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Information on EC 3.2.1.151 - xyloglucan-specific endo-beta-1,4-glucanase and Organism(s) Aspergillus niger and UniProt Accession A1XP58

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IUBMB Comments
The enzyme from Aspergillus aculeatus is specific for xyloglucan and does not hydrolyse other cell-wall components. The reaction involves endohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan with retention of the beta-configuration of the glycosyl residues.
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This record set is specific for:
Aspergillus niger
UNIPROT: A1XP58
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The taxonomic range for the selected organisms is: Aspergillus niger
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
xyloglucanase, xyloglucan endotransglucosylase/hydrolases, endoxyloglucanase, xeg12a, xeg5a, mtxgh74, caxth1, cel74a, xeg74, xcxgha, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
endoxyloglucanase
-
-
-
-
GH12 xyloglucanase
-
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oligoxyloglucan hydrolase
-
-
-
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XEG
-
-
-
-
XG-ase
-
-
-
-
XH
-
-
-
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xyloglucan endo-beta-1,4-glucanase
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-
-
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xyloglucan endohydrolase
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-
-
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xyloglucan-specific endo 1,4-beta-glucanase
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-
-
-
xyloglucan-specific family 12 hydrolase
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xyloglucanase
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-
-
-
xyloglucanendohydrolase
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-
-
-
xyloglycan hydrolase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
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-
SYSTEMATIC NAME
IUBMB Comments
[(1->6)-alpha-D-xylo]-(1->4)-beta-D-glucan glucanohydrolase
The enzyme from Aspergillus aculeatus is specific for xyloglucan and does not hydrolyse other cell-wall components. The reaction involves endohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan with retention of the beta-configuration of the glycosyl residues.
CAS REGISTRY NUMBER
COMMENTARY hide
76901-10-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
carboxymethyl curdlan + H2O
carboxymethyl curdlan oligosaccharides
show the reaction diagram
-
less than 2% of the activity with xyloglucan
-
?
carboxymethyl pachyman + H2O
carboxymethyl pachyman oligosaccharides
show the reaction diagram
-
less than 2% of the activity with xyloglucan
-
?
xyloglucan + H2O
xyloglucan oligosaccharides
show the reaction diagram
substrate xyloglucan from tamarind seed, cleavage at unbranched glucose in the backbone
-
-
?
azo-cellulose + H2O
azo-cellulose oligosaccharides
show the reaction diagram
-
-
-
?
beta-glucan + H2O
beta-glucan oligosaccharides
show the reaction diagram
-
-
-
?
xyloglucan + H2O
?
show the reaction diagram
-
-
-
-
?
xyloglucan + H2O
xyloglucan oligosaccharides
show the reaction diagram
xyloglucan oligosaccharide + H2O
?
show the reaction diagram
-
diverse substrates, substrate specificity, overview
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-
?
additional information
?
-
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
xyloglucan + H2O
xyloglucan oligosaccharides
show the reaction diagram
additional information
?
-
involved in plant cell wall polysaccharide degradation
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.54
xyloglucan
-
pH 5.0, 50°C, substrate from pea seed
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
34
xyloglucan
50°C, pH 5.0
49
xyloglucan
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pH 5.0, 50°C, substrate from pea seed
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
83
50°C, pH 5.0
0.01
-
substrate: xyloglucan, pH 5.0, 70°C
0.02
-
substrate: xyloglucan, pH 5.0, 50°C
113
-
substrate pea seed xyloglucan
19
substrate: xyloglucan
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50 - 70
-
activity at 50°C is higher than activity at 50°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.1
calculated from amino acid sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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?
XGEA_ASPNG
241
0
25456
Swiss-Prot
Secretory Pathway (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23300
x * 23300, calculated, mature protein, x * 32000, SDS-PAGE
32000
x * 23300, calculated, mature protein, x * 32000, SDS-PAGE
90500
calculated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 23300, calculated, mature protein, x * 32000, SDS-PAGE
additional information
-
AnXEG12A structure homology modelling, overview. Catalytic residues are D100, E115, and E201, predicted substrate binding residues are W22, and W119, and residues that are predicted to influence substrate specificity in GH12 are xyloglucanases W7, V94, and G127. The SST insertion sequence is loacted at residues 130-132
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no glycoprotein
N-glycosylation site at N32 is not glycosylated
proteolytic modification
sequence contains a signal peptide of 15 amino acids
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
10% loss of activity after 145h at pH 4.5
55
80% loss of activity after 145h and 50% loss of activity after 48h at pH 4.5
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Aspergillus niger
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hasper, A.A.; Dekkers, E.; Van Mil, M.; Van de Vondervoort, P.J.I.; De Graaff, L.H.
EglC, a new endoglucanase from Aspergillus niger with major activity towards xyloglucan
Appl. Environ. Microbiol.
68
1556-1560
2002
Aspergillus niger (Q8TFP1)
Manually annotated by BRENDA team
Master, E.R.; Zheng, Y.; Storms, R.; Tsang, A.; Powlowski, J.
A xyloglucan-specific family 12 glycosyl hydrolase from Aspergillus niger: recombinant expression, purification and characterization
Biochem. J.
411
161-170
2008
Aspergillus niger (A1XP58), Aspergillus niger
Manually annotated by BRENDA team
Powlowski, J.; Mahajan, S.; Schapira, M.; Master, E.R.
Substrate recognition and hydrolysis by a fungal xyloglucan-specific family 12 hydrolase
Carbohydr. Res.
344
1175-1179
2009
Aspergillus niger
Manually annotated by BRENDA team
van den Brink, J.; van Muiswinkel, G.C.; Theelen, B.; Hinz, S.W.; de Vries, R.P.
Efficient plant biomass degradation by thermophilic fungus Myceliophthora heterothallica
Appl. Environ. Microbiol.
79
1316-1324
2013
Aspergillus niger, Thermothelomyces heterothallicus, Thermothelomyces heterothallicus CBS 202.75, Thermothelomyces heterothallicus CBS 663.74, Thermothelomyces thermophilus, Thermothelomyces thermophilus ATCC 424674, Trichoderma reesei
Manually annotated by BRENDA team