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Information on EC 3.2.1.120 - oligoxyloglucan beta-glycosidase
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EC Tree
3.2.1.120 oligoxyloglucan beta-glycosidaseSpecify your search results
Word Map
- 3.2.1.120
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inventory
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psychotic-like
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self-experiences
- xyloglucans
- oligosaccharides
-
psychosis
-
schizophrenia
-
xylopyranosyl
-
emotional
- oligoxyloglucans
- biotechnology
-
consciousness
-
psychopathology
-
intelligence
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neurocognitive
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subscale
- cellobiose
- saccharides
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transglycosylation
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theorists
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non-reducing
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galactosylation
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
ipase, isoprimeverose-producing oligoxyloglucan hydrolase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EglC
-
-
-
-
family-74 xyloglucanase
-
-
-
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hydrolase, oligoxyloglucan
-
-
-
-
IPase
IpeA
isoprimeverose-producing oligoxyloglucan hydrolase
oligoxyloglucan hydrolase
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-
-
-
XEH
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-
-
-
XGH
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-
-
-
XTH
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-
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xyloglucan endohydrolase
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-
-
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xyloglucan endotransglucosylase/hydrolase
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-
-
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xyloglucan hydrolase
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xyloglucan-specific endo-beta-1,4-glucanase
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-
-
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IPase
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-
-
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isoprimeverose-producing oligoxyloglucan hydrolase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
R1-Glcbeta(1-4)Glcbeta[Xylbeta(1-6)Glcbeta(1-4)](1-4)Glcbeta(1-4)Glcbeta(1-4)-R2 + H2O = R1-Glcbeta(1-4)Glcbeta(1-4)Glcbeta(1-4)Glcbeta(1-4)-R2 + 6-O-beta-D-xylopyranosyl-beta-D-glucopyranose
R1-Glcbeta(1-4)Glcbeta[Xylbeta(1-6)Glcbeta(1-4)](1-4)Glcbeta(1-4)Glcbeta(1-4)-R2 + H2O = R1-Glcbeta(1-4)Glcbeta(1-4)Glcbeta(1-4)Glcbeta(1-4)-R2 + 6-O-beta-D-xylopyranosyl-beta-D-glucopyranose
mechanism
-
R1-Glcbeta(1-4)Glcbeta[Xylbeta(1-6)Glcbeta(1-4)](1-4)Glcbeta(1-4)Glcbeta(1-4)-R2 + H2O = R1-Glcbeta(1-4)Glcbeta(1-4)Glcbeta(1-4)Glcbeta(1-4)-R2 + 6-O-beta-D-xylopyranosyl-beta-D-glucopyranose
stereoselective cleavage of substrate
-
R1-Glcbeta(1-4)Glcbeta[Xylbeta(1-6)Glcbeta(1-4)](1-4)Glcbeta(1-4)Glcbeta(1-4)-R2 + H2O = R1-Glcbeta(1-4)Glcbeta(1-4)Glcbeta(1-4)Glcbeta(1-4)-R2 + 6-O-beta-D-xylopyranosyl-beta-D-glucopyranose
inverting mechanism
-
R1-Glcbeta(1-4)Glcbeta[Xylbeta(1-6)Glcbeta(1-4)](1-4)Glcbeta(1-4)Glcbeta(1-4)-R2 + H2O = R1-Glcbeta(1-4)Glcbeta(1-4)Glcbeta(1-4)Glcbeta(1-4)-R2 + 6-O-beta-D-xylopyranosyl-beta-D-glucopyranose
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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-
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SYSTEMATIC NAME
IUBMB Comments
oligoxyloglucan xyloglucohydrolase
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CAS REGISTRY NUMBER
COMMENTARY
97162-80-6
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(Xylbeta(1-6))Glcbeta(1-4)(Xylbeta(1-6))Glcbeta(1-4)Glc + H2O
beta-D-xylose + Xylbeta(1-6)Glcbeta(1-4)Glc
alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc + H2O
?
-
-
-
?
alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc + H2O
?
-
-
-
?
alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc + H2O
alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc + alpha-D-Xyl-(1->6)-beta-D-Glc
-
-
-
?
alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc + H2O
?
-
-
-
?
Xylbeta(1-6)Glcbeta(1-4)(Xylbeta(1-6))Glcbeta(1-4)(Xylbeta(1-6))Glcbeta(1-4)Glc + H2O
beta-D-xylose + (Xylbeta(1-6))Glcbeta(1-4)(Xylbeta(1-6))Glcbeta(1-4)Glc
Xylbeta(1-6)Glcbeta(1-4)(Xylbeta(1-6))Glcbeta(1-4)(Xylbeta(1-6))Glcbeta(1-4)Glc + isoprimeverose
Xylbeta(1-6)Glcbeta(1-4)(Xylbeta(1-6))Glcbeta(1-4)(Xylbeta(1-6))Glcbeta(1-4)(Xylbeta(1-6))Glcbeta(1-4)Glc
(Xylbeta(1-6))Glcbeta(1-4)(Xylbeta(1-6))Glcbeta(1-4)Glc + H2O
beta-D-xylose + Xylbeta(1-6)Glcbeta(1-4)Glc
-
-
-
-
?
(Xylbeta(1-6))Glcbeta(1-4)(Xylbeta(1-6))Glcbeta(1-4)Glc + H2O
beta-D-xylose + Xylbeta(1-6)Glcbeta(1-4)Glc
-
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactopyranose
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-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactopyranose
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-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
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-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
-
-
-
?
chemically modified cellulose + H2O
oligosaccharide + ?
-
best substrate
-
-
?
oligoxyloglucan + H2O
isoprimeverose + ?
the enzyme is involved in utilization of oligoxyloglucans as carbon sources
-
-
?
oligoxyloglucan + H2O
isoprimeverose + ?
the enzyme recognizes and releases isoprimeverose (alpha-D-xylopyranose-(1,6)-D-glucopyranose) units from the non-reducing ends of oligoxyloglucans. Xylopyranosyl-branching at the non-reducing ends was vital for IPase activity, and galactosylation at alpha-(1,6)-linked xylopyranosyl side chain completely abolishes activity. Hepta-oligoxyloglucan saccharide (Xyl3Glc4) substrate is preferred over tri-(Xyl1Glc2) and tetra-(Xyl2Glc2) oligoxyloglucan saccharides substrates. IpeA transfers isoprimeverose units to other saccharides, indicating transglycosylation activity
-
-
?
oligoxyloglucan + H2O
isoprimeverose + ?
the enzyme is involved in utilization of oligoxyloglucans as carbon sources
-
-
?
oligoxyloglucan + H2O
isoprimeverose + ?
the enzyme recognizes and releases isoprimeverose (alpha-D-xylopyranose-(1,6)-D-glucopyranose) units from the non-reducing ends of oligoxyloglucans. Xylopyranosyl-branching at the non-reducing ends was vital for IPase activity, and galactosylation at alpha-(1,6)-linked xylopyranosyl side chain completely abolishes activity. Hepta-oligoxyloglucan saccharide (Xyl3Glc4) substrate is preferred over tri-(Xyl1Glc2) and tetra-(Xyl2Glc2) oligoxyloglucan saccharides substrates. IpeA transfers isoprimeverose units to other saccharides, indicating transglycosylation activity
-
-
?
Xylbeta(1-6)Glcbeta(1-4)(Xylbeta(1-6))Glcbeta(1-4)(Xylbeta(1-6))Glcbeta(1-4)Glc + H2O
beta-D-xylose + (Xylbeta(1-6))Glcbeta(1-4)(Xylbeta(1-6))Glcbeta(1-4)Glc
-
-
-
-
?
Xylbeta(1-6)Glcbeta(1-4)(Xylbeta(1-6))Glcbeta(1-4)(Xylbeta(1-6))Glcbeta(1-4)Glc + H2O
beta-D-xylose + (Xylbeta(1-6))Glcbeta(1-4)(Xylbeta(1-6))Glcbeta(1-4)Glc
-
-
-
-
?
Xylbeta(1-6)Glcbeta(1-4)(Xylbeta(1-6))Glcbeta(1-4)(Xylbeta(1-6))Glcbeta(1-4)Glc + isoprimeverose
Xylbeta(1-6)Glcbeta(1-4)(Xylbeta(1-6))Glcbeta(1-4)(Xylbeta(1-6))Glcbeta(1-4)(Xylbeta(1-6))Glcbeta(1-4)Glc
-
-
-
-
?
Xylbeta(1-6)Glcbeta(1-4)(Xylbeta(1-6))Glcbeta(1-4)(Xylbeta(1-6))Glcbeta(1-4)Glc + isoprimeverose
Xylbeta(1-6)Glcbeta(1-4)(Xylbeta(1-6))Glcbeta(1-4)(Xylbeta(1-6))Glcbeta(1-4)(Xylbeta(1-6))Glcbeta(1-4)Glc
-
-
-
-
?
Xylbeta(1-6)Glcbeta(1-4)Glc + H2O
Xylbeta(1-6)Glc + beta-D-glucopyranose
-
-
-
-
?
Xylbeta(1-6)Glcbeta(1-4)Glc + H2O
Xylbeta(1-6)Glc + beta-D-glucopyranose
-
-
-
-
?
xyloglucan + H2O
isoprimeverose + ?
the combinations of beta-galactosidase LacA and isoprimeverose-producing oligoxyloglucan hydrolase IpeA is crucial for xyloglucan degradation. Specifically, the combination of LacA and IpeA is a key step in the degradation of xyloglucan oligosaccharides, because IpeA requires LacA for the removal of galactopyranosyl residues, which prevent IpeA activity, and LacA requires IpeA for the removal of isoprimeverose units, which interfere with the formation of the LacA-xyloglucan oligosaccharide complex
-
-
?
xyloglucan + H2O
isoprimeverose + ?
isoprimeverose-producing oligoxyloglucan hydrolase requires LacA for the removal of galactopyranosyl residues
-
-
?
xyloglucan + H2O
isoprimeverose + ?
the combinations of beta-galactosidase LacA and isoprimeverose-producing oligoxyloglucan hydrolase IpeA is crucial for xyloglucan degradation. Specifically, the combination of LacA and IpeA is a key step in the degradation of xyloglucan oligosaccharides, because IpeA requires LacA for the removal of galactopyranosyl residues, which prevent IpeA activity, and LacA requires IpeA for the removal of isoprimeverose units, which interfere with the formation of the LacA-xyloglucan oligosaccharide complex
-
-
?
xyloglucan + H2O
isoprimeverose + ?
isoprimeverose-producing oligoxyloglucan hydrolase requires LacA for the removal of galactopyranosyl residues
-
-
?
xyloglucan fragment oligosaccharide + H2O
isoprimeverose
-
highly specific for
isoprimeverose is split off from the nonreducing end of the backbone of the substrate
?
xyloglucan fragment oligosaccharide + H2O
isoprimeverose
-
specifically cleaves 1,4-beta-glucosyl-linkages
products are nona- and heptasaccharides
?
additional information
?
-
-
main roles of enzyme are wall restructuring and integration/wall assembly
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-
?
additional information
?
-
-
no substrate: carboxymethylcellulose, swollen cellulose
-
-
?
additional information
?
-
-
no substrate: carboxymethylcellulose, swollen cellulose
-
-
?
additional information
?
-
-
enzyme allows for use of cellulose as carbon source by breaking down surrounding cellulose fibrils
-
-
?
additional information
?
-
-
enzyme is capable of hydrolizing xyloglucans within the native cell wall architecture, thereby increasing the cell wall extensibility
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
xyloglucan fragment oligosaccharide + H2O
isoprimeverose
-
highly specific for
isoprimeverose is split off from the nonreducing end of the backbone of the substrate
?
oligoxyloglucan + H2O
isoprimeverose + ?
the enzyme is involved in utilization of oligoxyloglucans as carbon sources
-
-
?
oligoxyloglucan + H2O
isoprimeverose + ?
the enzyme is involved in utilization of oligoxyloglucans as carbon sources
-
-
?
xyloglucan + H2O
isoprimeverose + ?
the combinations of beta-galactosidase LacA and isoprimeverose-producing oligoxyloglucan hydrolase IpeA is crucial for xyloglucan degradation. Specifically, the combination of LacA and IpeA is a key step in the degradation of xyloglucan oligosaccharides, because IpeA requires LacA for the removal of galactopyranosyl residues, which prevent IpeA activity, and LacA requires IpeA for the removal of isoprimeverose units, which interfere with the formation of the LacA-xyloglucan oligosaccharide complex
-
-
?
xyloglucan + H2O
isoprimeverose + ?
the combinations of beta-galactosidase LacA and isoprimeverose-producing oligoxyloglucan hydrolase IpeA is crucial for xyloglucan degradation. Specifically, the combination of LacA and IpeA is a key step in the degradation of xyloglucan oligosaccharides, because IpeA requires LacA for the removal of galactopyranosyl residues, which prevent IpeA activity, and LacA requires IpeA for the removal of isoprimeverose units, which interfere with the formation of the LacA-xyloglucan oligosaccharide complex
-
-
?
additional information
?
-
-
main roles of enzyme are wall restructuring and integration/wall assembly
-
-
?
additional information
?
-
-
enzyme allows for use of cellulose as carbon source by breaking down surrounding cellulose fibrils
-
-
?
additional information
?
-
-
enzyme is capable of hydrolizing xyloglucans within the native cell wall architecture, thereby increasing the cell wall extensibility
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.79
alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc
pH 4.5, 60°C
2.35
alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc
pH 4.5, 60°C
0.7
Xylbeta(1-6)Glcbeta(1-4)(Xylbeta(1-6))Glcbeta(1-4)(Xylbeta(1-6))Glcbeta(1-4)Glc
-
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1216
alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc
pH 4.5, 60°C
661
alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc
pH 4.5, 60°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
678
alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc
pH 4.5, 60°C
282
alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc
pH 4.5, 60°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.32
substrate: 4-nitrophenyl beta-D-galactopyranoside, pH 4.5, 60°C
296
substrate: alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc, pH 4.5, 60°C
297
substrate: alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[beta-D-Gal-(1->2)-alpha-D-Xyl-(1->6)]-beta-D-Glc, pH 4.5, 60°C
422
substrate: alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc, pH 4.5, 60°C
427
substrate: alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glcol, pH 4.5, 60°C
85
-
with Xylbeta(1-6)Glcbeta(1-4)(Xylbeta(1-6))Glcbeta(1-4)(Xylbeta(1-6))Glcbeta(1-4)Glc
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
the combinations of beta-galactosidase LacA and isoprimeverose-producing oligoxyloglucan hydrolase IpeA is crucial for xyloglucan degradation. Specifically, the combination of LacA and IpeA is a key step in the degradation of xyloglucan oligosaccharides, because IpeA requires LacA for the removal of galactopyranosyl residues, which prevent IpeA activity, and LacA requires IpeA for the removal of isoprimeverose units, which interfere with the formation of the LacA-xyloglucan oligosaccharide complex
physiological function
the enzyme is involved in utilization of oligoxyloglucans as carbon sources
physiological function
-
the combinations of beta-galactosidase LacA and isoprimeverose-producing oligoxyloglucan hydrolase IpeA is crucial for xyloglucan degradation. Specifically, the combination of LacA and IpeA is a key step in the degradation of xyloglucan oligosaccharides, because IpeA requires LacA for the removal of galactopyranosyl residues, which prevent IpeA activity, and LacA requires IpeA for the removal of isoprimeverose units, which interfere with the formation of the LacA-xyloglucan oligosaccharide complex
-
physiological function
-
the enzyme is involved in utilization of oligoxyloglucans as carbon sources
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A2H4P699_FAGTA
504
1
56782
TrEMBL
Secretory Pathway (Reliability: 1)
Q2U8V9_ASPOR
Aspergillus oryzae (strain ATCC 42149 / RIB 40)
779
0
85095
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23600
-
x * 23600, mass spectroscopy, x * 34000, SDS-PAGE, x * 23760, deduced from gene sequence
23760
-
x * 23600, mass spectroscopy, x * 34000, SDS-PAGE, x * 23760, deduced from gene sequence
34000
-
x * 23600, mass spectroscopy, x * 34000, SDS-PAGE, x * 23760, deduced from gene sequence
79440
-
x * 79440, mass spectroscopy, x * 79480, deduced from gene sequence
79480
-
x * 79440, mass spectroscopy, x * 79480, deduced from gene sequence
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 23600, mass spectroscopy, x * 34000, SDS-PAGE, x * 23760, deduced from gene sequence
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
55
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is expressed in xylose and xyloglucan media and is strongly induced in the presence of xyloglucan endo-xyloglucanase-hydrolyzed products
the enzyme is expressed in xylose and xyloglucan media and is strongly induced in the presence of xyloglucan endo-xyloglucanase-hydrolyzed products
the enzyme is expressed in xylose and xyloglucan media and is strongly induced in the presence of xyloglucan endo-xyloglucanase-hydrolyzed products
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
biotechnology
-
use of fungal and plant enzyme during liquefaction of raw and blanched apple
biotechnology
Malus malus
-
use of fungal and plant enzyme during liquefaction of raw and blanched apple
biotechnology
-
method for rapidly identifying six of the most commonly found xyloglucan oligosaccharide units using purified enzyme
biotechnology
-
method for rapidly identifying six of the most commonly found xyloglucan oligosaccharide units using purified enzyme
-
biotechnology
-
method for rapidly identifying six of the most commonly found xyloglucan oligosaccharide units using purified enzyme
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rose, J.K.C.; Braam, J.; Fry, S.C.; Nishitani, K.
The XTH family of enzymes involved in xyloglucan endotransglucosylation and endohydrolysis: Current perspectives and a new unifying nomenclature
Plant Cell Physiol.
43
1421-1435
2002
Arabidopsis thaliana
brenda
Kato, Y.; Matsushita, J.; Kubodera, T.; Matsuda, K.
A novel enzyme producing isoprimeverose from oligoxyloglucans of Aspergillus oryzae
J. Biochem.
97
801-810
1985
Aspergillus oryzae
brenda
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
brenda
Matsumoto, T.; Sakai, F.; Hayashi, T.
A xyloglucan-specific endo-1,4-beta-glucanase isolated from auxin-treated pea stems
Plant Physiol.
114
661-667
1997
Pisum sativum
brenda
Kaku, T.; Tabuchi, A.; Wakabayashi, K.; Kamisaka, S.; Hoson, T.
Action of xyloglucan hydrolase within the native cell wall architecture and its effect on cell wall extensibility in azuki bean epicotyls
Plant Cell Physiol.
43
21-26
2002
Vigna angularis
brenda
Irwin, D.C.; Cheng, M.; Xiang, B.; Rose, J.K.C.; Wilson, D.B.
Cloning, expression and characterization of a family-74 xyloglucanase from Thermobifida fusca
Eur. J. Biochem.
270
3083-3091
2003
Thermobifida fusca
brenda
Vincken, J.P.; van den Broek, L.A.M.; van der Lei, D.D.; Beldman, G.; Voragen, A.G.J.
Fungal and plant xyloglucanases may act in concert during liquefaction of apples
J. Sci. Food Agric.
73
407-416
1997
Malus malus, Trichoderma viride
brenda
Tabuchi, A.; Kamisaka, S.; Hoson, T.
Purification of xyloglucan hydrolase/endotransferase from cell walls of azuki bean epicotyls
Plant Cell Physiol.
38
653-658
1997
Vigna angularis
-
brenda
Pauly, M.; Andersen, L.N.; Kauppinen, S.; Kofod, L.V.; York, W.S.; Albersheim, P.; Darvill, A.
A xyloglucan-specific endo-beta-1,4-glucanase from Aspergillus aculeatus: expression cloning in yeast, purification and characterization of the recombinant enzyme
Glycobiology
9
93-100
1999
Aspergillus aculeatus
brenda
Konishi, T.; Mitsuishi, Y.; Kato, Y.
Analysis of the oligosaccharide units of xyloglucans by digestion with isoprimeverose-producing oligoxyloglucan hydrolase followed by anion-exchange chromatography
Biosci. Biotechnol. Biochem.
62
2421-2424
1998
Penicillium sp., Penicillium sp. M451, Penicillium sp. M9
brenda
Yaoi, K.; Hiyoshi, A.; Mitsuishi, Y.
Screening, purification and characterization of a prokaryotic isoprimeverose-producing oligoxyloglucan hydrolase from Oerskovia sp. Y1
J. Appl. Glycosci.
54
91-94
2007
Oerskovia sp., Oerskovia sp. Y1
-
brenda
Matsuzawa, T.; Watanabe, M.; Kameda, T.; Kameyama, A.; Yaoi, K.
Cooperation between beta-galactosidase and an isoprimeverose-producing oligoxyloglucan hydrolase is key for xyloglucan degradation in Aspergillus oryzae
FEBS J.
286
3182-3193
2019
Aspergillus oryzae (Q2U8V9), Aspergillus oryzae ATCC 42149 (Q2U8V9)
brenda
Matsuzawa, T.; Mitsuishi, Y.; Kameyama, A.; Yaoi, K.
Identification of the gene encoding isoprimeverose-producing oligoxyloglucan hydrolase in Aspergillus oryzae
J. Biol. Chem.
291
5080-5087
2016
Aspergillus oryzae (Q2U8V9), Aspergillus oryzae, Aspergillus oryzae ATCC 42149 (Q2U8V9)
brenda
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Release 2023.1 (January 2023)
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