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Information on EC 2.4.1.19 - cyclomaltodextrin glucanotransferase and Organism(s) Evansella clarkii and UniProt Accession Q8L3E0

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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:
Evansella clarkii
UNIPROT: Q8L3E0
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The taxonomic range for the selected organisms is: Evansella clarkii
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha-1,4-glucan 4-glycosyltransferase, cyclizing
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alpha-cyclodextrin glucanotransferase
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alpha-cyclodextrin glycosyltransferase
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Bacillus macerans amylase
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beta-cyclodextrin glucanotransferase
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beta-cyclodextrin glycosyltransferase
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BMA
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CGTase
cyclodextrin glucanotransferase
cyclodextrin glycosyltransferase
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cyclomaltodextrin glucotransferase
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cyclomaltodextrin glycosyltransferase
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gamma-cyclodextrin glycosyltransferase
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konchizaimu
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neutral-cyclodextrin glycosyltransferase
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additional information
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CGTases are members of the largest family of glycoside hydrolases acting on starch and related alpha-glucans, glycoside hydrolase family 13
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cyclization
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hydrolysis
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transglycosylation
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hexosyl group transfer
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PATHWAY SOURCE
PATHWAYS
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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 hide
9030-09-5
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
starch
gamma-cyclodextrin
show the reaction diagram
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?
additional information
?
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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
additional information
?
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cyclodextrin glucanotransferases produce a mixture of cyclic alpha-(1,4)-linked oligosaccharides, cyclodextrins, from starch. The enzyme from Bacillus clarkii produces 80% gamma-cyclodextrins with an overall conversion of starch into cyclodextrins of 14%
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
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around, wild-type enzyme and mutant enzymes A223H, A223R and A223K, gamma-cyclodextrin-forming activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q8L3E0_9BACI
702
0
78332
TrEMBL
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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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
hanging-drop vapour-diffusion method at 293 K. X-ray diffraction data are collected to 2.2 A. The crystal belongs to space group R3, with unit-cell parameters a = b = 211.6, c = 52.7 A
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A223H
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mutant snzyme shows slight decreases in gamma-cyclodextrin-forming activity at pH 10.0, but shows 2fold increases at pH 7.5. pH activity profiles of the mutant shows higher activity at neutral pHs (pH 6-9) than that of the wild type CGTase
A223K
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mutant enzyme shows slight decreases in gamma-cyclodextrin-forming activity at pH 10.0, but shows 3fold increases at pH 7.5. pH activity profiles of the mutant show higher activity at neutral pHs (pH 6-9) than that of the wild type CGTase
A223R
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mutant enzyme shows a 4fold increase in gamma-cycodextrin-forming activity at pH 7.5 and 1.5fold increase in activity at pH 10.0. Mutant enzyme shows higher activity in pH range pH 6-10.5
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
the enzyme can be applied in biotechnology for the production of cyclodextrins and oligosaccharides with novel properties
industry
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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
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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
Akita, M.; Hatada, Y.; Hidaka, Y.; Ohta, Y.; Takada, M.; Nakagawa, Y.; Ogawa, K.; Nakakuki, T.; Ito, S.; Horikoshi, K.
Crystallization and preliminary X-ray study of gamma-type cyclodextrin glycosyltransferase from Bacillus clarkii
Acta Crystallogr. Sect. D
60
586-587
2004
Evansella clarkii
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Nakagawa, Y.; Takada, M.; Ogawa, K.; Hatada, Y.; Horikoshi, K.
Site-directed mutations in alanine 223 and glycine 255 in the acceptor site of gamma-cyclodextrin glucanotransferase from alkalophilic Bacillus clarkii 7364 affect cyclodextrin production
J. Biochem.
140
329-336
2006
Evansella clarkii, Evansella clarkii 7364
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
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
Manually annotated by BRENDA team