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Information on EC 3.2.1.155 - xyloglucan-specific exo-beta-1,4-glucanase and Organism(s) Acetivibrio thermocellus and UniProt Accession Q70DK5

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IUBMB Comments
The enzyme removes branched oligosaccharides, containing preferentially four glucoside residues in the main chain, from xyloglucan molecules in a processive manner after the initial endo-type attack on a polysaccharide [1-5]. Hydrolysis occurs at either the unsubstituted D-glucopyranose residue in the main backbone and/or the D-glucopyranose residue bearing a xylosyl group [1-5]. The enzyme does not display activity, or shows very low activity, towards other beta-D-glucans [1,2,4,5].
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Acetivibrio thermocellus
UNIPROT: Q70DK5
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The taxonomic range for the selected organisms is: Acetivibrio thermocellus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Hydrolysis of (1->4)-D-glucosidic linkages in xyloglucans so as to successively remove oligosaccharides from the chain end.
Synonyms
xyloglucanase xgh74a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
xyloglucanase Xgh74A
-
xyloglucanase Xgh74A
-
-
SYSTEMATIC NAME
IUBMB Comments
[(1->6)-alpha-D-xylo]-(1->4)-beta-D-glucan exo-glucohydrolase
The enzyme removes branched oligosaccharides, containing preferentially four glucoside residues in the main chain, from xyloglucan molecules in a processive manner after the initial endo-type attack on a polysaccharide [1-5]. Hydrolysis occurs at either the unsubstituted D-glucopyranose residue in the main backbone and/or the D-glucopyranose residue bearing a xylosyl group [1-5]. The enzyme does not display activity, or shows very low activity, towards other beta-D-glucans [1,2,4,5].
CAS REGISTRY NUMBER
COMMENTARY hide
1000598-79-7
-
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
beta-glucan + H2O
beta-glucan oligosaccharides
show the reaction diagram
8% of the activity with xyloglucan
-
-
?
carboxymethyl cellulose + H2O
carboxymethyl cellulose oligosaccharides
show the reaction diagram
5% of the activity with xyloglucan
-
-
?
xyloglucan + H2O
xyloglucan oligosaccharides
show the reaction diagram
the enzyme is a true endo-glucanase when it acts on linear substrates without bulky substituents in the polymer backbone. When the enzyme acts on polymeric substrate with bulky side chains, its mode of action is switched to exo-like
XXXG, XXLG and XLLG oligosaccharides
-
?
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
-
-
?
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
?
show the reaction diagram
Xgh74 contributes to the in vivo degradation of the hemicellulose xyloglucan and xylan by the cellulosome of Clostridium thermocellum
-
-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.4
hydrolysis of tamarind seed xyloglucan
6.4
hydrolysis of tamarid xyloglucan
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.7 - 7.8
more than 50% of maximal activity in the pH-range 5.7-7.8, hydrolysis of tamarind seed xyloglucan
5.7 - 7.8
50% of maximal activity at pH 5.7 and at pH 7.8
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
75
hydrolysis of tamarind seed xyloglucan
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
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?
XG74_ACETH
842
0
92393
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zverlov, V.V.; Schantz, N.; Schmitt-Kopplin, P.; Schwarz, W.H.
Two new major subunits in the cellulosome of Clostridium thermocellum: xyloglucanase Xgh74A and endoxylanase Xyn10D
Microbiology
151
3395-3401
2005
Acetivibrio thermocellus, Acetivibrio thermocellus (Q70DK5)
Manually annotated by BRENDA team