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Information on EC 2.4.1.19 - cyclomaltodextrin glucanotransferase and Organism(s) Thermoanaerobacterium thermosulfurigenes and UniProt Accession P26827
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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).
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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: Thermoanaerobacterium thermosulfurigenes
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, cyclomaltodextrin glucanyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-1,4-glucan 4-glycosyltransferase, cyclizing
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-
-
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alpha-cyclodextrin glucanotransferase
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-
-
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alpha-cyclodextrin glycosyltransferase
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-
-
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Bacillus macerans amylase
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-
-
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beta-cyclodextrin glucanotransferase
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-
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beta-cyclodextrin glycosyltransferase
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-
-
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BMA
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-
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CGTase
cyclodextrin glucanotransferase
cyclodextrin glycosyltransferase
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-
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cyclomaltodextrin glucotransferase
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cyclomaltodextrin glycosyltransferase
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-
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gamma-cyclodextrin glycosyltransferase
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-
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konchizaimu
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-
-
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neutral-cyclodextrin glycosyltransferase
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-
-
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additional information
CGTase
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-
-
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cyclodextrin glucanotransferase
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-
-
-
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 belongs to the superfamily of glycoside hydrolases
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cyclizes part of a (1->4)-alpha-D-glucan chain by formation of a (1->4)-alpha-D-glucosidic bond
reaction in four steps via cyclization, disproportionation, hydrolysis, and coupling. The second step of the reaction involves the transfer of the covalently bound saccharide to an acceptor molecule
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
cyclization
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-
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hydrolysis
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-
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transglycosylation
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-
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hexosyl group transfer
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-
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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
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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
4,6-O-ethylidene-4-nitrophenyl-alpha-D-maltoheptaoside + maltose
?
-
maltose as donor and acceptor, overview
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-
?
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
soluble starch + glycosyl acceptor
beta-cyclodextrin
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-
-
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r
soluble starch + glycosyl acceptor
cyclodextrins
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-
-
-
r
starch + glycosyl acceptor
cyclodextrin
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the cyclodextrin product specificity can be changed into linear product specificity, by introducing a five-residue insertion mutation at the donor substrate binding subsites. The CGTase mutants remain clearly different from the maltogenic alpha-amylase, as they have much lower hydrolytic activities, they form linear products of variable sizes and they retain a low cyclodextrin forming activity, whereas maltogenic alpha-amylases produce primarily maltose. The five-residue insertion, concomitantly, strongly enhances the exo-specificity of CGTase
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-
?
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
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-
-
r
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
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product ratios 43% alpha-cyclodextrin, 46% beta-cyclodextrin and 11% gamma-cyclodextrin
r
additional information
?
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the enzyme primarily catalyses the formation of cyclic alpha-1,4-linked cyclodextrins from starch. This enzyme also possesses unusually high hydrolytic activity as a side reaction, thought to be due to partial retention of ancestral enzyme function. Product formation, alpha-, beta-, and gamma-cyclodextrins, of wild-type and mutant enzymes, substrate-binding subsites of CGTase, and sugar binding structure, overview
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-
?
additional information
?
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-
CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview
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-
?
additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Thermoanaerobacterium thermosulfurigenes produces alpha- and beta-cyclodextrins
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?
additional information
?
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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 also shows high hydrolytic activity on potato starch
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-
?
additional information
?
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-
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
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-
?
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
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
?
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-
cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Thermoanaerobacterium thermosulfurigenes produces alpha- and beta-cyclodextrins
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.15
4,6-O-ethylidene-4-nitrophenyl alpha-D-maltoheptaoside
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pH 6.0, 60°C, wild-type enzyme
0.2
4,6-O-ethylidene-4-nitrophenyl alpha-D-maltoheptaoside
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pH 6.0, 60°C, mutant W239R
0.24
4,6-O-ethylidene-4-nitrophenyl alpha-D-maltoheptaoside
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pH 6.0, 60°C, mutant S77P
0.27
4,6-O-ethylidene-4-nitrophenyl alpha-D-maltoheptaoside
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pH 6.0, 60°C, mutant W239L
additional information
additional information
-
reaction kinetics
-
additional information
additional information
-
kinetics of the four reaction steps, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
558
4,6-O-ethylidene-4-nitrophenyl alpha-D-maltoheptaoside
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pH 6.0, 60°C, mutant S77P
644
4,6-O-ethylidene-4-nitrophenyl alpha-D-maltoheptaoside
-
pH 6.0, 60°C, mutant W239R
1082
4,6-O-ethylidene-4-nitrophenyl alpha-D-maltoheptaoside
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pH 6.0, 60°C, mutant W239L
1244
4,6-O-ethylidene-4-nitrophenyl alpha-D-maltoheptaoside
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pH 6.0, 60°C, wild-type enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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). CDGT_THETU
710
1
78417
Swiss-Prot
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PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant mutant S77P CGTase in 10 mM sodium acetate, pH 5.5, large crystals from 17-20%-saturated ammonium sulfate at room temperature in 100 mM HEPES, pH 7.6, or 100 mM HEPES, pH 7.8, or 100 mM Tris/HCl, pH 8.0, like the wild-type enzyme, crystals are soaked in 25% v/v glycerol and directly flash-cooled, or soaked in 2% w/v acarbose, 4% w/v maltohexaose and 25% glycerol in 20% saturated ammonium sulfate for 25 min followed by flash-cooling, X-ray diffraction structure determination and analysis at 1.6 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S77P
-
site-directed mutagenesis, mutant kinetics compared to the wild-type enzyme, molecular modelling of the location and effect of S77P mutation on the Tabium CGTase active-site conformation
W239L
-
site-directed mutagenesis, mutant kinetics compared to the wild-type enzyme, the mutation destroys a hydrogen-bonding interaction between the side chains of Asp209 and Trp239, compromising the stability of the mutant
W239R
-
site-directed mutagenesis, mutant kinetics compared to the wild-type enzyme, the mutation destroys a hydrogen-bonding interaction between the side chains of Asp209 and Trp239, compromising the stability of the mutant
additional information
additional information
-
engineering cyclodextrin glycosyltransferase into a starch hydrolase with a high exospecificity. the cyclodextrin product specificity can be changed into linear product specificity, by introducing a five-residue insertion mutation at the donor substrate binding subsites. The CGTase mutants remain clearly different from the maltogenic alpha-amylase, as they have much lower hydrolytic activities, they form linear products of variable sizes and they retain a low cyclodextrin forming activity, whereas maltogenic alpha-amylases produce primarily maltose. The five-residue insertion, concomitantly, strongly enhances the exo-specificity of CGTase
additional information
-
mutations in two residues, Ser-77 and Trp-239, on the outer region of the active site, lowers the hydrolytic activity up to 15fold with retention of cyclization activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant enzymes in Bacillus subtilis strain DB104A, subcloning in Escherichia coli strain MC1061
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phylogenetic analysis, expression in Bacillus subtilis strain DB104A
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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
synthesis
synthesis
thermostable, useful for industrial utilization
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
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
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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), Bacillus sp. (in: Bacteria) (P31746), Bacillus sp. (in: Bacteria) 1011, Brevibacterium sp., Brevibacterium sp. 9605, Geobacillus stearothermophilus, Geobacillus stearothermophilus (P31797), Klebsiella oxytoca, Klebsiella pneumoniae, Paenibacillus macerans, Paenibacillus macerans (P04830), Thermoanaerobacter sp., Thermoanaerobacterium thermosulfurigenes, Thermoanaerobacterium thermosulfurigenes (P26827), Thermococcus sp., Thermococcus sp. B1001
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
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
Leemhuis, H.; Kragh, K.M.; Dijkstra, B.W.; Dijkhuizen, L.
Engineering cyclodextrin glycosyltransferase into a starch hydrolase with a high exo-specificity
J. Biotechnol.
103
203-212
2003
Thermoanaerobacterium thermosulfurigenes
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
Kelly, R.M.; Leemhuis, H.; Rozeboom, H.J.; van Oosterwijk, N.; Dijkstra, B.W.; Dijkhuizen, L.
Elimination of competing hydrolysis and coupling side reactions of a cyclodextrin glucanotransferase by directed evolution
Biochem. J.
413
517-525
2008
Thermoanaerobacterium thermosulfurigenes, Thermoanaerobacterium thermosulfurigenes EM1
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
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