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Information on EC 3.2.1.177 - alpha-D-xyloside xylohydrolase and Organism(s) Saccharolobus solfataricus and UniProt Accession Q9P999
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3.2.1.177 alpha-D-xyloside xylohydrolaseIUBMB Comments
The enzyme catalyses hydrolysis of a terminal, unsubstituted xyloside at the extreme reducing end of a xylogluco-oligosaccharide. Representative alpha-xylosidases from glycoside hydrolase family 31 utilize a two-step (double-displacement) mechanism involving a covalent glycosyl-enzyme intermediate, and retain the anomeric configuration of the product.
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Word Map
- 3.2.1.177
- xyloglucan
- oligosaccharides
- xxxg
- isoprimeverose
- beta-glucosidase
- apoplastic
- heptasaccharide
- nasturtium
-
oligosaccharide-specific
- majus
- alpha-glucosides
-
tropaeolum
- cello-oligosaccharides
- synthesis
- biotechnology
The taxonomic range for the selected organisms is: Saccharolobus solfataricus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Hydrolysis of terminal, non-reducing alpha-D-xylose residues with release of alpha-D-xylose.
Synonyms
alpha-xylosidase, atxyl1, mexyl31, cjxyl31a, xyl31a, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-xylosidase
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SYSTEMATIC NAME
IUBMB Comments
alpha-D-xyloside xylohydrolase
The enzyme catalyses hydrolysis of a terminal, unsubstituted xyloside at the extreme reducing end of a xylogluco-oligosaccharide. Representative alpha-xylosidases from glycoside hydrolase family 31 utilize a two-step (double-displacement) mechanism involving a covalent glycosyl-enzyme intermediate, and retain the anomeric configuration of the product.
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
4-nitrophenyl alpha-D-xyloside + H2O
4-nitrophenol + alpha-D-xylose
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-
-
?
4-nitrophenyl alpha-maltoside + H2O
4-nitrophenyl alpha-D-glucoside + D-glucose
low activity
-
-
?
4-nitrophenyl beta-isoprimeveroside + H2O
4-nitrophenyl beta-D-glucoside + D-xylose
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-
-
?
4-nitrophenyl beta-isoprimeveroside + H2O
alpha-D-xylose + 4-nitrophenyl beta-D-glucopyranoside
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-
-
?
4-nitrophenyl-alpha-D-glucoside + H2O
4-nitrophenol + alpha-D-glucose
kcat/KM is 0.2% compared to the value for 4-nitrophenyl-beta-isoprimeveroside
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-
?
4-nitrophenyl-alpha-D-xyloside + H2O
4-nitrophenol + alpha-D-xylose
kcat/KM is 3% compared to the value for 4-nitrophenyl-beta-isoprimeveroside
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-
?
maltose + H2O
2 D-glucose
kcat/KM is 1% compared to the value for 4-nitrophenyl-beta-isoprimeveroside
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-
?
maltotriose + H2O
D-maltose + D-glucose
kcat/KM is 3% compared to the value for 4-nitrophenyl-beta-isoprimeveroside
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-
?
isoprimeverose + H2O
alpha-D-xylose + beta-D-glucose
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-
-
?
isoprimeverose + H2O
alpha-D-xylose + beta-D-glucose
kcat/KM is 11.5% compared to the value for 4-nitrophenyl-beta-isoprimeveroside
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-
?
xyloglucan oligosaccharide + H2O
alpha-D-xylose + ?
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-
-
?
xyloglucan oligosaccharide + H2O
alpha-D-xylose + ?
xyloglucan oligosaccharide from tamarind seed xyloglucan
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-
?
additional information
?
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exo-acting enzyme, attacks the non-reducing end of the substrate. No activity is found on isomaltose, trehalose, sucrose, starch, amylose, glycogen, pullulan, xyloglucan, 4-nitrophenyl-alpha-D-galactoside, 4-nitrophenyl-alpha-L-arabinoside, 4-nitrophenyl-alpha-L-rhamnoside, 4-nitrophenyl-alpha-D-mannoside, and 4-nitrophenyl-alpha-L-fucoside
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?
additional information
?
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exo-acting enzyme, attacks the non-reducing end of the substrate. No activity is found on isomaltose, trehalose, sucrose, starch, amylose, glycogen, pullulan, xyloglucan, 4-nitrophenyl-alpha-D-galactoside, 4-nitrophenyl-alpha-L-arabinoside, 4-nitrophenyl-alpha-L-rhamnoside, 4-nitrophenyl-alpha-D-mannoside, and 4-nitrophenyl-alpha-L-fucoside
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?
additional information
?
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the enzyme has transxylosidic activity, forming, in a retaining mode alpha-xylosides. The attachment of xylose is greatly favored on the oxygen of the C-6 of (i) a free glucose molecule, (ii) the 4-nitrophenyl beta derivative of glucose, and (iii) the 4-nitrophenyl beta-derivative of cellobiose. The exo-acting characteristic of this enzyme is also operative in the synthetic mode as is found in the hydrolytic reaction
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?
additional information
?
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the enzyme has transxylosidic activity, forming, in a retaining mode alpha-xylosides. The attachment of xylose is greatly favored on the oxygen of the C-6 of (i) a free glucose molecule, (ii) the 4-nitrophenyl beta derivative of glucose, and (iii) the 4-nitrophenyl beta-derivative of cellobiose. The exo-acting characteristic of this enzyme is also operative in the synthetic mode as is found in the hydrolytic reaction
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?
additional information
?
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the enzyme has transxylosidic activity and is able to synthesize alpha-xylosides. The attachment of xylose is greatly favored on the oxygen of the C-6 of a free glucose molecule, the 4-nitrophenyl-beta derivative of glucose, and the 4-nitrophenyl derivative of cellobiose
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-
?
additional information
?
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the enzyme has transxylosidic activity and is able to synthesize alpha-xylosides. The attachment of xylose is greatly favored on the oxygen of the C-6 of a free glucose molecule, the 4-nitrophenyl-beta derivative of glucose, and the 4-nitrophenyl derivative of cellobiose
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-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Moracci, M.; Cobucci Ponzano, B.; Trincone, A.; Fusco, S.; De Rosa, M.; van Der Oost, J.; Sensen, C.W.; Charlebois, R.L.; Rossi, M.
Identification and molecular characterization of the first alpha-xylosidase from an archaeon
J. Biol. Chem.
275
22082-22089
2000
Saccharolobus solfataricus (Q9P999), Saccharolobus solfataricus, Saccharolobus solfataricus MT4 (Q9P999)
Trincone, A.; Cobucci-Ponzano, B.; Di Lauro, B.; Rossi, M.; Mitsubishi, Y.; Moracci, M.
Enzymatic synthesis and hydrolysis of xylogluco-oligosaccharides using the first archaeal alpha-xylosidase from Sulfolobus solfataricus
Extremophiles
5
277-282
2001
Saccharolobus solfataricus, Saccharolobus solfataricus (Q9P999), Saccharolobus solfataricus P2 (Q9P999)
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