Information on EC 3.2.1.155 - xyloglucan-specific exo-beta-1,4-glucanase

for references in articles please use BRENDA:EC3.2.1.155
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.2.1.155
-
RECOMMENDED NAME
GeneOntology No.
xyloglucan-specific exo-beta-1,4-glucanase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of (1->4)-D-glucosidic linkages in xyloglucans so as to successively remove oligosaccharides from the chain end.
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
xyloglucan degradation II (exoglucanase)
-
-
SYSTEMATIC NAME
IUBMB Comments
[(1->6)-alpha-D-xylo]-(1->4)-beta-D-glucan exo-glucohydrolase
The enzyme removes XXXG heptasaccharides, XXLG/XLXG octasaccharides and XLLG nonasaccharides from the end of tamarind seed xyloglucan polymers in a processive manner. Hydrolysis occurs at the unsubstituted D-glucopyranose residue in the main backbone. It is not known whether the cleavage takes place at the reducing or non-reducing end of the polymer. Very low activity with beta-D-glucans. The enzyme from Chrysosporium lucknowense shifts to an endoglucanase mode when acting on linear substrates without bulky substituents on the polymeric backbone such as barley beta-glucan.
CAS REGISTRY NUMBER
COMMENTARY hide
1000598-79-7
-
76901-10-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl xyloglucan derivatives + H2O
oligosaccharides
show the reaction diagram
artificial substrate
-
-
?
beta-glucan + H2O
beta-glucan oligosaccharides
show the reaction diagram
carboxymethyl cellulose + H2O
carboxymethyl cellulose oligosaccharides
show the reaction diagram
tamarind xyloglucan + H2O
oligosaccharides
show the reaction diagram
highly specific for, exo-type reaction
with end products XXXG, XXLG/XLXG, and XLLG
-
?
tamarind xyloglucan + H2O
oligosacchrides
show the reaction diagram
XXXGXXXG + H2O
XXX + XXXG + GXXXG
show the reaction diagram
-
-
-
?
xyloglucan + H2O
?
show the reaction diagram
Xgh74 contributes to the in vivo degradation of the hemicellulose xyloglucan and xylan by the cellulosome of Clostridium thermocellum
-
-
?
xyloglucan + H2O
cellotetraose
show the reaction diagram
tamarind xyloglucan. Xgh74A hydrolyzes every fourth beta-1,4-glucan bond in the xyloglucan backbone, thus producing decorated cellotetraose units
-
-
?
xyloglucan + H2O
xyloglucan oligosaccharides
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
xyloglucan + H2O
?
show the reaction diagram
Q70DK5
Xgh74 contributes to the in vivo degradation of the hemicellulose xyloglucan and xylan by the cellulosome of Clostridium thermocellum
-
-
?
xyloglucan + H2O
xyloglucan oligosaccharides
show the reaction diagram
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12 - 30
beta-Glucan
46
carboxymethylcellulose
-
-
3 - 99
xyloglucan
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.4
hydrolysis of tamarid xyloglucan; hydrolysis of tamarind seed xyloglucan
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.3 - 6.9
more than 50% of maximal activity in the pH-range 4.5-7.2
4.5 - 7.2
-
more than 50% of maximal activity in the pH-range 4.5-7.2
5.7 - 7.8
50% of maximal activity at pH 5.7 and at pH 7.8; more than 50% of maximal activity in the pH-range 5.7-7.8, hydrolysis of tamarind seed xyloglucan
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
75
; hydrolysis of tamarind seed xyloglucan
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.8
-
isoelectric focusing
3.8
-
isoelectric focusing; isoelectrofocusing
4.1 - 4.3
isoelectric focusing, several enzyme forms; isoelectrofocusing, there may be different forms of the enzyme resulting from O-glycosylation
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
-
x * 32000, SDS-PAGE
78000
-
x * 78000, SDS-PAGE
105000
x * 105000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
peptide fingerprinting
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
2 putative N-glycosylation sites in Cel74A; enzyme contains two putative N-glycosylation sites. There may be different forms of the enzyme resulting from O-glycosylation
additional information
Cel74A contains a signal peptide
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
40°C, stable for at least 24 h
658199
5 - 7.5
stable
667262
5
40°C, stable for at least 24 h
658199
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
stable up to
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by ion exchange chromatography, to homogeneity
-
further purification of the commercial preparation, by ion exchange chromatography, to homogeneity
recombinant
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis