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Information on EC 3.2.1.151 - xyloglucan-specific endo-beta-1,4-glucanase and Organism(s) Aspergillus aculeatus and UniProt Accession O94218

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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 aculeatus
UNIPROT: O94218
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The taxonomic range for the selected organisms is: Aspergillus aculeatus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
xyloglucanase, xyloglucan endotransglucosylase/hydrolases, endoxyloglucanase, xeg12a, xeg5a, mtxgh74, caxth1, xeg74, cel74a, xcxgha, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
endoxyloglucanase
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oligoxyloglucan hydrolase
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XG-ase
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XH
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xyloglucan endo-beta-1,4-glucanase
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xyloglucan endohydrolase
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xyloglucan-specific endo 1,4-beta-glucanase
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xyloglucan-specific endo-beta-1,4-glucanase
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xyloglucanase
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xyloglucanendohydrolase
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xyloglycan hydrolase
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additional information
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XEG is a glycohydrolase GH12 family endo-glucanase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
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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
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SUBSTRATE
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
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?
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
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Humulus lupulus xyloglucan-specific endoglucanase inhibitor proteins
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XEGIPs, the inhibitor proteins act specifically against the members of fungal glycoside hydrolase family 12, three homologues: HlXEGIP1 causes 85% inhibition at 0.03 mg, HlXEGIP2 95%, but HlXEGIP3 is inactive. Physiological function and enzyme interaction of the xyloglucan-specific endoglucanase inhibitor proteins, cloning and phylogenetic as well as expression analysis in hop, overview
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xyloglucan-specific endo-beta-1,4-glucanase inhibitor proteins
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XEGIPs, e.g. from tomato, carrot, or tobacco, inhibhition by formation of tight complexes
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additional information
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no inhibition by gamma-conglutin from Lupinus albus, although it exhibits high structural similarity to xyloglucan-specific endo-beta-1,4-glucanase inhibitor proteins, overview
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.6
xyloglucan
pH 5, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
113
xyloglucan
from tamarind, pH 5, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.4
pH gradient 3.5-9.5
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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the enzyme belongs to the glycoside hydrolase family 12, GH12
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
XGEA_ASPAC
238
0
25159
Swiss-Prot
Secretory Pathway (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23600
mass spectrometry
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 3.8
optimally stable, stability declines sharply below pH 2.8 and above pH 5
646677
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
optimally stable below
50
80% loss of activity after 2h
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (O94218), Aspergillus aculeatus
Manually annotated by BRENDA team
Scarafoni, A.; Ronchi, A.; Duranti, M.
gamma-Conglutin, the Lupinus albus XEGIP-like protein, whose expression is elicited by chitosan, lacks of the typical inhibitory activity against GH12 endo-glucanases
Phytochemistry
71
142-148
2010
Aspergillus aculeatus
Manually annotated by BRENDA team
Habrylo, O.; Forster, A.; Jeltsch, J.M.; Phalip, V.
The characterisation of xyloglucanase inhibitors from Humulus lupulus
Phytochemistry
90
70-77
2013
Aspergillus aculeatus
Manually annotated by BRENDA team