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Information on EC 3.2.1.54 - cyclomaltodextrinase

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EC Tree
IUBMB Comments
Also hydrolyses linear maltodextrin.
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This record set is specific for:
UNIPROT: Q8TZP8
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
cdase, cyclomaltodextrinase, tva ii, cyclodextrinase, maltodextrin glucosidase, alpha-amylase ii, cdase i-5, ra.04, tk1770, env cda13a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CD-hydrolyzing amylase
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CD-ase
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CDase
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cyclodextrinase
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cycloheptaglucanase
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cyclohexaglucanase
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cyclomaltodextrin dextrin-hydrolase
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Cyclomaltodextrin hydrolase, decycling
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
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PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
cyclomaltodextrin dextrin-hydrolase (decyclizing)
Also hydrolyses linear maltodextrin.
CAS REGISTRY NUMBER
COMMENTARY hide
37288-41-8
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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
beta-cyclodextrin + H2O
?
show the reaction diagram
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-
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?
maltoheptaose + H2O
?
show the reaction diagram
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?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.78 - 154
beta-cyclodextrin
9.07 - 9.77
maltoheptaose
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
199 - 382
beta-cyclodextrin
1.63 - 93.3
maltoheptaose
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.29 - 43.5
beta-cyclodextrin
0.17 - 10.3
maltoheptaose
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q8TZP8_PYRFU
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
645
0
76084
TrEMBL
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop method at 18°C. The structure studies supporting the proposition that cyclodextrin-hydrolyzing amylases from hyperthermophilic microorganisms contain all of the structural components required for substrate binding within a single monomer, distinguishing PFTA from the classical bacterial cyclodextrin-hydrolyzing enzymes of the GH13 family
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G415E
the mutant enzyme reveals considerable differences in substrate preference relative to the wild-type enzyme. Increased substrate selectivity of the mutant enzyme for the beta-cyclodextrin substrate, whereas the mutant shows no difference in activity for the maltoheptaose substrate
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
the G415E mutant is an excellent candidate for the industrial production of specific-length maltooligosaccharides from cyclodextrins
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Park, J.T.; Song, H.N.; Jung, T.Y.; Lee, M.H.; Park, S.G.; Woo, E.J.; Park, K.H.
A novel domain arrangement in a monomeric cyclodextrin-hydrolyzing enzyme from the hyperthermophile Pyrococcus furiosus
Biochim. Biophys. Acta
1834
380-386
2013
Pyrococcus furiosus (Q8TZP8)
Manually annotated by BRENDA team