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Information on EC 3.2.1.54 - cyclomaltodextrinase and Organism(s) Flavobacterium sp. 92 and UniProt Accession Q8KKG0

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EC Tree
IUBMB Comments
Also hydrolyses linear maltodextrin.
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This record set is specific for:
Flavobacterium sp. 92
UNIPROT: Q8KKG0
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The taxonomic range for the selected organisms is: Flavobacterium sp. 92
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, lscda13, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CD-ase
-
-
-
-
CDase
-
-
-
-
cyclodextrinase
-
-
-
-
cycloheptaglucanase
-
-
-
-
cyclohexaglucanase
-
-
-
-
cyclomaltodextrin dextrin-hydrolase
-
-
-
-
Cyclomaltodextrin hydrolase, decycling
-
-
-
-
cyclomaltodextrinase
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
cyclomaltodextrin dextrin-hydrolase (decyclizing)
Also hydrolyses linear maltodextrin.
CAS REGISTRY NUMBER
COMMENTARY hide
37288-41-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-cyclodextrin + H2O
?
show the reaction diagram
-
-
-
?
beta-cyclodextrin + H2O
?
show the reaction diagram
-
-
-
?
gamma-cyclodextrin + H2O
?
show the reaction diagram
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.1
alpha-cyclodextrin
wild-type
2.9
beta-cyclodextrin
wild-type
2.2
gamma-cyclodextrin
wild-type
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
40.9
alpha-cyclodextrin
wild-type
26.5
beta-cyclodextrin
wild-type
17.4
gamma-cyclodextrin
wild-type
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36.1
wild-type, alpha-cyclodextrin
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q8KKG0_9FLAO
619
0
70029
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
132000
mutant enzyme T49P
138000
double mutant T49P-G523R
182000
mutant enzyme G523R
209000
wild-type, size-exclusion chromatography
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
a loose dimer of tight dimers
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant E340Q alpha-cyclodextrin complex, 0.1 M HEPES, 3.8 M NaCl, 3 mM CaCl2, pH 7.5, vapor diffusion, hanging drop, temperature 20°C, X-ray diffraction structure determination and analysis at 2.65 A resolution, space group H 3 2, T79P contact mutant, 0.1 M Tris, 17% PEG1500, pH 8.75, vapor diffusion, hanging drop, temperature 20°C, X-ray diffraction structure determination and analysis at 1.71 A resolution, space group P 21 21 2, mutant T49P, E340Q alpha-cyclodextrin complex, 0.1 M Tris, 17% PEG1500, pH 8.75, vapor diffusion, hanging drop, temperature 20°C, X-ray diffraction structure determination and analysis at 1.65 A resolution, space group P 21 21 2, mutant T49P, E340Q beta-cyclodextrin complex, resolution 1.69 A, mutant T49P, E340Q gamma-cyclodextrin complex, resolution 1.77 A
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E340Q
The active center mutant E340Q yields as much purified protein as the wild-type, and shows a residual, though very low, activity for alpha-cyclomaltodextrinase as derived from the crystal structure analysis
G523R
molucular weight 182000, does not show a clear dimer mass
R464A
Arg464 is suggested to chaperone the substrates to the active center of the same enzyme subunit
R464S
Arg464 is suggested to chaperone the substrates to the active center of the same enzyme subunit
T49P
molucular weight 132000, mutant T49P, which causes the dissociation of the tetrameric wild-type FspCMD to the tight dimers, reduces the activity to less than 50% with a particularly strong reduction for beta-cyclomaltodextrinase and gamma-cyclomaltodextrinase
additional information
the double mutant T49P-G523R does not show a clear monomer mass
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ion-exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21 (DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Buedenbender, S.; Schulz, G.E.
Structural base for enzymatic cyclodextrin hydrolysis
J. Mol. Biol.
385
606-617
2009
Flavobacterium sp. 92 (Q8KKG0)
Manually annotated by BRENDA team