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Information on EC 3.2.1.11 - dextranase and Organism(s) Talaromyces minioluteus and UniProt Accession P48845

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EC Tree
     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.11 dextranase
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This record set is specific for:
Talaromyces minioluteus
UNIPROT: P48845 not found.
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Word Map
The taxonomic range for the selected organisms is: Talaromyces minioluteus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
dextranase, endodextranase, endo-dextranase, extracellular dextranase, aodex, alpha-glucanase, dex410, tpdex, smdex, dex49a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Alpha-1,6-glucan-6-glucanohydrolase
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-
-
-
alpha-D-1,6-glucan-6-glucanohydrolase
-
-
-
-
dextran hydrolase
-
-
-
-
dextranase DL 2
-
-
-
-
DL 2
-
-
-
-
endo-dextranase
-
-
-
-
endodextranase
-
-
-
-
rDex
-
recombinant dextranase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
6-alpha-D-glucan 6-glucanohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
9025-70-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dextran + H2O
fragments of dextran
show the reaction diagram
-
-
-
?
(4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-sindacene-3-propionic acid, succinimidyl ester)-quenched dextran + H2O
?
show the reaction diagram
-
-
-
?
dextran + H2O
fragments of dextran
show the reaction diagram
-
-
-
-
?
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
dextran + H2O
fragments of dextran
show the reaction diagram
-
-
-
?
dextran + H2O
fragments of dextran
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
aflatoxin B1
inhibits dextranase activities of CYP3A4-expressing cultures, maximum inhibition of 22% at 2 microg/ml. Only negligibly inhibits strain INVSC1 expressing dextranase
aflatoxin G1
substantially less inhibitory towards dextranase activities of CYP3A4-expressing cultures than aflatoxin B1, showing a maximum inhibition of about 12% at 2 microg/ml, whereas strain INVSC1 expressing dextranase is only marginally inhibited
T-2 toxin
100% inhibition at 10 microg/ml of dextranase activities of CYP3A4-expressing cultures and strain INVSC1
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
950 - 1000
-
recombinant dextranase
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 6
-
approx. 50% of maximal activity at pH 6.3, complete loss of activity above pH 7.5
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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?
DEXT_TALMI
608
0
65961
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
67000
x * 67000, SDS-PAGE
66000
-
1 * 66000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 67000, SDS-PAGE
monomer
-
1 * 66000
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
glycosylation sites at N5, N537 and N540
glycoprotein
additional information
-
rDEX has 2 disulphide bridges
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of apo-Dex49A and Dex49A complexed with product at 1.8 A and 1.65 A, respectively
crystallization of selenomethionyl-rDEX
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N5A/N537A/N540A
glycosylation-free mutant of Dex49A
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
50% loss of activity after 7.6 h
60
-
thermal denaturation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant and native dextranase
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Pichia pastoris
expressed in Saccharomyces cerevisiae INVSc1 via fusion of the DNA segment encoding the mature dextranase protein with alpha-factor signal sequence, and insertion into the GAL1-controlled expression vector pYES2/CT (construction of the four dextranase-expressing plasmids pYES2/CT-dex, pYES2/CT-dex-tag, pYES2/CT-alphaF-dex(m) and pYES2/CT-alphaF-dex(m)-tag). Dextranase construct pYESCT2-alphaF-dex(m) introduced into a strain of Saccharomyces cerevisiae expressing the human cytochrome P4503A4 (CYP3A4) and the cognate reductase
expression in Pichia pastoris
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Beldarrain, A.; Acosta, N.; Betancourt, L.; Gonzalez, L.J.; Pons, T.
Enzymic, spectroscopic and calorimetric studies of a recombinant dextranase expressed in Pichia pastoris
Biotechnol. Appl. Biochem.
38
211-221
2003
Talaromyces minioluteus
Manually annotated by BRENDA team
Betancourt, L.H.; Garcia, R.; Gonzalez, J.; Montesino, R.; Quintero, O.; Takao, T.; Shimonishi, Y.; Cremata, J.A.
Dextranase (alpha-1,6 glucan-6-glucanohydrolase) from Penicillium minioluteum expressed in Pichia pastoris: two host cells with minor differences in N-glycosylation
FEMS Yeast Res.
1
151-160
2001
Talaromyces minioluteus
Manually annotated by BRENDA team
Larsson, A.M.; Andersson, R.; Stahlberg, J.; Kenne, L.; Jones, T.A.
Dextranase from Penicillium minioluteum: reaction course, crystal structure, and product complex
Structure
11
1111-1121
2003
Talaromyces minioluteus (P48845), Talaromyces minioluteus
Manually annotated by BRENDA team
Li, X.; Millson, S.H.; Coker, R.D.; Evans, I.H.
Cloning and expression of Penicillium minioluteum dextranase in Saccharomyces cerevisiae and its exploitation as a reporter in the detection of mycotoxins
Biotechnol. Lett.
28
1955-1964
2006
Talaromyces minioluteus (Q27JJ3), Talaromyces minioluteus, Talaromyces minioluteus IMI068219 (Q27JJ3)
Manually annotated by BRENDA team