanotransferases cleave the alpha-1,4-glycosidic bonds between the subsites -1 and +1 in alpha-glucans yielding a stable covalent glycosyl-intermediate bound at the donor subsites. The glycosyl-intermediate is then transferred to the 4-hydroxyl of its own non-reducing end forming a new alpha-1,4-glycosidic bond to yield a cyclic product
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
soluble starch + glycosyl acceptor
cyclodextrins
-
-
beta-cyclodextrin is the main product
-
?
additional information
?
-
-
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
-
-
?
additional information
?
-
-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzymes from Bacillus circulans strans produce beta-cyclodextrins, except for strain DF 9R that also produces alpha-cyclodextrins
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Ca2+
-
the enzyme has three Ca2+ binding sites. Ca2+ has a small contribution to the enzyme's thermostability
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ethanol
-
the enzyme keeps very good levels of alpha-cyclodextrin activity using starch or maltodextrin as substrates even at 20% ethanol (around 55-60%). The degradation of the alpha-cyclodextrin is strongly inhibited by ethanol, even at very low concentrations
additional information
-
the enzyme shows substrate and product inhibition
-
acarbose
the acceptor substrate binding site near the active site of the enzyme is involved in inhibition by acarbose, mutants K232E, F283L, and A230V show increased resistance, overview
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Km value is 0.69 mg/ml for wild-type, 0.57 mg/ml for mutant Q179G, 0.54 mg/ml for mutant Q179l, substrate soluble potato starch, pH 6.4, 56°C
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
127.5
soluble potato starch
-
mutant Q179L, pH 6.4, 56°C, calculated as production of beta-cyclodextrin
-
246.2
soluble potato starch
-
wild-type, pH 6.4, 56°C, calculated as production of beta-cyclodextrin
-
247.2
soluble potato starch
-
mutant Q179G, pH 6.4, 56°C, calculated as production of beta-cyclodextrin
-
48
starch
pH 6.0, 60°C, beta-cyclization activity, mutant A230V/H140Q
329
starch
pH 6.0, 60°C, beta-cyclization activity, wild-type enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
strain C31, 6.623.4 units, 1 unit is the amount of enzyme which causes 10% reduction in the intensity of the blue colour of the starch-iodine complex
additional information
-
strain DF9, R-variation, 353 units, 1 unit is the amount which produces a difference of absorbance of 1.0 per minute
additional information
-
strain DF9, S-variation, 388 units, 1 unit is the amount which produces a difference of absorbance of 1.0 per minute
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 4.7
4.6
-
ATCC 21783 contains 3 isozymes, neutral, alkalic and acidic, possessing markedly different pH optima, 4.6, 7.0 and 9.5
5.5
5.5 - 5.8
8 - 9
9.5
-
ATCC 21783 contains 3 isozymes, neutral, alkalic and acidic, possessing markedly different pH optima, 4.6, 7.0 and 9.5
5.5
-
enzyme immobilized on glyoxyl-agarose and free enzyme present similar pH/activities profiles, with two peaks at pH values of 5.5 and 7 and a minimum at pH 6.0-6.5 in both amylolytic and CGTase activities
7
-
ATCC 21783 contains 3 isozymes, neutral, alkalic and acidic, possessing markedly different pH optima, 4.6, 7.0 and 9.5
7
-
ATCC 21783, purified enzyme, crude enzyme has 3 pH optima, 4.5-5.0, 7.0 and 8.0-9.0
7
-
enzyme immobilized on glyoxyl-agarose and free enzyme present similar pH/activities profiles, with two peaks at pH values of 5.5 and 7 and a minimum at pH 6.0-6.5 in both amylolytic and CGTase activities
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 9
-
enzyme immobilized on glyoxyl-agarose and free enzyme present similar pH/activities profiles, with two peaks at pH values of 5.5 and 7 and a minimum at pH 6.0-6.5 in both amylolytic and CGTase activities. Activities decrease after these two maximum values. The glyoxyl CGTase retains 30% of amylase activity at pH 4 and 50% at pH 9. The soluble enzyme retains 10% and 30%, respectively. In synthetic activities differences are not significant
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
50
55
60
65
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 70
45 - 70
-
45°C: soluble enzyme shows about 50% of maximal activity, enzyme immobilized on glyoxyl-agarose shows about 60% of maximal activity, 70°C: soluble enzyme shows about 60% of maximal activity, enzyme immobilized on gyoxyl-agarose shows about 75% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
conditions used to produce cyclodextrins with cyclodextrin glycosyltransferase from Bacillus circulans DF 9R are optimized using experimental designs. The optimum conditions for cyclodextrin production are: 5% (w/v) cassava starch, 15 U of enzyme per gram of substrate, reaction temperature of 56°C and pH 6.4. After 4 h, the proportion of starch converted to cyclodextrin reaches 66% (w/w) and the weight ratio of alpha-cyclodextrin:beta-cyclodextrin:gamma-cyclodextrin is 1.00:0.70:0.16
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80000
85000 - 88000
88000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
additional information
-
CGTases are five domain proteins with the active site located at the bottom of a (beta/alpha)8-barrel in the A domain. Substrates bind across the enzyme surface in a long groove formed by the domains A and B that can accommodate at least 7 glucose residues at the donor subsites and 3 at the acceptor subsites
additional information
enzyme peptide mapping and sequencing, overview. Enzyme structure-function relationship, involving protein ethoxyformylation, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D577A
the mutation increases the beta-cyclization activity of the enzyme (23% higher catalytic efficiency compared to the wild type)
D577G
the mutation increases the beta-cyclization activity of the enzyme (43.9% higher catalytic efficiency compared to the wild type)
D577I
the mutation decreases the beta-cyclization activity of the enzyme (14.5% lower catalytic efficiency compared to the wild type)
D577L
the mutation decreases the beta-cyclization activity of the enzyme (8.8% lower catalytic efficiency compared to the wild type)
D577R
the mutant exhibits beta-cyclization activity that is greater than that of the wild type by 3.3%
D577V
the mutation decreases the beta-cyclization activity of the enzyme (18.8% lower catalytic efficiency compared to the wild type)
Y89D
the mutant exhibits total and beta-cyclization activities that are greater than that of the wild type by 14.3% and 17.6%, respectively
Y89D/D577R
the mutant exhibits total and beta-cyclization activities that are greater than that of the wild type by 14% and 35.1%, respectively
Y89G
the mutant exhibits total and beta-cyclization activities that are greater than that of the wild type by 10.6% and 14.6%, respectively
Y89G/D577R
the mutant exhibits total and beta-cyclization activities that are greater than that of the wild type by 25% and 29.3%, respectively
Y89N
the mutant exhibits total and beta-cyclization activities that are greater than that of the wild type by 8.9% and 13%, respectively
Y89N/D577R
the mutant exhibits total and beta-cyclization activities that are greater than that of the wild type by 19.4% and 25.2%, respectively
A230V
the mutation confers increased resistance to inhibition by acarbose, the mutant shows highly increased IC50 compared to the wild-type enzyme
A315D
-
the mutation significantly changes the contribution of Ca2+ to the enzyme's thermostability
D577A
-
the mutation increases the beta-cyclization activity of the enzyme with 23% higher catalytic efficiency compared to the wild type. The mutation also increases the affinity for maltodextrin
D577E
-
the mutant displays an 11.2% increase in the beta-cyclization activity compared to the wild type enzyme
D577G
-
the mutation increases the beta-cyclization activity of the enzyme with 43.9% higher catalytic efficiency compared to the wild type. The mutation also increases the affinity for maltodextrin
D577H
-
the mutant displays a slight decrease in the beta-cyclization activity compared to the wild type enzyme
D577K
D577R
-
the mutant displays a 30.7% increase in the beta-cyclization activity compared to the wild type enzyme
F283L
the mutation confers increased resistance to inhibition by acarbose, the mutant shows highly increased IC50 compared to the wild-type enzyme
H140Q
the mutation confers increased resistance to inhibition by acarbose, the mutant shows highly increased IC50 compared to the wild-type enzyme
K192R
-
increase in half-life at 60°C from 9.7 min for the wild-type enzyme to 11.6 min for the mutant enzyme
K232E
the mutation confers increased resistance to inhibition by acarbose, the mutant shows highly increased IC50 compared to the wild-type enzyme
L600E
the mutant shows wild type cyclization activities. The mutation decreases the product inhibition exhibited by beta-cyclodextrin as compared to the wild type enzyme
L600I
the mutant shows decreased cyclization activities compared to the wild type enzyme. The mutation decreases the product inhibition exhibited by beta-cyclodextrin as compared to the wild type enzyme
L600R
the mutant shows increased cyclization activities compared to the wild type enzyme. The mutation decreases the product inhibition exhibited by beta-cyclodextrin as compared to the wild type enzyme
L600Y
the mutant shows wild type cyclization activities. The mutation decreases the product inhibition exhibited by beta-cyclodextrin as compared to the wild type enzyme
N188D
-
increase in half-life at 60°C from 9.7 min for the wild-type enzyme to 35 min for the mutant enzyme
N188D/K192R
-
increase in half-life at 60°C from 9.7 min for the wild-type enzyme to 56 min for the mutant enzyme
Q179G
-
mutation to residue G which is conserved in all the corresponding enzymes except in that from Bacillus circulans Df 9R. Activity and kinetic parameters remain unchanged
Q179L
-
mutation results in a different ratio of cyclodextrin products with a ratio for alpha- to beta- to gamma-cyclodextrin 1:1.7:0.7, a lower catalytic efficiency, and a decreased ability to convert starch into cyclodextrins
T185S
-
increase in half-life at 60°C from 9.7 min for the wild-type enzyme to 14.8 min for the mutant enzyme
T186Y
-
decrease in half-life at 60°C from 9.7 min for the wild-type enzyme to 8 min for the mutant enzyme
additional information
D577K
-
the mutant displays a 1.5% increase in the beta-cyclization activity compared to the wild type enzyme
D577K
-
the mutation significantly changes the contribution of Ca2+ to the enzyme's thermostability
additional information
construction of chimeric cyclodextrin glucanotransferases from Bacillus circulans A11 and Paenibacillus macerans IAM1243 and analysis of their product specificity
additional information
error-prone PCR mutagenesis for searching the sequence space of CGTase for acarbose-insensitive variants, overview
additional information
-
position 179 is involved in enzyme product specificity and must be occupied by Gly or by amino acid residues able to interact with the substrate through hydrogen bonds in a way that the cyclization process occurs efficiently
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 9
6 - 10
6 - 8
6 - 9
6 - 9.5
7 - 8
-
strain E 192, maximum stability, only 14% decrease in activity at pH 7.0
488842
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
if submitted to strong stirring, promoting the apparition of gas bubbles and shear forces, the enzyme becomes inactivated at 25°C. This inactivation does not occur if the enzyme is immobilized on any porous support
40 - 60
-
strain E 192, heat labile, rapid inactivation at temperatures above 45, remaining activity is 75% after 20 min at 40°C, 10% at 50°C and only 5% after 1 min at 60°C, protected by substrate and Ca2+ enzyme is stable for at least 24 h at pH 6.0, very stable at pH 7.0, 48 h without any loss of activity
50
55
-
half-life of soluble enzyme at pH 7 is 1.5 h. The immobilization of the enzyme on CNBr-agarose does not promote an increment in the stability of the enzyme at 55°C, although it prevents the effect of the stirred system
58 - 60
60
65
60
-
half-life: 9.7 min for wild-type enzyme, 8 min for mutant enzyme T186Y, 35 min for mutant enzyme N188D, 11.6 min for mutant enzyme K192E and 56 min for mutant enzyme N188D/K192R
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
thermostability at 60°C and pH 7 reveals that the enzyme adsorbed on ionic supports is slightly less stable than the CNBr-agarose immobilized enzyme. The enzyme immobilized on Eupergit presents a very similar stability to this preparation while the glyoxyl-agarose is much more stable than any other preparation (by around a 15-fold factor) the glyoxyl-agarose immobilized enzyme is much more stable than any other preparation in presence of ethanol
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 13.7fold from strain ATCC 21783 by ultrafiltration and consecutive starch adsorption
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of wild-type and mutant enzymes in Bacillus subtilis strain DB104A
phylogenetic analysis, expression of the enzyme from strain BC8 in Escherichia coli strain JM103, and of the enzyme from strain BC251 in Bacillus subtilis strain DB104A
-
the cyclodextrin glucanotransferase gene is cloned into plasmid pYD1, which allows regulated expression, secretion, and detection. The expression of CGTase with a-agglutinin at the N-terminal end on the extracellular surface of Saccharomyces cerevisiae is confirmed by immunofluorescence microscopy. This surface-anchored CGTase gives the yeast the ability to directly utilize starch as a sole carbon source and the ability to produce the anticipated products, cyclodextrins, as well as glucose and maltose. The resulting glucose and maltose, which are efficient acceptors in the CGTase coupling reaction, could be consumed by yeast fermentation and thus facilitated cyclodextrin production. On the other hand, ethanol produced by the yeast may form a complex with cyclodextrin and shift the equilibrium in favor of cyclodextrin production. The yeast with immobilized CGTase produces 24.07 mg/ml cyclodextrins when it is incubated in yeast medium supplemented with 4% starch
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
industry
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
nutrition
synthesis
nutrition
-
used for producing linear oligosaccharides, serving as sweeteners
synthesis
-
ATCC 21783, enzyme is becoming commercially important since cyclodextrins have found various practical applications
synthesis
-
industrial strain E 192, industrial production of cyclodextrins
synthesis
-
constructing proteins having new properties of industrial importance
synthesis
-
production of alpha-cyclodextrin. Cyclodextrins serve as molecular hosts, are used in the food industry for capturing and retaining flavors and are also used in the formulation of pharmaceuticals.
synthesis
-
synthesis of cyclodextrins with multiple applications in the food, pharmaceutical, cosmetic, agricultural and chemical industries. Conditions used to produce cyclodextrins with cyclodextrin glycosyltransferase from Bacillus circulans DF 9R are optimized using experimental designs
synthesis
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
synthesis
the enzyme is of interest for industrial cyclodextrin production
synthesis
CGTases is used to catalyze cyclomaltooligosaccharides/cyclodextrins production in important industrial processes
synthesis
-
cyclodextrin glucanotransferases are industrially important enzymes that produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch, overview. Use of complexing agents during cyclodextrin synthesis and the variation in solubility of the different cyclodextrins to allow selective precipitation. Usage of the enzyme as immobilized biocatalyst
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nakamura, N.; Horikoshi, K.
Purification and properties of neutral-cyclodextrin glycosyl-transferase of an alkalophilic Bacillus sp.
Agric. Biol. Chem.
40
1785-1791
1976
Geobacillus stearothermophilus, Niallia circulans, Priestia megaterium, Paenibacillus macerans, Bacillus sp. (in: Bacteria)
-
Kato, T.; Horikoshi, K.
Immobilzed cyclomaltodextrin glucanotransferase of an alkalophilic Bacillus sp. No. 38-2
Biotechnol. Bioeng.
26
595-598
1984
Geobacillus stearothermophilus, Niallia circulans, Priestia megaterium, Paenibacillus macerans, Bacillus sp. (in: Bacteria), Klebsiella pneumoniae
Maekelae, M.; Mattsson, P.; Schinina, M.E.; Korpela, T.
Purification and properties of cyclomaltodextrin glucanotransferase from an alkalophilic Bacillus
Biotechnol. Appl. Biochem.
10
414-427
1988
Niallia circulans, Paenibacillus macerans, Bacillus sp. (in: Bacteria), Klebsiella pneumoniae, Bacillus sp. (in: Bacteria) 1011, Paenibacillus macerans IAM1243
-
Pongsawasdi, P.; Yagisawa, M.
Purification and properties of cyclomaltodextrin glucanotransferase from Bacillus circulans
Agric. Biol. Chem.
52
1099-1103
1988
Niallia circulans, Priestia megaterium, Paenibacillus macerans, Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) Ha3-3-2 / ATCC 39612, Niallia circulans C31
-
Fujita, Y.; Tsubouchi, H.; Inagi, Y.; Tomita, K.; Ozaki, A.; Nakanishi, K.
Purification and properties of cyclodextrin glycosyltransferase from Bacillus sp. AL-6
J. Ferment. Bioeng.
70
150-154
1990
Niallia circulans, Priestia megaterium, Bacillus subtilis, Paenibacillus macerans, Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) AL-6, Bacillus subtilis 313
-
Akimaru, K.; Yagi, T.; Yamamoto, S.
Purification and properties of Bacillus coagulans cyclomaltodextrin glucanotransferase
J. Ferment. Bioeng.
71
322-328
1991
Geobacillus stearothermophilus, Niallia circulans, Weizmannia coagulans, Priestia megaterium, Bacillus subtilis, Paenibacillus macerans, Bacillus ohbensis, Bacillus sp. (in: Bacteria), Klebsiella oxytoca, Klebsiella pneumoniae, Geobacillus stearothermophilus TC-60, Bacillus subtilis 313
-
Bovetto, L.J.; Backer, D.P.; Villette, J.R.; Sicard, P.J.; Bouquelet, S.J.L.
Cyclomaltodextrin glucanotransferase from Bacillus circulans E 192. I. Purification and characterization of the enzyme
Biotechnol. Appl. Biochem.
15
48-58
1992
Geobacillus stearothermophilus, Alkalihalobacillus alcalophilus, Niallia circulans, Priestia megaterium, Paenibacillus macerans, Bacillus ohbensis, Klebsiella pneumoniae, Micrococcus sp., Niallia circulans E 192, Niallia circulans 8
Bovetto, L.J.; Villette, J.R.; Fontaine, I.F.; Sicard, P.J.; Bouquelet, S.J.L.
Cyclomaltodextrin glucanotransferase from Bacillus circulans E 192. II. Action Patterns
Biotechnol. Appl. Biochem.
15
59-68
1992
Niallia circulans, Klebsiella pneumoniae, Niallia circulans E 192, Niallia circulans 8
-
Fujiwara, S.; Kakihara, H.; Sakaguchi, K.; Imanaka, T.
Analysis of mutations in cyclodextrin glucanotransferase from Bacillus stearothermophilus which affect cyclization characteristics and thermostability
J. Bacteriol.
174
7478-7481
1992
Geobacillus stearothermophilus, Niallia circulans, Paenibacillus macerans, Klebsiella oxytoca, Geobacillus stearothermophilus NO2, Geobacillus stearothermophilus TC-91, Niallia circulans 8
Fujiwara, S.; Kakihara, H.; Woo, K.B.; Lejeune, A.; Kanemoto, M.; Sakaguchi, K.; Imanaka, T.
Cyclization characteristics of cyclodextrin glucanotransferase are conferred by the NH2-terminal region of the enzyme
Appl. Environ. Microbiol.
58
4016-4025
1992
Bacillus licheniformis, Bacillus sp. (in: Bacteria), Bacillus subtilis, Bacillus subtilis NA-1, Geobacillus stearothermophilus, Geobacillus stearothermophilus (P31797), Geobacillus stearothermophilus NO2, Klebsiella oxytoca, Klebsiella pneumoniae, Niallia circulans, Niallia circulans 8, Paenibacillus macerans, Paenibacillus macerans (P04830), Paenibacillus macerans IAM1243, Priestia megaterium
Shibuya, T.; Miwa, Y.; Nakano, M.; Yamauchi, T.; Chaen, H.; Sakai, S.; Kurimoto, M.
Enzymatic synthesis of a novel trisaccharide, glucosyl lactoside
Biosci. Biotechnol. Biochem.
57
56-60
1993
Geobacillus stearothermophilus, Niallia circulans, Paenibacillus macerans, Geobacillus stearothermophilus TC-91
Tomita, K.; Kaneda, M.; Kawamura, K.; Nakanishi, K.
Purification and properties of a cyclodextrin glucanotransferase from Bacillus autolyticus 11149 and selective formation of beta-cyclodextrin
J. Ferment. Bioeng.
75
89-92
1993
Geobacillus stearothermophilus, Bacillus autolyticus, Niallia circulans, Paenibacillus macerans, Bacillus sp. (in: Bacteria), Klebsiella oxytoca, Bacillus sp. (in: Bacteria) AL-6, Bacillus autolyticus 11149
-
Villette, J.R.; Helbecque, N.; Albani, J.R.; Sicard, P.J.; Bouquelet, J.L.
Cyclomaltodextrin glucanotransferase from Bacillus circulans E 192: nitration with tetranitromethane
Biotechnol. Appl. Biochem.
17
205-216
1993
Niallia circulans, Niallia circulans E 192
-
Nakamura, A.; Haga, K.; Yamane, K.
Four aromatic residues in the active center of cyclodextrin glucanotransferase from alkalophilic Bacillus sp. 1011: effects of replacements on substrate binding and cyclization characteristics
Biochemistry
33
9929-9936
1994
Geobacillus stearothermophilus, Niallia circulans, Bacillus licheniformis, Paenibacillus macerans, Bacillus ohbensis, Bacillus sp. (in: Bacteria), Klebsiella pneumoniae, Bacillus sp. (in: Bacteria) 1011, Bacillus sp. (in: Bacteria) 17-1, Bacillus sp. (in: Bacteria) B1018
Ferrarotti, S.A.; Rosso, A.M.; Marechal, M.A.; Krymkiewicz, N.; Marechal, L.R.
Isolation of two strains (S-R type) of Bacillus circulans and purification of a cyclomaltodextrin-glucanotransferase
Cell. Mol. Biol.
42
653-657
1996
Geobacillus stearothermophilus, Alkalihalobacillus alcalophilus, Niallia circulans, Weizmannia coagulans, Priestia megaterium, Bacillus subtilis, Lederbergia lentus, Paenibacillus macerans, Bacillus sp. (in: Bacteria), Klebsiella oxytoca, Niallia circulans DF9
Tonkova, A.
Bacterial cyclodextrin glucanotransferase
Enzyme Microb. Technol.
22
678-686
1998
Bacillus cereus, Bacillus cereus NCIMB 13123, Bacillus licheniformis, Bacillus ohbensis, Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) 1011, Bacillus sp. (in: Bacteria) AL-6, Bacillus sp. (in: Bacteria) INMIA 1919, Bacillus sp. (in: Bacteria) INMIA A7/1, Bacillus sp. (in: Bacteria) INMIA T4, Bacillus sp. (in: Bacteria) INMIA t6, Geobacillus stearothermophilus, Geobacillus stearothermophilus N2, Klebsiella oxytoca, Klebsiella pneumoniae, Lederbergia lentus, Lysinibacillus sphaericus, Lysinibacillus sphaericus ATCC 7055, Micrococcus luteus, Niallia circulans, Niallia circulans 8, Paenibacillus macerans, Paenibacillus macerans IAM1243, Priestia megaterium, Priestia megaterium No5, Salimicrobium halophilum, Salimicrobium halophilum INMIA-3849, Thermoanaerobacterium thermosulfurigenes, Thermoanaerobacterium thermosulfurigenes EM1, Weizmannia coagulans
-
Yamamoto, T.; Shiraki, K.; Fujiwara, S.; Takagi, M.; Fukui, K.; Imanaka, T.
In vitro heat effect on functional and conformational changes of cyclodextrin glucanotransferase from hyperthermophilic archaea
Biochem. Biophys. Res. Commun.
265
57-61
1999
Geobacillus stearothermophilus, Niallia circulans, Niallia circulans 251, Niallia circulans 8, Thermoanaerobacterium thermosulfurigenes, Thermoanaerobacterium thermosulfurigenes EM1, Thermococcus sp., Thermococcus sp. (Q9UWN2), Thermococcus sp. B1001
Abelyan, V.A.; Balayan, A.M.; Manukyan, L.S.; Afyan, K.B.; Meliksetyan, V.S.; Andreasyan, N.A.; Markosyan, A.A.
Characteristics of cyclodextrin production using cyclodextrin glucanotransferases from various groups of microorganisms
Appl. Biochem. Microbiol.
38
616-624
2002
Geobacillus stearothermophilus, Alkalihalobacillus alcalophilus, Niallia circulans, Weizmannia coagulans, Salimicrobium halophilum, Bacillus licheniformis, Paenibacillus macerans, Thermoactinomyces vulgaris, Bacillus licheniformis B-4025, Paenibacillus macerans BIO-2m, Thermoactinomyces vulgaris Tac-3554, Geobacillus stearothermophilus B-4006, Salimicrobium halophilum BIO-12H BIO-13H, Niallia circulans BIO-3m, Bacillus licheniformis BIO-9m, Alkalihalobacillus alcalophilus BA-4229, Weizmannia coagulans BIO-13m, Alkalihalobacillus alcalophilus B-3103
Lee, S.H.; Kim, Y.W.; Lee, S.; Auh, J.H.; Yoo, S.S.; Kim, T.J.; Kim, J.W.; Kim, S.T.; Rho, H.J.; Choi, J.H.; Kim, Y.B.; Park, K.H.
Modulation of cyclizing activity and thermostability of cyclodextrin glucanotransferase and its application as an antistaling enzyme
J. Agric. Food Chem.
50
1411-1415
2002
Geobacillus stearothermophilus, Bacillus licheniformis, Paenibacillus macerans, Klebsiella pneumoniae, Niallia circulans (P43379), Geobacillus stearothermophilus NO2, Niallia circulans 251 (P43379), Geobacillus stearothermophilus ET1
Rashid, N.; Cornista, J.; Ezaki, S.; Fukui, T.; Atomi, H.; Imanaka, T.
Characterization of an archaeal cyclodextrin glucanotransferase with a novel C-terminal domain
J. Bacteriol.
184
777-784
2002
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) 1011, Geobacillus stearothermophilus, Geobacillus stearothermophilus (P31797), Klebsiella oxytoca (P08704), Niallia circulans, Niallia circulans (P43379), Niallia circulans 251, Niallia circulans 251 (P43379), Paenibacillus macerans (P31835), Thermoanaerobacterium thermosulfurigenes, Thermoanaerobacterium thermosulfurigenes EM1, Thermococcus kodakarensis (Q8X268), Thermococcus sp., Thermococcus sp. (Q9UWN2), Thermococcus sp. B1001, Thermococcus sp. B1001 (Q9UWN2)
Doukyu, N.; Kuwahara, H.; Aono, R.
Isolation of Paenibacillus illinoisensis that produces cyclodextrin glucanotransferase resistant to organic solvents
Biosci. Biotechnol. Biochem.
67
334-340
2003
Niallia circulans, Priestia megaterium, Salimicrobium halophilum, Paenibacillus macerans, Bacillus ohbensis, Bacillus sp. (in: Bacteria), Brevibacterium sp., Thermoanaerobacterium thermosulfurigenes, Paenibacillus illinoisensis, Paenibacillus illinoisensis ST-12K, Brevibacterium sp. 9605, Bacillus sp. (in: Bacteria) BE101, Niallia circulans 251
Rosso, A.; Ferrarotti, S.; Miranda, M.V.; Krymkiewicz, N.; Nudel, B.C.; Cascone, O.
Rapid affinity purification processes for cyclodextrin glycosyltransferase from Bacillus circulans
Biotechnol. Lett.
27
1171-1175
2005
Niallia circulans
Rimphanitchayakit, V.; Tonozuka, T.; Sakano, Y.
Construction of chimeric cyclodextrin glucanotransferases from Bacillus circulans A11 and Paenibacillus macerans IAM1243 and analysis of their product specificity
Carbohydr. Res.
340
2279-2289
2005
Paenibacillus macerans (O52766), Niallia circulans (Q9F5W3), Paenibacillus macerans IAM1243 (O52766), Paenibacillus macerans IAM1243, Niallia circulans A11 (Q9F5W3)
Tsuchiyama, Y.; Yamamoto, K.; Asou, T.; Okabe, M.; Yagi, Y.; Okamoto, R.
A novel process of cyclodextrin production by use of specific adsorbents. Part I. Screening of specific adsorbents
J. Ferment. Bioeng.
71
407-412
1991
Niallia circulans
-
Leemhuis, H.; Rozeboom, H.J.; Dijkstra, B.W.; Dijkhuizen, L.
Improved thermostability of Bacillus circulans cyclodextrin glycosyltransferase by the introduction of a salt bridge
Proteins
54
128-134
2004
Niallia circulans
Wang, Z.; Qi, Q.; Wang, P.G.
Engineering of cyclodextrin glucanotransferase on the cell surface of Saccharomyces cerevisiae for improved cyclodextrin production
Appl. Environ. Microbiol.
72
1873-1877
2006
Niallia circulans, Niallia circulans 251
Qi, Q.; Zimmermann, W.
Cyclodextrin glucanotransferase: from gene to applications
Appl. Microbiol. Biotechnol.
66
475-485
2005
Bacillus licheniformis (P14014), Bacillus ohbensis (P27036), Bacillus sp. (in: Bacteria) (O82984), Bacillus sp. (in: Bacteria) (P05618), Bacillus sp. (in: Bacteria) (P17692), Bacillus sp. (in: Bacteria) (P30921), Bacillus sp. (in: Bacteria) (P31747), Bacillus sp. (in: Bacteria) (Q59239), Bacillus sp. (in: Bacteria) 1011 (P05618), Bacillus sp. (in: Bacteria) 1018 (P17692), Bacillus sp. (in: Bacteria) 17.1 (P30921), Bacillus sp. (in: Bacteria) 38-2 (P30921), Bacillus sp. (in: Bacteria) 6.6.3 (P31747), Bacillus sp. (in: Bacteria) A2-5a (O82984), Bacillus sp. (in: Bacteria) KC201 (Q59239), Brevibacillus brevis (O30565), Brevibacillus brevis CD162 (O30565), Cytobacillus firmus, Cytobacillus firmus 290-3, Evansella clarkii (Q8L3E0), Evansella clarkii 7384 (Q8L3E0), Geobacillus stearothermophilus (P31797), Klebsiella oxytoca (P08704), Klebsiella oxytoca M5a1 (P08704), Niallia circulans (P30920), Niallia circulans (P43379), Niallia circulans (Q9F5W3), Niallia circulans 251 (P43379), Niallia circulans 8 (P30920), Niallia circulans A11 (Q9F5W3), Nostoc sp. (Q8RMG0), Nostoc sp. 9229 (Q8RMG0), Paenibacillus macerans (P31835), Salipaludibacillus agaradhaerens, Salipaludibacillus agaradhaerens (Q7X3T0), Salipaludibacillus agaradhaerens DSM 8721 (Q7X3T0), Salipaludibacillus agaradhaerens DSM 9948, Salipaludibacillus agaradhaerens LS-3C, Streptococcus pyogenes, Thermoanaerobacter sp., Thermoanaerobacterium thermosulfurigenes (P26827), Thermococcus kodakarensis (Q8X268), Thermococcus sp. (Q9UWN2), Thermococcus sp. B1001 (Q9UWN2), Xanthomonas axonopodis, Xanthomonas campestris
Szerman, N.; Schroh, I.; Rossi, A.L.; Rosso, A.M.; Krymkiewicz, N.; Ferrarotti, S.A.
Cyclodextrin production by cyclodextrin glycosyltransferase from Bacillus circulans DF 9R
Biores. Technol.
98
2886-2891
2007
Niallia circulans, Niallia circulans DF 9R
Ferrarotti, S.A.; Bolivar, J.M.; Mateo, C.; Wilson, L.; Guisan, J.M.; Fernandez-Lafuente, R.
Immobilization and stabilization of a cyclodextrin glycosyltransferase by covalent attachment on highly activated glyoxyl-agarose supports
Biotechnol. Prog.
22
1140-1145
2006
Niallia circulans, Niallia circulans DF 9R
Vassileva, A.; Atanasova, N.; Ivanova, V.; Dhulster, P.; Tonkova, A.
Characterisation of cyclodextrin glucanotransferase from Bacillus circulans ATCC 21783 in terms of cyclodextrin production
Ann. Microbiol.
57
609-615
2007
Niallia circulans (P30920)
-
Kelly, R.M.; Leemhuis, H.; Gaetjen, L.; Dijkhuizen, L.
Evolution toward small molecule inhibitor resistance affects native enzyme function and stability, generating acarbose-insensitive cyclodextrin glucanotransferase variants
J. Biol. Chem.
283
10727-10734
2008
Niallia circulans (P30920), Niallia circulans 251 (P30920)
Kelly, R.M.; Dijkhuizen, L.; Leemhuis, H.
The evolution of cyclodextrin glucanotransferase product specificity
Appl. Microbiol. Biotechnol.
84
119-133
2009
Anaerobranca gottschalkii, Bacillus sp. (in: Bacteria) (P05618), Geobacillus stearothermophilus (P31797), Geobacillus stearothermophilus NO2 (P31797), Klebsiella pneumoniae, Klebsiella pneumoniae M5a1, Niallia circulans, Thermoanaerobacter sp., Thermoanaerobacterium thermosulfurigenes, Thermoanaerobacterium thermosulfurigenes EM1, Thermococcus sp., Thermococcus sp. B1001
Leemhuis, H.; Kelly, R.M.; Dijkhuizen, L.
Engineering of cyclodextrin glucanotransferases and the impact for biotechnological applications
Appl. Microbiol. Biotechnol.
85
823-835
2010
Alkalihalobacillus clausii, Alkalihalobacillus clausii E16, Anaerobranca gottschalkii, Bacillus licheniformis, Bacillus ohbensis, Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) B1018, Bacillus sp. (in: Bacteria) BL-31, Bacillus sp. (in: Bacteria) G1, Bacillus sp. (in: Bacteria) KC201, Bacillus sp. (in: Bacteria) TS1-1, Brevibacillus brevis, Brevibacillus brevis CD162, Cytobacillus firmus, Evansella clarkii, Evansella clarkii 7384, Geobacillus stearothermophilus, Geobacillus stearothermophilus ET1, Klebsiella pneumoniae, Klebsiella pneumoniae M5a1, Niallia circulans, Paenibacillus campinasensis, Paenibacillus campinasensis H69-3, Paenibacillus graminis, Paenibacillus graminis NC22.13, Paenibacillus illinoisensis, Paenibacillus illinoisensis ST-12 K, Paenibacillus macerans, Paenibacillus pabuli, Paenibacillus pabuli US132, Paenibacillus sp., Priestia megaterium, Salipaludibacillus agaradhaerens, Salipaludibacillus agaradhaerens LS-3C, Thermoanaerobacter sp., Thermoanaerobacterium thermosulfurigenes, Thermoanaerobacterium thermosulfurigenes EM1
Costa, H.; del Canto, S.; Ferrarotti, S.; de Jimenez Bonino, M.B.
Structure-function relationship in cyclodextrin glycosyltransferase from Bacillus circulans DF 9R
Carbohydr. Res.
344
74-79
2009
Niallia circulans (C4MH58), Niallia circulans DF 9R (C4MH58)
Gaston, J.; Szerman, N.; Costa, H.; Krymkiewicz, N.; Ferrarotti, S.
Cyclodextrin glycosyltransferase from Bacillus circulans DF 9R: activity and kinetic studies
Enzyme Microb. Technol.
45
36-41
2009
Niallia circulans, Niallia circulans DF 9R
-
Costa, H.; Distefano, A.J.; Marino-Buslje, C.; Hidalgo, A.; Berenguer, J.; Biscoglio de Jimenez Bonino, M.; Ferrarotti, S.A.
The residue 179 is involved in product specificity of the Bacillus circulans DF 9R cyclodextrin glycosyltransferase
Appl. Microbiol. Biotechnol.
94
123-130
2012
Niallia circulans, Niallia circulans DF 9R
Li, Z.; Huang, M.; Gu, Z.; Holler, T.P.; Cheng, L.; Hong, Y.; Li, C.
Asp577 mutations enhance the catalytic efficiency of cyclodextrin glycosyltransferase from Bacillus circulans
Int. J. Biol. Macromol.
83
111-116
2016
Niallia circulans, Niallia circulans STB01
Li, C.; Ban, X.; Gu, Z.; Li, Z.
Calcium ion contribution to thermostability of cyclodextrin glycosyltransferase is closely related to calcium-binding site CaIII
J. Agric. Food Chem.
61
8836-8841
2013
Niallia circulans, Paenibacillus macerans
Huang, M.; Li, C.; Gu, Z.; Cheng, L.; Hong, Y.; Li, Z.
Mutations in cyclodextrin glycosyltransferase from Bacillus circulans enhance beta-cyclization activity and beta-cyclodextrin production
J. Agric. Food Chem.
62
11209-11214
2014
Niallia circulans, Niallia circulans STB01
Tao, X.; Su, L.; Wu, J.
Current studies on the enzymatic preparation 2-O-alpha-D-glucopyranosyl-L-ascorbic acid with cyclodextrin glycosyltransferase
Crit. Rev. Biotechnol.
39
249-257
2019
Geobacillus stearothermophilus, Alkalihalobacillus alcalophilus, Niallia circulans, Paenibacillus macerans, Thermoanaerobacter sp., Paenibacillus sp., Anaerobranca gottschalkii, Paenibacillus sp. JK-12, Paenibacillus sp. JB-13, Bacillus sp. SK 13.002, Alkalihalobacillus alcalophilus 7-12, Niallia circulans 251
Chen, S.; Li, Z.; Gu, Z.; Hong, Y.; Cheng, L.; Holler, T.P.; Li, C.
Leu600 mutations decrease product inhibition of the beta-cyclodextrin glycosyltransferase from Bacillus circulans STB01
Int. J. Biol. Macromol.
115
1194-1201
2018
Niallia circulans (A0A097CPM3), Niallia circulans STB01 (A0A097CPM3)
Li, Z.; Huang, M.; Gu, Z.; Holler, T.; Cheng, L.; Hong, Y.; Li, C.
Asp577 mutations enhance the catalytic efficiency of cyclodextrin glycosyltransferase from Bacillus circulans
Int. J. Biol. Macromol.
83
111-116
2016
Niallia circulans (P43379), Niallia circulans, Niallia circulans STB01 (P43379)
Li, C.; Xu, Q.; Gu, Z.; Chen, S.; Wu, J.; Hong, Y.; Cheng, L.; Li, Z.
Cyclodextrin glycosyltransferase variants experience different modes of product inhibition
J. Mol. Catal. B
133
203-210
2016
Niallia circulans, Paenibacillus macerans, Paenibacillus macerans JFB05-01, Niallia circulans STB01
-
Huang, M.; Ren, J.; Li, C.; Gu, Z.; Hong, Y.; Cheng, L.; Li, Z.
Double mutations enhance beta-cyclization activity of cyclodextrin glycosyltransferase from Bacillus circulans
J. Mol. Catal. B
133
S100-S105
2016
Niallia circulans (P43379), Niallia circulans STB01 (P43379)
-
EXTERNAL LINKS (specific for EC-Number 2.4.1.19)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
