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Information on EC 2.4.1.19 - cyclomaltodextrin glucanotransferase and Organism(s) Paenibacillus macerans and UniProt Accession P04830

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.19 cyclomaltodextrin glucanotransferase
IUBMB 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).
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This record set is specific for:
Paenibacillus macerans
UNIPROT: P04830
Word Map
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The taxonomic range for the selected organisms is: Paenibacillus macerans
Synonyms
1,4-alpha-D-glucopyranosyl transferase, Akrilex C cyclodextrin glycosyltransferase, alpha-1,4-glucan 4-glycosyltransferase, cyclizing, alpha-CGTase, alpha-cyclodextrin glucanotransferase, alpha-cyclodextrin glycosyltransferase, Bacillus macerans amylase, beta-CGTase, beta-cyclodextrin glucanotransferase, beta-cyclodextrin glycosyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Akrilex C cyclodextrin glycosyltransferase
1209
immobilized enzyme
alpha-1,4-glucan 4-glycosyltransferase, cyclizing
-
-
-
-
alpha-cyclodextrin glucanotransferase
alpha-cyclodextrin glycosyltransferase
Bacillus macerans amylase
-
-
-
-
beta-CGTase
277472
-
beta-cyclodextrin glucanotransferase
-
-
-
-
beta-cyclodextrin glycosyltransferase
-
-
-
-
BMA
-
-
-
-
CGT
277472
gene name
CGTase
cyclodextrin glucanotransferase
cyclodextrin glycosyltransferase
cyclomaltodextrin glucanyltransferase
1209
-
cyclomaltodextrin glucotransferase
-
-
-
-
cyclomaltodextrin glycosyltransferase
-
-
-
-
gamma-cyclodextrin glycosyltransferase
-
-
-
-
konchizaimu
-
-
-
-
M-CGTase
1209
-
neutral-cyclodextrin glycosyltransferase
-
-
-
-
additional information
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cyclization
-
-
-
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hexosyl group transfer
-
-
-
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hydrolysis
-
-
-
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transglycosylation
-
-
-
-
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 hide
9030-09-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-1,4-glucan + glycosyl acceptor
cyclodextrins
show the reaction diagram
-
-
-
-
r
alpha-cyclodextrin + D-glucose
beta-cyclodextrin + maltooligosaccharide
show the reaction diagram
-
immobilized enzyme
-
r
alpha-cyclodextrin + glycosyl acceptor
beta-cyclodextrin + maltooligosaccharide
show the reaction diagram
alpha-cyclodextrin + maltohexaose
beta-cyclodextrin + maltooligosaccharide
show the reaction diagram
-
immobilized enzyme
-
r
alpha-cyclodextrin + maltose
beta-cyclodextrin + maltooligosaccharide
show the reaction diagram
-
immobilized enzyme
-
r
alpha-cyclodextrin + maltotetraose
beta-cyclodextrin + maltooligosaccharide
show the reaction diagram
-
immobilized enzyme
-
r
alpha-cyclodextrin + maltotriose
beta-cyclodextrin + maltooligosaccharide
show the reaction diagram
-
immobilized enzyme
-
r
alpha-cyclodextrin + sucrose
beta-cyclodextrin + maltooligosaccharide
show the reaction diagram
-
immobilized enzyme
-
r
amylose + glycosyl acceptor
cyclodextrin
show the reaction diagram
-
-
higher yield of large-ring cyclodextrins are ontained with a reaction temperature of 60C compared to 40C
-
?
beta-cyclodextrin + D-glucose
alpha-cyclodextrin + maltooligosaccharide
show the reaction diagram
-
immobilized enzyme
-
r
beta-cyclodextrin + glycosyl acceptor
alpha-cyclodextrin + maltooligosaccharide
show the reaction diagram
beta-cyclodextrin + maltohexaose
alpha-cyclodextrin + maltooligosaccharide
show the reaction diagram
-
immobilized enzyme
-
r
beta-cyclodextrin + maltose
alpha-cyclodextrin + maltooligosaccharide
show the reaction diagram
beta-cyclodextrin + maltotetraose
alpha-cyclodextrin + maltooligosaccharide
show the reaction diagram
-
immobilized enzyme
-
r
beta-cyclodextrin + maltotriose
alpha-cyclodextrin + maltooligosaccharide
show the reaction diagram
-
immobilized enzyme
-
r
beta-cyclodextrin + sucrose
alpha-cyclodextrin + maltooligosaccharide
show the reaction diagram
-
immobilized enzyme
-
r
cyclohexaamylose + D-glucose
linear oligosaccharide
show the reaction diagram
-
-
-
r
cyclohexaamylose + maltose
linear oligosaccharide
show the reaction diagram
-
-
-
r
cyclohexaamylose + sucrose
linear oligosaccharide
show the reaction diagram
-
-
-
r
cyclomaltohexaose + methyl alpha-D-glucopyranoside
maltodextrin glycoside
show the reaction diagram
-
the reactions are optimized by using different ratios of the D-glucopyranosides to cyclomaltohexaose. The lower ratios of 0.5-1.0 give a wide range of sizes from d.p. 2-17 and higher. As the molar ratio is increased from 1.0 to 3.0, the larger sizes, d.p. 917, decrease, and the small and intermediate sizes, d.p. 28, increase. As the molar ratios are increased further from 3.0 to 5.0, the large sizes completely disappear, the intermediate sizes, d.p. 48, decrease, and the small sizes, d.p. 2 and 3 become predominant
-
-
?
cyclomaltohexaose + methyl beta-D-glucopyranoside
maltodextrin glycoside
show the reaction diagram
-
the reactions are optimized by using different ratios of the D-glucopyranosides to cyclomaltohexaose. The lower ratios of 0.5-1.0 give a wide range of sizes from d.p. 2-17 and higher. As the molar ratio is increased from 1.0 to 3.0, the larger sizes, d.p. 917, decrease, and the small and intermediate sizes, d.p. 28, increase. As the molar ratios are increased further from 3.0 to 5.0, the large sizes completely disappear, the intermediate sizes, d.p. 48, decrease, and the small sizes, d.p. 2 and 3 become predominant
-
-
?
cyclomaltohexaose + phenyl alpha-D-glucopyranoside
maltodextrin glycoside
show the reaction diagram
-
the reactions are optimized by using different ratios of the D-glucopyranosides to cyclomaltohexaose. The lower ratios of 0.51.0 give a wide range of sizes from d.p. 217 and higher. As the molar ratio is increased from 1.0 to 3.0, the larger sizes, d.p. 917, decrease, and the small and intermediate sizes, d.p. 28, increase. As the molar ratios are increased further from 3.0 to 5.0, the large sizes completely disappear, the intermediate sizes, d.p. 48, decrease, and the small sizes, d.p. 2 and 3 become predominant
-
-
?
cyclomaltohexaose + phenyl beta-D-glucopyranoside
maltodextrin glycoside
show the reaction diagram
-
the reactions are optimized by using different ratios of the D-glucopyranosides to cyclomaltohexaose. The lower ratios of 0.51.0 give a wide range of sizes from d.p. 217 and higher. As the molar ratio is increased from 1.0 to 3.0, the larger sizes, d.p. 917, decrease, and the small and intermediate sizes, d.p. 28, increase. As the molar ratios are increased further from 3.0 to 5.0, the large sizes completely disappear, the intermediate sizes, d.p. 48, decrease, and the small sizes, d.p. 2 and 3 become predominant
-
-
?
dodecyl-beta-D-maltoside + alpha-cyclodextrin
dodecyl-beta-D-maltooctaoside + ?
show the reaction diagram
-
the equilibrium lays to 80% on the side of dodecyl-beta-D-maltooctaoside production when the enzyme from Bacillus macerans is used as biocatalyst
-
-
r
glycogen + acceptor
beta-cyclodextrin
show the reaction diagram
L-ascorbic acid + beta-cyclodextrin
L-ascorbic acid-2-O-alpha-D-glucoside + ?
show the reaction diagram
-
-
-
?
L-ascorbic acid + maltodextrin
L-ascorbic acid-2-O-alpha-D-glucoside + ?
show the reaction diagram
-
-
-
?
maltodextrin + L-ascorbic acid
2-O-D-glucopyranosyl-L-ascorbic acid + ?
show the reaction diagram
-
-
-
-
?
maltooligosaccharides + glycosyl acceptor
cyclodextrins
show the reaction diagram
soluble starch
alpha-cyclodextrin
show the reaction diagram
-
poly-lysine fused immobilization increases the Vmax of the immobilized CGTase by 40% without a change in Km. Maximum alpha-cyclodextrin productivity of 539.4 g/l*h is obtained with 2% soluble starch solution which is constantly fed at a flow rate of 4.0 ml/min in a continuous operation mode of a packed-bed reactor
-
-
?
soluble starch
alpha-cyclodextrin + beta-cyclodextrin + gamma-cyclodextrin
show the reaction diagram
-
-
at the initial stage of the reaction, alpha-cyclodextrin is the main product. Subsequently, the proportion of beta-cyclodextrin increases and becomes the main product after prolonged incubation. After 10 h or 40 h of incubation, the conversion rates of starch into cyclodextrins are 36.8% or 42.3%, respectively
-
?
soluble starch + cellobiose
?
show the reaction diagram
-
-
-
-
r
soluble starch + D-fructose
?
show the reaction diagram
-
-
-
-
r
soluble starch + D-galactose
?
show the reaction diagram
soluble starch + D-glucose
cyclodextrins
show the reaction diagram
-
-
-
-
-
soluble starch + D-maltose
cyclodextrins
show the reaction diagram
-
-
-
-
r
soluble starch + D-rhamnose
?
show the reaction diagram
-
-
-
-
r
soluble starch + D-sorbose
?
show the reaction diagram
-
-
-
-
r
soluble starch + D-xylose
?
show the reaction diagram
soluble starch + glycosyl acceptor
alpha-cyclodextrin
show the reaction diagram
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
show the reaction diagram
soluble starch + glycosyl acceptor
beta-cyclodextrin
show the reaction diagram
soluble starch + glycosyl acceptor
cyclodextrin
show the reaction diagram
-
-
-
-
?
soluble starch + glycosyl acceptor
cyclodextrins
show the reaction diagram
soluble starch + glycosyl acceptor
cyclohexaamylose
show the reaction diagram
-
-
-
r
soluble starch + glycosyl acceptor
gamma-cyclodextrin
show the reaction diagram
soluble starch + glycosyl acceptor
Schardinger dextrins
show the reaction diagram
-
-
-
-
r
soluble starch + H2O
cyclodextrins
show the reaction diagram
soluble starch + L-sorbose
?
show the reaction diagram
-
-
-
-
r
soluble starch + maltotriose
cyclodextrins
show the reaction diagram
-
-
-
-
r
soluble starch + myo-inositol
?
show the reaction diagram
-
-
-
-
r
soluble starch + ribose
?
show the reaction diagram
-
-
-
-
r
soluble starch + sucrose
?
show the reaction diagram
-
-
-
-
r
starch
cyclodextrin
show the reaction diagram
starch + glycosyl acceptor
alpha-cyclodextrin
show the reaction diagram
-
-
-
-
?
starch + glycosyl acceptor
cyclodextrins
show the reaction diagram
starch + hesperidin
glycosyl hesperidin
show the reaction diagram
-
-
-
-
r
starch + salicin
glycosyl salicin
show the reaction diagram
-
-
-
-
r
starch + stevioside
glycosyl stevioside
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
soluble starch + glycosyl acceptor
cyclodextrins
show the reaction diagram
-
-
alpha-cyclodextrin is the main product
-
?
soluble starch + glycosyl acceptor
Schardinger dextrins
show the reaction diagram
-
-
-
-
r
starch + glycosyl acceptor
alpha-cyclodextrin
show the reaction diagram
-
-
-
-
?
starch + glycosyl acceptor
cyclodextrins
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
-
0.5 mM, 125% of initial activity
CaCl2
-
5 mM, 20% activation of cross-linked enzyme crystals, 2% activation of soluble enzyme
Co2+
-
10 mM, 28% inhibition
Cu2+
-
10 mM, 20% inhibition
Fe2+
-
10 mM, 58% inhibition
FeCl2
-
5 mM, 110% activation of cross-linked enzyme crystals, inhibition of soluble enzyme
Hg2+
-
10 mM, complete inhibition
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Hg2+
-
1 mM, 5% of initial activity
HgCl2
-
5 mM, 68% inhibition of cross-linked enzyme crystals, 40% of soluble enzyme
MgCl2
-
5 mM, 15% inhibition of cross-linked enzyme crystals, 22% of soluble enzyme
Ni2+
-
1 mM, 58% of initial activity
starch
-
substrate inhibition at 0.01 and 0.0055 mg starch/ml for free and immobilized enzyme
ZnCl2
-
5 mM, 30% inhibition of cross-linked enzyme crystals, 80% of soluble enzyme
additional information
-
not inhibited by L-ascorbic acid
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bromobenzene
-
increases the yield of beta-cyclodextrin
Ca2+
-
4 mM, 22% activation
cyclohexadec-8-ene-1-one
-
increases the yield of gamma-cyclodextrin
Cyclohexane
cyclotridecanone
-
increases the yield of gamma-cyclodextrin
Decanol
-
increases the yield of alpha-cyclodextrin
EDTA
-
10 mM, 105% of initial activity
ethanol
Isopropanol
-
increases the yield of beta-cyclodextrin
n-butanol
-
increases the yield of alpha-cyclodextrin
Octanol
-
increases the yield of alpha-cyclodextrin
pentadecane
-
increases the yield of beta-cyclodextrin
Toluene
Trichloroethylene
-
increases the yield of beta-cyclodextrin
undecane
-
increases the yield of beta-cyclodextrin
additional information
-
synergistic promoting effects of glycine and Ca2+ on the extracellular secretion of the recombinant protein in Escherichia coli, optimal at 150 mM and 20 mM, respectively, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.26 - 2.32
alpha-cyclodextrin
0.08
beta-cyclodextrin
-
cyclodextrin opening
0.25
gamma-cyclodextrin
-
cyclodextrin opening
38.3 - 51.7
L-ascorbic acid
0.47 - 0.64
maltodextrin
0.58 - 2.1
starch
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000086 - 0.000133
L-ascorbic acid
0.004 - 0.0124
maltodextrin
0.442 - 1.66
starch
additional information
additional information
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
Ki-value for starch: 0.01 mg/ml (soluble enzyme), 0.0055 mg/ml (enzyme immobilized on alginate)
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.01
-
gamma-cyclodextrin, opening
0.02
-
beta-cyclodextrin, opening
1.1
-
gamma-cyclization, wild-type enzyme
1.24
-
gamma-cyclodextrin, opening
1.42
-
alpha-cyclodextrin, opening
2.4
-
maltotriose, disproportionation
14.4
-
beta-cyclodextrin-forming activity, recombinant wild-type enzyme
21.7
-
beta-cyclodextrin-forming activity, recombinant mutant K47R
32.2
-
beta-cyclization, wild-type enzyme
35.9
-
beta-cyclodextrin-forming activity, recombinant mutant K47H
37.4
-
alpha-cyclodextrin, coupling
45.9
-
alpha-cyclodextrin-forming activity, recombinant mutant K47L
46.4
-
alpha-cyclodextrin-forming activity, recombinant mutant K47S
47.4
-
alpha-cyclodextrin-forming activity, recombinant mutant K47T
51.4
-
beta-cyclodextrin-forming activity, recombinant mutant K47T
51.5
-
beta-cyclodextrin-forming activity, recombinant mutant K47S
53.1
-
beta-cyclodextrin-forming activity, recombinant mutant K47L
62.9
-
alpha-cyclodextrin-forming activity, recombinant mutant K47H
77.3
-
alpha-cyclodextrin-forming activity, recombinant mutant K47R
85.1
-
alpha-cyclodextrin-forming activity, recombinant wild-type enzyme
190.4
-
alpha-cyclization, wild-type enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 5.7
5.7
recombinant enzyme, cgtM gene product
6.1 - 6.2
additional information
-
the enzymes are more active in glycine/NaOH buffer compared with Na2HPO4/NaH2PO4 buffer at the same pH
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 8.5
4 - 9.5
-
loss of cyclization activity above and below
5 - 7
-
pH 5.0: about 70% of maximal activity, pH 9.0: about 70% of maximal activity, native enzyme
5 - 8
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
strain IFO3490
40 - 60
-
immobilized enzyme
45
-
recombinant enzyme
50
-
native enzyme
60 - 70
-
cross-linked enzyme crystals
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 70
40 - 50
-
more than 95% of maximum activity, recombinant enzyme
40 - 70
-
40C: about 50% of maximal activity, 70C: about 80% of maximal activity
40 - 75
-
40C: about 40% of maximal activity, 75C: about 15% of maximal activity, soluble enzyme
40 - 80
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
no alpha-CGTase activity in the soluble cytoplasmic fraction, very low activity in the periplasmic fraction
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
the enzyme is responsible for cyclodextrin formation. Cyclodextrins are cyclic, nonreducing oligo-glucopyranose molecules linked via alpha(1,4)-glycosidic bonds mainly consisting of six, seven, or eight glucose residue, alpha-, beta-, or gamma-cyclodextrin, respectively
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
CDGT1_PAEMA
714
0
76960
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
38000
65000
66000
67000
68000
72000
-
1 * 72000, SDS-PAGE
74000
74010
strain IFO3490, amino acid composition deduced from nucleotide sequence
75000
76000
-
x * 76000, about, His-tagged wild-type and mutant enzymes, SDS-PAGE
139000
-
ATCC 8514, intracelluar enzyme
139300
-
sedimentation and diffusion data
145000
-
ATCC 8514, extracelluar enzyme
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
monomer
additional information
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion technique. Cross-linked enzyme crystals can be useful biocatalysts because they are stable at elevated temperature, in organic solvents, and in the presence of enzyme inactivation surfactant. They also maintain their activity against protein-digesting enzyme
-
mutant Y167H, hanging drop vapor diffusion method, using 15% (w/v) PEG 4000, 0.05 M Tris-HCl, 0.1 M sodium acetate buffer, 25 mM Na2HPO4, 150 mM NaCl, 10 mM imidazole pH 8.5
mutant Y195I, hanging drop vapor diffusion method, using 0.2 M sodium acetate trihydrate, 0.1 M Tris hydrochloride pH 9.0, 30% (w/v) polyethylene glycol 4000, at 22C
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D372K
-
site-directed mutagenesis, the mutant shows a great shift in substrate specificity towards the production of alpha-cyclodextrin
D372K/Y89R
-
site-directed mutagenesis, the mutant enzyme shows a 1.5fold increase in the production of alpha-cyclodextrin, with a concomitant 43% decrease in the production of beta-cyclodextrin compared to the wild-type CGTase
K47F
improved synthesis of 2-O-D-glucopyranosyl-L-ascorbic acid with maltodextrin as glucosyl donor, 30% increase in yield. Mutation leads to relatively lower cyclization activities and higher disproportionation activities. The enhancement of maltodextrin specificity may be due to the short residue chain and the removal of hydrogen bonding interactions between the side chain of residue 47 and the sugar at -3 subsite
K47H
-
site-directed mutagenesis, the mutant shows a shift in product specificity, slight enhancement of beta-cyclodextrin production and slight reduction of alpha-cyclodextrin production compared to the wild-type enzyme, the mutant enzyme exhibits lower stability compared to the wild-type enzyme
K47R
-
site-directed mutagenesis, the mutant shows a shift in product specificity, slight enhancement of beta-cyclodextrin production and slight reduction of alpha-cyclodextrin production compared to the wild-type enzyme, the mutant enzyme exhibits lower stability compared to the wild-type enzyme
K47S
-
site-directed mutagenesis, the mutant shows a shift in product specificity, enhancement of beta-cyclodextrin production and reduction of alpha-cyclodextrin production compared to the wild-type enzyme, the mutant enzyme exhibits lower stability compared to the wild-type enzyme
K47T
-
site-directed mutagenesis, the mutant shows a shift in product specificity, enhancement of beta-cyclodextrin production and reduction of alpha-cyclodextrin production compared to the wild-type enzyme, the mutant enzyme exhibits lower stability compared to the wild-type enzyme
K47V
improved synthesis of 2-O-D-glucopyranosyl-L-ascorbic acid with maltodextrin as glucosyl donor, 48% increase in yield. Mutation leads to relatively lower cyclization activities and higher disproportionation activities. The enhancement of maltodextrin specificity may be due to the short residue chain and the removal of hydrogen bonding interactions between the side chain of residue 47 and the sugar at -3 subsite
K47W
improved synthesis of 2-O-D-glucopyranosyl-L-ascorbic acid with maltodextrin as glucosyl donor, 24% increase in yield. Mutation leads to relatively lower cyclization activities and higher disproportionation activities. The enhancement of maltodextrin specificity may be due to the short residue chain and the removal of hydrogen bonding interactions between the side chain of residue 47 and the sugar at -3 subsite
Q265K
-
the mutant shows 15% cyclization (alpha-cyclodextrin-forming) and 236% hydrolysis (starch-degrading) activities compared to the wild type enzyme; the mutant with enhanced maltodextrin specificity produces higher 2-O-D-glucopyranosyl-L-ascorbic acid yields than the wild type enzyme. Compared with the wild type enzyme, the mutant has lower cyclization activity and higher hydrolysis and disproportionation activity
Q265K/Y195S
-
the mutant shows no cyclization (alpha-cyclodextrin-forming) and 226% hydrolysis (starch-degrading) activities compared to the wild type enzyme
R146A/D147P
-
the double mutant exhibits a ratio of alpha-cyclodextrin to total cyclodextrin production of 75.1%, approximately one-fifth greater than that of the wild-type enzyme (63.2%), without loss of thermostability
R146P/D147A
-
the double mutant exhibits a ratio of alpha-cyclodextrin to total cyclodextrin production of 76.1%, approximately one-fifth greater than that of the wild-type enzyme (63.2%), without loss of thermostability
Y167H
Y195I
-
the mutation drastically alters the cyclodextrin specificity of the enzyme by switching toward the synthesis of both beta- and gamma-cyclodextrins
Y195S
-
the mutant shows no cyclization (alpha-cyclodextrin-forming) and 200% hydrolysis (starch-degrading) activities compared to the wild type enzyme; the mutant with enhanced maltodextrin specificity produces higher 2-O-D-glucopyranosyl-L-ascorbic acid yields than the wild type enzyme. Compared with the wild type enzyme, the mutant has lower cyclization activity and higher hydrolysis and disproportionation activity
Y195S/Q265K
-
compared with the wild type enzyme, the mutant has no cyclization activity and 498% hydrolysis and disproportionation activity
Y195S/Y260R
-
compared with the wild type enzyme, the mutant has lower cyclization activity and higher hydrolysis and disproportionation activity
Y260R
-
the mutant shows no cyclization (alpha-cyclodextrin-forming) and 226% hydrolysis (starch-degrading) activities compared to the wild type enzyme; the mutant with enhanced maltodextrin specificity produces higher 2-O-D-glucopyranosyl-L-ascorbic acid yields than the wild type enzyme. Compared with the wild type enzyme, the mutant has lower cyclization activity and higher hydrolysis and disproportionation activity
Y260R/Q265K
-
compared with the wild type enzyme, the mutant has 8% cyclization activity and 213% hydrolysis activity
Y260R/Q265K/Y195S
-
the mutant shows 12% cyclization (alpha-cyclodextrin-forming) and 557% hydrolysis (starch-degrading) activities compared to the wild type enzyme
Y260R/Y195S
-
the mutant shows no cyclization (alpha-cyclodextrin-forming) and 492% hydrolysis (starch-degrading) activities compared to the wild type enzyme
Y89D
-
site-directed mutagenesis, the mutant shows a shift in substrate specificity towards the production of alpha-cyclodextrin
Y89K
-
site-directed mutagenesis, the mutant shows a shift in substrate specificity towards the production of alpha-cyclodextrin
Y89N
-
site-directed mutagenesis, the mutant shows a shift in substrate specificity towards the production of alpha-cyclodextrin
Y89R
-
site-directed mutagenesis, the mutant shows a great shift in substrate specificity towards the production of alpha-cyclodextrin
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 10
-
-
488830
5.5
-
the half-life at pH 5.5 is 29.8 h
735493
6 - 9.5
-
-
719222
6.5 - 8.5
-
stable at 50C
488839
8 - 10
-
-
488825, 488855
additional information
-
the immobilized and the crosslinked imprinted CGTase shows higher stability in the ranges from pH 3 to 7 and from pH 9 to 11
673578
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 50
-
immobilized enzyme is stable at 40C, heat inactivation above 50C
45
-
half-life about 1.25 h
50 - 55
-
thermal stability of immobilized enzyme on chitosan increases from 50C to 55C
50 - 60
-
purified enzyme is quite stable at 50C, but loses 80% of its activity at 60C for 30 min
50 - 70
-
immobilized enzyme is more stable than soluble enzyme, inactivation of the soluble enzyme at 50C is 1.6 times, at 60C is 6.9 times and at 70C is 24.3 times faster
58 - 60
-
undergoes rapid inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
cross-linked enzyme crystals are slightly more resistant to 2-butanol and acetonitrile than DMSO. In 15% solution of 2-butanol, over 100% of the activity is retained in CGTase-cross-linking enzyme crystals while 28% of the activity remains in the case of soluble CGTase
-
enzyme immobilized on alginate shows a high operational stability by retaining almost 75% of the initial activity after seventh use
-
immobilization in strongly hydrophilic microenvironment markedly enhances conformational stability in a wide temperature and pH range
-
more than 80% of the initial immobilized and crosslinked imprinted CGTase activity is retained for up to five cycles of synthesis reactions
-
prolonged digestion with trypsin does not affect the catalytic properties
-
SDS, 1%, only 7% of the activity of soluble enzyme activity remains, cross-linked enzyme crystals exhibit strong activity
-
the immobilized and CD8-crosslinked imprinted CGTase shows 15% higher stability in phosphate buffer containing up to 50% ethanol or cyclohexane compared to the native enzyme
-
the operational half-life of the packed-bed enzyme reactor (enzyme immobilized onto a cation exchanger by ionic interaction, poly-lysine fused immobilization) is estimated 12 days at 25C and pH 6.0
-
the temperature stability of the immobilized and crosslinked imprinted CGTase at 60C is considerably higher than that of the native enzyme
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-butanol
-
in 15% solution of 2-butanol, over 100% of the activity is retained in CGTase-cross-linking enzyme crystals while 28% of the activity remains in the case of soluble CGTase
2-propanol
-
stable in presence, but not active, relative residual activity 96%
acetonitrile
-
in 15% solution of 2-butanol, over 100% of the activity is retained in CGTase-cross-linking enzyme crystals while 60% of the activity remains in the case of soluble CGTase
benzene
-
relative residual activity 92%
chloroform
-
stable in presence, but not active
cyclohexane
-
relative residual activity 91%
Ethanol
-
stable in presence, but not active, relative residual activity 99%
hexane
-
n-hexane, relative residual activity 90%
Methanol
-
stable in presence, but not active, relative residual activity 98%
p-xylene
-
p-xylene, relative residual activity 100%
toluene
-
relative residual activity 100%
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
mutant Y167H with ammonium sulfate precipitation and Ni-NTA agarose column chromatography
Ni-NTA agarose column chromatography
-
Ni-NTA agarose column chromatography and Sephacryl-100 gel filtration
-
recombinant enzyme
-
recombinant enzyme, cgtM gene product
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
wild-type and recombinant enzymes
-
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
cloned and overexpressed in Bacillus subtilis
-
cloned and overexpressed in Escherichia coli
-
coexpression of folding accessory proteins for production of active cyclodextrin glycosyltransferase in Escherichia coli. The optimal coexpression partner, human peptidyl-prolyl cis-trans isomerase, is applied to fed-batch cultures of recombinant Escherichia coli in an attempt to develop an industrialy viable process
-
DNA and amino acid sequence determination and analysis, phylogenetic tree
-
expressed as inclusion body in recombinant Escherichia coli. The refolding yield of CGTase is enhanced by 71% by the immobilized poly-arginine fused minichaperone (MiniELR10) compared with a conventional refolding method. Minichaperone immobilized by poly-arginine fusion could assist refolding of heterologous proteins expressed as inclusion body
-
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
expression in Escherichia coli strain BL21(DE3), glycine, as a medium supplement, can enhance the extracellular secretion of recombinant alpha-CGTase by 11fold. Glycine supplementation exerts impaired cell growth inhibiting an increased enzyme production, but Ca2+ can remedy cell growth inhibition induced by glycine, thereby leading to further increase in the glycine-enhanced extracellular secretion of recombinant alpha-CGTase, effects on the bacterial cell membrane permeability, overview
-
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
mutant Y167H is expressed in Escherichia coli BL21(DE3) cells
mutant Y195I is expressed in Escherichia coli BL21(DE3) cells
-
overexpression and extracellular secretion of the recombinant alpha-cyclodextrin glycosyltransferase in Escherichia coli strain BL21(DE3), promotable by glycine, when supplemented optimally at the middle of the exponential growth phase at 1%, the enzyme production is increased by 11fold, glycine supplementation at the beginning of cell growth achieves a 1.2fold activation, overview. Glycine increases the cell membrane permeability, mechanism, overview
-
strain IFO3490, vector plasmid pTB523, gene cgtM cloned in Bacillus subtilis NA-1, sequence determined, chimeric GTAse gene constructed by using cgt-1 from Bacillus stearothermophilus NO2
subcloning in Escherichia coli strain JM109, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
pharmacology
-
important enzyme in pharmaceutical industry
synthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
DePinto, J.A.; Campbell, L.L.
Purification and properties of the amylase of Bacillus macerans
Biochemistry
7
114-120
1968
Bacillus subtilis, Homo sapiens, Paenibacillus macerans, Sus scrofa
Manually annotated by BRENDA team
Kitahata, S.; Tsuyama, N.; Okada, S.
Purification and some properties of cyclodextrin glycosyltransferase from a strain of Bacillus species
Agric. Biol. Chem.
38
387-393
1974
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) 5, Paenibacillus macerans
-
Manually annotated by BRENDA team
Nakamura, N.; Horikoshi, K.
Purification and properties of neutral-cyclodextrin glycosyl-transferase of an alkalophilic Bacillus sp.
Agric. Biol. Chem.
40
1785-1791
1976
Bacillus circulans, Bacillus megaterium, Bacillus sp. (in: Bacteria), Geobacillus stearothermophilus, Paenibacillus macerans
-
Manually annotated by BRENDA team
Bender, H.
Cyclodextrin glucanotransferase from Klebsiella pneumoniae. 1. Formation, purification and properties of the enzyme from Klebsiella pneumoniae M 5 al
Arch. Microbiol.
111
271-282
1977
Bacillus megaterium, Bacillus megaterium No5, Klebsiella oxytoca, Klebsiella pneumoniae, Klebsiella pneumoniae M5, Paenibacillus macerans
Manually annotated by BRENDA team
Kobayashi, S.; Kainuma, K.; Suzuki, S.
Purification and some properties of Bacillus macerans cycloamylose (cyclodextrin) glucanotransferase
Carbohydr. Res.
61
229-238
1978
Paenibacillus macerans
Manually annotated by BRENDA team
Stavn, A.; Granum, P.E.
Purification and physiocochemical properties of an extra-cellular cycloamylose (cyclodextrin) glucanotransferase from Bacillus macerans
Carbohydr. Res.
75
243-250
1979
Paenibacillus macerans
Manually annotated by BRENDA team
Ivony, K.; Szajani, B.; Seres, G.
Immobilization of starch-degrading enzymes. I. A comparative study on soluble and immobilized cyclodextrin glycosyltransferase
J. Appl. Biochem.
5
158-164
1983
Paenibacillus macerans
-
Manually annotated by BRENDA team
Kato, T.; Horikoshi, K.
Immobilzed cyclomaltodextrin glucanotransferase of an alkalophilic Bacillus sp. No. 38-2
Biotechnol. Bioeng.
26
595-598
1984
Bacillus circulans, Bacillus megaterium, Bacillus sp. (in: Bacteria), Geobacillus stearothermophilus, Klebsiella pneumoniae, Paenibacillus macerans
Manually annotated by BRENDA team
Aoki, H.; Yao, D.; Misawa, M.
Production and characterization of a thermostable bacterial cyclodextrin glycosyltransferase
Prog. Biotechnol.
3
81-93
1987
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) IT25, Geobacillus stearothermophilus, Klebsiella oxytoca, Paenibacillus macerans
-
Manually annotated by BRENDA team
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
Bacillus circulans, Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) 1011, Klebsiella pneumoniae, Paenibacillus macerans, Paenibacillus macerans IAM1243
-
Manually annotated by BRENDA team
Pongsawasdi, P.; Yagisawa, M.
Purification and properties of cyclomaltodextrin glucanotransferase from Bacillus circulans
Agric. Biol. Chem.
52
1099-1103
1988
Bacillus circulans, Bacillus circulans C31, Bacillus megaterium, Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) Ha3-3-2 / ATCC 39612, Paenibacillus macerans
-
Manually annotated by BRENDA team
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
Bacillus circulans, Bacillus megaterium, Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) AL-6, Bacillus subtilis, Bacillus subtilis 313, Paenibacillus macerans
-
Manually annotated by BRENDA team
Akimaru, K.; Yagi, T.; Yamamoto, S.
Purification and properties of Bacillus coagulans cyclomaltodextrin glucanotransferase
J. Ferment. Bioeng.
71
322-328
1991
Bacillus circulans, Bacillus coagulans, Bacillus megaterium, Bacillus ohbensis, Bacillus sp. (in: Bacteria), Bacillus subtilis, Bacillus subtilis 313, Geobacillus stearothermophilus, Geobacillus stearothermophilus TC-60, Klebsiella oxytoca, Klebsiella pneumoniae, Paenibacillus macerans
-
Manually annotated by BRENDA team
Lee, S.H.; Shin, H.D.; Lee, Y.H.
Evaluation of immobilization methods for cyclodextrin glucanotransferase and characterization of its enzymic properties
J. Microbiol. Biotechnol.
1
54-62
1991
Paenibacillus macerans
-
Manually annotated by BRENDA team
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
Bacillus alcalophilus, Bacillus circulans, Bacillus circulans 8, Bacillus circulans E 192, Bacillus megaterium, Bacillus ohbensis, Geobacillus stearothermophilus, Klebsiella pneumoniae, Micrococcus sp., Paenibacillus macerans
Manually annotated by BRENDA team
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
Bacillus circulans, Bacillus circulans 8, Geobacillus stearothermophilus, Geobacillus stearothermophilus NO2, Geobacillus stearothermophilus TC-91, Klebsiella oxytoca, Paenibacillus macerans
Manually annotated by BRENDA team
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 circulans, Bacillus circulans 8, Bacillus licheniformis, Bacillus megaterium, Bacillus sp. (in: Bacteria), Bacillus subtilis, Bacillus subtilis NA-1, Geobacillus stearothermophilus, Geobacillus stearothermophilus (P31797), Geobacillus stearothermophilus NO2, Klebsiella oxytoca, Klebsiella pneumoniae, Paenibacillus macerans (P04830), Paenibacillus macerans, Paenibacillus macerans IAM1243
Manually annotated by BRENDA team
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
Bacillus circulans, Geobacillus stearothermophilus, Geobacillus stearothermophilus TC-91, Paenibacillus macerans
Manually annotated by BRENDA team
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
Bacillus autolyticus, Bacillus autolyticus 11149, Bacillus circulans, Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) AL-6, Geobacillus stearothermophilus, Klebsiella oxytoca, Paenibacillus macerans
-
Manually annotated by BRENDA team
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
Bacillus circulans, Bacillus licheniformis, Bacillus ohbensis, Bacillus sp. (in: Bacteria) 1011, Bacillus sp. (in: Bacteria) 17-1, Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) B1018, Geobacillus stearothermophilus, Klebsiella pneumoniae, Paenibacillus macerans
Manually annotated by BRENDA team
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
Bacillus alcalophilus, Bacillus circulans, Bacillus circulans DF9, Bacillus coagulans, Bacillus lentus, Bacillus megaterium, Bacillus sp. (in: Bacteria), Bacillus subtilis, Geobacillus stearothermophilus, Klebsiella oxytoca, Paenibacillus macerans
Manually annotated by BRENDA team
Park, D.C.; Kim, T.K.; Lee, Y.H.
Characteristics of transglycosylation reaction of cyclodextrin glucanotransferase in the heterogeneous enzyme reaction system using extrusion starch as a glucosyl donor
Enzyme Microb. Technol.
22
217-222
1998
Bacillus megaterium, Bacillus megaterium No5, Geobacillus stearothermophilus, Paenibacillus macerans
-
Manually annotated by BRENDA team
Tonkova, A.
Bacterial cyclodextrin glucanotransferase
Enzyme Microb. Technol.
22
678-686
1998
Bacillus cereus, Bacillus cereus NCIMB 13123, Bacillus circulans, Bacillus circulans 8, Bacillus coagulans, Bacillus lentus, Bacillus licheniformis, Bacillus megaterium, Bacillus megaterium No5, 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, Lysinibacillus sphaericus, Lysinibacillus sphaericus ATCC 7055, Micrococcus luteus, Paenibacillus macerans, Paenibacillus macerans IAM1243, Salimicrobium halophilum, Salimicrobium halophilum INMIA-3849, Thermoanaerobacterium thermosulfurigenes, Thermoanaerobacterium thermosulfurigenes EM1
-
Manually annotated by BRENDA team
Jeang, C.L.; Wung, C.H.; Chang, B.Y.; Yeh, S.S.; Lour, D.W.
Characterization of the Bacillus macerans cyclodextrin glucanotransferase overexpressed in Escherichia coli
Proc. Natl. Sci. Counc. Repub. China B
23
62-68
1999
Paenibacillus macerans
Manually annotated by BRENDA team
Tachibana, Y.; Kuramura, A.; Shirasaka, N.; Suzuki, Y.; Yamamoto, T.; Fujiwara, S.; Takagi, M.; Imanaka, T.
Purification and characterization of an extremely thermostable cyclomaltodextrin glucanotransferase from a newly isolated hyperthermophilic archaeon, a Thermococcus sp
Appl. Environ. Microbiol.
65
1991-1997
1999
Bacillus licheniformis (P14014), Bacillus sp. (in: Bacteria) 1011, Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) (P31746), Brevibacterium sp., Brevibacterium sp. 9605, Geobacillus stearothermophilus, Geobacillus stearothermophilus (P31797), Klebsiella oxytoca, Klebsiella pneumoniae, Paenibacillus macerans (P04830), Paenibacillus macerans, Thermoanaerobacterium thermosulfurigenes (P26827), Thermoanaerobacterium thermosulfurigenes, Thermoanaerobacter sp., Thermococcus sp., Thermococcus sp. B1001
Manually annotated by BRENDA team
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
Bacillus alcalophilus, Bacillus alcalophilus B-3103, Bacillus alcalophilus BA-4229, Bacillus circulans, Bacillus circulans BIO-3m, Bacillus coagulans, Bacillus coagulans BIO-13m, Bacillus licheniformis, Bacillus licheniformis B-4025, Bacillus licheniformis BIO-9m, Geobacillus stearothermophilus, Geobacillus stearothermophilus B-4006, Paenibacillus macerans, Paenibacillus macerans BIO-2m, Salimicrobium halophilum, Salimicrobium halophilum BIO-12H BIO-13H, Thermoactinomyces vulgaris, Thermoactinomyces vulgaris Tac-3554
Manually annotated by BRENDA team
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
Bacillus circulans (P43379), Bacillus circulans 251 (P43379), Bacillus licheniformis, Geobacillus stearothermophilus, Geobacillus stearothermophilus ET1, Geobacillus stearothermophilus NO2, Klebsiella pneumoniae, Paenibacillus macerans
Manually annotated by BRENDA team
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 circulans, Bacillus circulans (P43379), Bacillus circulans 251, Bacillus circulans 251 (P43379), Bacillus sp. (in: Bacteria) 1011, Bacillus sp. (in: Bacteria), Geobacillus stearothermophilus, Geobacillus stearothermophilus (P31797), Klebsiella oxytoca (P08704), Paenibacillus macerans (P31835), Thermoanaerobacterium thermosulfurigenes, Thermoanaerobacterium thermosulfurigenes EM1, Thermococcus kodakarensis (Q8X268), Thermococcus sp. (Q9UWN2), Thermococcus sp., Thermococcus sp. B1001 (Q9UWN2), Thermococcus sp. B1001
Manually annotated by BRENDA team
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
Bacillus circulans, Bacillus circulans 251, Bacillus megaterium, Bacillus ohbensis, Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) BE101, Brevibacterium sp., Brevibacterium sp. 9605, Paenibacillus illinoisensis, Paenibacillus illinoisensis ST-12K, Paenibacillus macerans, Salimicrobium halophilum, Thermoanaerobacterium thermosulfurigenes
Manually annotated by BRENDA team
Yoon, S.H.; Bruce Fulton, D.; Robyt, J.F.
Enzymatic synthesis of two salicin analogues by reaction of salicyl alcohol with Bacillus macerans cyclomaltodextrin glucanyltransferase and Leuconostoc mesenteroides B-742CB dextransucrase
Carbohydr. Res.
339
1517-1529
2004
Paenibacillus macerans
Manually annotated by BRENDA team
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
Bacillus circulans (Q9F5W3), Bacillus circulans A11, Bacillus circulans A11 (Q9F5W3), Paenibacillus macerans (O52766), Paenibacillus macerans IAM1243 (O52766), Paenibacillus macerans IAM1243
Manually annotated by BRENDA team
Kim, W.; Chae, H.; Park, C.; Lee, K.
Stability and activity of crosslinking enzyme crystals of cyclodextrin glucanotransferase isolated from Bacillus macerans
J. Mol. Catal. B
26
287-292
2003
Paenibacillus macerans
-
Manually annotated by BRENDA team
Kim, S.G.; Kweon, D.H.; Lee, D.H.; Park, Y.C.; Seo, J.H.
Coexpression of folding accessory proteins for production of active cyclodextrin glycosyltransferase of Bacillus macerans in recombinant Escherichia coli
Protein Expr. Purif.
41
426-432
2005
Paenibacillus macerans
Manually annotated by BRENDA team
Qi, Q.; She, X.; Endo, T.; Zimmermann, W.
Effect of the reaction temperature on the transglycosylation reactions catalyzed by the cyclodextrin glucanotransferase from Bacillus macerans for the synthesis of large-ring cyclodextrins
Tetrahedron
60
799-806
2004
Paenibacillus macerans
-
Manually annotated by BRENDA team
Qi, Q.; Zimmermann, W.
Cyclodextrin glucanotransferase: from gene to applications
Appl. Microbiol. Biotechnol.
66
475-485
2005
Bacillus circulans (P30920), Bacillus circulans (P43379), Bacillus circulans (Q9F5W3), Bacillus circulans 251 (P43379), Bacillus circulans 8 (P30920), Bacillus circulans A11 (Q9F5W3), Bacillus clarkii (Q8L3E0), Bacillus clarkii 7384 (Q8L3E0), Bacillus firmus, Bacillus firmus 290-3, Bacillus licheniformis (P14014), Bacillus ohbensis (P27036), Bacillus sp. (in: Bacteria) 1011 (P05618), Bacillus sp. (in: Bacteria) 1018 (P17692), 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) 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), Geobacillus stearothermophilus (P31797), Klebsiella oxytoca (P08704), Klebsiella oxytoca M5a1 (P08704), Nostoc sp. (Q8RMG0), Nostoc sp. 9229 (Q8RMG0), Paenibacillus macerans (P31835), Salipaludibacillus agaradhaerens (Q7X3T0), Salipaludibacillus agaradhaerens, Salipaludibacillus agaradhaerens DSM 8721 (Q7X3T0), Salipaludibacillus agaradhaerens DSM 9948, Salipaludibacillus agaradhaerens LS-3C, Streptococcus pyogenes, Thermoanaerobacterium thermosulfurigenes (P26827), Thermoanaerobacter sp., Thermococcus kodakarensis (Q8X268), Thermococcus sp. (Q9UWN2), Thermococcus sp. B1001 (Q9UWN2), Xanthomonas axonopodis, Xanthomonas campestris
Manually annotated by BRENDA team
Yoon, S.H.; Robyt, J.F.
Optimized synthesis of specific sizes of maltodextrin glycosides by the coupling reactions of Bacillus macerans cyclomaltodextrin glucanyltransferase
Carbohydr. Res.
341
210-217
2006
Paenibacillus macerans
Manually annotated by BRENDA team
Kim, S.; Kim, J.; Yu, H.; Lee, D.; Kweon, D.; Seo, J.
Application of poly-arginine fused minichaperone to renaturation of cyclodextrin glycosyltransferase expressed in recombinant Escherichia coli
Enzyme Microb. Technol.
39
459-465
2006
Paenibacillus macerans
-
Manually annotated by BRENDA team
Arya, S.K.; Srivastava, S.K.
Kinetics of immobilized cyclodextrin gluconotransferase produced by Bacillus macerans ATCC 8244
Enzyme Microb. Technol.
39
507-510
2006
Paenibacillus macerans
-
Manually annotated by BRENDA team
Kaulpiboon, J.; Pongsawasdi, P.; Zimmermann, W.
Molecular imprinting of cyclodextrin glycosyltransferases from Paenibacillus sp. A11 and Bacillus macerans with gamma-cyclodextrin
FEBS J.
274
1001-1010
2007
Paenibacillus macerans, Paenibacillus sp., Paenibacillus sp. A11
Manually annotated by BRENDA team
Jeang, C.L.; Lin, D.G.; Hsieh, S.H.
Characterization of cyclodextrin glycosyltransferase of the same gene expressed from Bacillus macerans, Bacillus subtilis, and Escherichia coli
J. Agric. Food Chem.
53
6301-6304
2005
Bacillus subtilis, Escherichia coli, Paenibacillus macerans, Paenibacillus macerans IAM1243
Manually annotated by BRENDA team
Rha, C.; Lee, D.; Kim, S.; Min, W.; Byun, S.; Kweon, D.; Han, N.S.; Seo, J.
Production of cyclodextrin by poly-lysine fused Bacillus macerans cyclodextrin glycosyltransferase immobilized on cation exchanger
J. Mol. Catal. B
34
39-43
2005
Paenibacillus macerans
-
Manually annotated by BRENDA team
Vollu, R.E.; da Mota, F.F.; Gomes, E.A.; Seldin, L.
Cyclodextrin production and genetic characterization of cyclodextrin glucanotranferase of Paenibacillus graminis
Biotechnol. Lett.
30
929-935
2008
Paenibacillus graminis, Paenibacillus macerans (P31835), Paenibacillus macerans, Paenibacillus macerans LMD24.10 (P31835)
Manually annotated by BRENDA team
Son, Y.J.; Rha, C.S.; Park, Y.C.; Shin, S.Y.; Lee, Y.S.; Seo, J.H.
Production of cyclodextrins in ultrafiltration membrane reactor containing cyclodextrin glycosyltransferase from Bacillus macerans
J. Microbiol. Biotechnol.
18
725-729
2008
Paenibacillus macerans (P31835), Paenibacillus macerans
Manually annotated by BRENDA team
Li, Z.; Zhang, J.; Wang, M.; Gu, Z.; Du, G.; Li, J.; Wu, J.; Chen, J.
Mutations at subsite -3 in cyclodextrin glycosyltransferase from Paenibacillus macerans enhancing alpha-cyclodextrin specificity
Appl. Microbiol. Biotechnol.
83
483-490
2009
Paenibacillus macerans
Manually annotated by BRENDA team
Li, Z.; Gu, Z.; Wang, M.; Du, G.; Wu, J.; Chen, J.
Delayed supplementation of glycine enhances extracellular secretion of the recombinant alpha-cyclodextrin glycosyltransferase in Escherichia coli
Appl. Microbiol. Biotechnol.
85
553-561
2010
Paenibacillus macerans, Paenibacillus macerans JFB05-01
Manually annotated by BRENDA team
Leemhuis, H.; Kelly, R.M.; Dijkhuizen, L.
Engineering of cyclodextrin glucanotransferases and the impact for biotechnological applications
Appl. Microbiol. Biotechnol.
85
823-835
2010
Anaerobranca gottschalkii, Bacillus circulans, Bacillus clarkii, Bacillus clarkii 7384, Bacillus clausii, Bacillus clausii E16, Bacillus firmus, Bacillus licheniformis, Bacillus megaterium, 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, Geobacillus stearothermophilus, Geobacillus stearothermophilus ET1, Klebsiella pneumoniae, Klebsiella pneumoniae M5a1, 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., Salipaludibacillus agaradhaerens, Salipaludibacillus agaradhaerens LS-3C, Thermoanaerobacterium thermosulfurigenes, Thermoanaerobacterium thermosulfurigenes EM1, Thermoanaerobacter sp.
Manually annotated by BRENDA team
Svensson, D.; Ulvenlund, S.; Adlercreutz, P.
Efficient synthesis of a long carbohydrate chain alkyl glycoside catalyzed by cyclodextrin glycosyltransferase (CGTase)
Biotechnol. Bioeng.
104
854-861
2009
Paenibacillus macerans, Thermoanaerobacter sp.
Manually annotated by BRENDA team
Yoon, S.H.; Bruce Fulton, D.; Robyt, J.F.
Synthesis of dopamine and L-DOPA-alpha-glycosides by reaction with cyclomaltohexaose catalyzed by cyclomaltodextrin glucanyltransferase
Carbohydr. Res.
344
2349-2356
2009
Paenibacillus macerans
Manually annotated by BRENDA team
Li, Z.F.; Li, B.; Liu, Z.G.; Wang, M.; Gu, Z.B.; Du, G.C.; Wu, J.; Chen, J.
Calcium leads to further increase in glycine-enhanced extracellular secretion of recombinant alpha-cyclodextrin glycosyltransferase in Escherichia coli
J. Agric. Food Chem.
57
6231-6237
2009
Paenibacillus macerans, Paenibacillus macerans JFB05-01
Manually annotated by BRENDA team
Li, Z.F.; Zhang, J.Y.; Sun, Q.; Wang, M.; Gu, Z.B.; Du, G.C.; Wu, J.; Chen, J.
Mutations of lysine 47 in cyclodextrin glycosyltransferase from Paenibacillus macerans enhance beta-cyclodextrin specificity
J. Agric. Food Chem.
57
8386-8391
2009
Paenibacillus macerans, Paenibacillus macerans JFB05-01
Manually annotated by BRENDA team
Han, R.; Liu, L.; Shin, H.D.; Chen, R.R.; Du, G.; Chen, J.
Site-saturation engineering of lysine 47 in cyclodextrin glycosyltransferase from Paenibacillus macerans to enhance substrate specificity towards maltodextrin for enzymatic synthesis of 2-O-D-glucopyranosyl-L-ascorbic acid (AA-2G)
Appl. Microbiol. Biotechnol.
97
5851-5860
2013
Paenibacillus macerans (O52766), Paenibacillus macerans
Manually annotated by BRENDA team
Li, Z.; Li, B.; Gu, Z.; Du, G.; Wu, J.; Chen, J.
Extracellular expression and biochemical characterization of alpha-cyclodextrin glycosyltransferase from Paenibacillus macerans
Carbohydr. Res.
345
886-892
2010
Paenibacillus macerans, Paenibacillus macerans JBF05-01
Manually annotated by BRENDA team
Yue, Y.; Liu, S.; Li, H.; Song, B.; Xie, T.; Sun, Y.; Chao, Y.; Qian, S.
Crystallization and preliminary X-ray diffraction studies of Tyr167His mutant alpha-cyclodextrin glucanotransferase from Bacillus macerans
Acta Crystallogr. Sect. F
69
1186-1189
2013
Paenibacillus macerans (S5ZJ19), Paenibacillus macerans 602-1 (S5ZJ19)
Manually annotated by BRENDA team
Han, R.; Liu, L.; Shin, H.; Chen, R.; Li, J.; Du, G.; Chen, J.
Systems engineering of tyrosine 195, tyrosine 260, and glutamine 265 in cyclodextrin glycosyltransferase from Paenibacillus macerans to enhance maltodextrin specificity for 2-O-D-glucopyranosyl-L-ascorbic acid synthesis
Appl. Environ. Microbiol.
79
672-677
2013
Paenibacillus macerans, Paenibacillus macerans JFB05-01
Manually annotated by BRENDA team
Wang, L.; Duan, X.; Wu, J.
Enhancing the alpha-cyclodextrin specificity of cyclodextrin glycosyltransferase from Paenibacillus macerans by mutagenesis masking the subsite -7
Appl. Environ. Microbiol.
82
2247-2255
2016
Paenibacillus macerans
Manually annotated by BRENDA team
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
Bacillus circulans, Paenibacillus macerans
Manually annotated by BRENDA team
Xie, T.; Hou, Y.; Li, D.; Yue, Y.; Qian, S.; Chao, Y.
Structural basis of a mutant Y195I alpha-cyclodextrin glycosyltransferase with switched product specificity from alpha-cyclodextrin to beta-/gamma-cyclodextrin
J. Biotechnol.
182-183
92-96
2014
Paenibacillus macerans, Paenibacillus macerans 602-1
Manually annotated by BRENDA team
Song, B.; Yue, Y.; Xie, T.; Qian, S.; Chao, Y.
Mutation of tyrosine167histidine at remote substrate binding subsite -6 in alpha-cyclodextrin glycosyltransferase enhancing alpha-cyclodextrin specificity by directed evolution
Mol. Biotechnol.
56
232-239
2014
Paenibacillus macerans, Paenibacillus macerans 602-1
Manually annotated by BRENDA team
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