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Information on EC 2.4.1.19 - cyclomaltodextrin glucanotransferase and Organism(s) Bacillus ohbensis and UniProt Accession P27036

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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:
Bacillus ohbensis
UNIPROT: P27036
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Word Map
The taxonomic range for the selected organisms is: Bacillus ohbensis
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
cyclodextrin glycosyltransferase, cyclodextrin glucanotransferase, cyclomaltodextrin glucanotransferase, alpha-cgtase, beta-cgtase, toruzyme, cyclodextrin glucosyltransferase, alpha-cyclodextrin glycosyltransferase, cyclodextrin-glycosyltransferase, cyclodextrin glycosyl transferase, more
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
soluble starch + glycosyl acceptor
alpha-cyclodextrin + beta cyclodextrin + gamma-cyclodextrin
show the reaction diagram
soluble starch + glycosyl acceptor
beta-cyclodextrin
show the reaction diagram
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r
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 obhensis produces beta-cyclodextrins
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?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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?
CDGT_BACOH
704
1
78621
Swiss-Prot
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9.5
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stable at 55°C
488839
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned and expressed in Escherichia coli
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nucleotide sequence determined
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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
Akimaru, K.; Yagi, T.; Yamamoto, S.
Purification and properties of Bacillus coagulans cyclomaltodextrin glucanotransferase
J. Ferment. Bioeng.
71
322-328
1991
Geobacillus stearothermophilus, Niallia circulans, Weizmannia coagulans, Priestia megaterium, Bacillus subtilis, Paenibacillus macerans, Bacillus ohbensis, Bacillus sp. (in: Bacteria), Klebsiella oxytoca, Klebsiella pneumoniae, Geobacillus stearothermophilus TC-60, Bacillus subtilis 313
-
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
Geobacillus stearothermophilus, Alkalihalobacillus alcalophilus, Niallia circulans, Priestia megaterium, Paenibacillus macerans, Bacillus ohbensis, Klebsiella pneumoniae, Micrococcus sp., Niallia circulans E 192, Niallia circulans 8
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
Geobacillus stearothermophilus, Niallia circulans, Bacillus licheniformis, Paenibacillus macerans, Bacillus ohbensis, Bacillus sp. (in: Bacteria), Klebsiella pneumoniae, Bacillus sp. (in: Bacteria) 1011, Bacillus sp. (in: Bacteria) 17-1, Bacillus sp. (in: Bacteria) B1018
Manually annotated by BRENDA team
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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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
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
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
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