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Information on EC 3.2.1.177 - alpha-D-xyloside xylohydrolase
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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 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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-D-xyloside xylohydrolase
alpha-xylosidase
XylS
alpha-xylosidase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of terminal, non-reducing alpha-D-xylose residues with release of alpha-D-xylose.
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-
-
-
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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.
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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
4-methylumbelliferyl-alpha-D-glucoside + H2O
4-methylumbelliferol + D-glucose
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
low activity
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
low activity
-
-
?
4-nitrophenyl alpha-D-xylopyranoside + H2O
4-nitrophenol + D-xylose
best substrate
-
-
?
4-nitrophenyl alpha-D-xyloside + H2O
4-nitrophenol + alpha-D-xylose
-
-
-
?
4-nitrophenyl beta-isoprimeveroside + H2O
4-nitrophenyl beta-D-glucoside + D-xylose
-
-
-
?
4-nitrophenyl beta-isoprimeveroside + H2O
alpha-D-xylose + 4-nitrophenyl beta-D-glucopyranoside
4-nitrophenyl-alpha-D-xylopyranoside + H2O
4-nitrophenol + alpha-D-xylose
-
-
-
?
alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc + H2O
alpha-D-Xyl-(1->6)-beta-D-Glc-(1->4)-beta-D-Glc + D-xylose
low activity
-
-
?
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 + H2O
?
low activity
-
-
?
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)-D-Glc + H2O
D-xylose + 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) D-Glc
-
-
-
-
?
isoprimeverose + H2O
D-xylose + D-glucose
6-O-(alpha-D-xylopyranosyl)-D-glucose or 6-O-alpha-D-xylopyranosyl-beta-D-glucopyranose, low activity
-
-
?
xyloglucan + H2O
?
-
pea xyloglucan, tamarind xyloglucans, etiolated peas, green peas, corn stover, lamb's quarters
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-
?
xyloglucan oligosaccharide + H2O
?
-
extensive interactions between the enzyme's active-site variants and xyloglucan hexa- and heptasaccharides. The enzyme recognizes the entire cello-tetraosyl backbone of the substrate and product in positive enzyme subsites and makes further significant interactions with internal pendant alpha-(1->6)-linked xylosyl units, role of the PA14 domain, stereochemistry of the hydrolysis, overview
-
-
?
4-nitrophenyl alpha-maltoside + H2O
4-nitrophenyl alpha-D-glucoside + D-glucose
low activity
-
-
?
4-nitrophenyl alpha-maltoside + H2O
4-nitrophenyl alpha-D-glucoside + D-glucose
low activity
-
-
?
4-nitrophenyl beta-isoprimeveroside + H2O
alpha-D-xylose + 4-nitrophenyl beta-D-glucopyranoside
-
-
-
?
4-nitrophenyl beta-isoprimeveroside + H2O
alpha-D-xylose + 4-nitrophenyl beta-D-glucopyranoside
-
-
-
?
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
-
-
?
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
-
-
?
4-nitrophenyl-alpha-D-xyloside + H2O
4-nitrophenol + alpha-D-xylose
-
-
-
?
4-nitrophenyl-alpha-D-xyloside + H2O
4-nitrophenol + alpha-D-xylose
-
-
-
-
?
4-nitrophenyl-alpha-D-xyloside + H2O
4-nitrophenol + alpha-D-xylose
kcat/KM is 3% compared to the value for 4-nitrophenyl-beta-isoprimeveroside
-
-
?
4-nitrophenyl-alpha-D-xyloside + H2O
4-nitrophenol + alpha-D-xylose
kcat/KM is 3% compared to the value for 4-nitrophenyl-beta-isoprimeveroside
-
-
?
alpha-D-xylopyranosyl fluoride + H2O
alpha-D-xylose + fluoride
-
-
-
?
isoprimeverose + H2O
alpha-D-xylose + beta-D-glucose
kcat/KM is 11.5% compared to the value for 4-nitrophenyl-beta-isoprimeveroside
-
-
?
isoprimeverose + H2O
alpha-D-xylose + beta-D-glucose
-
-
-
?
isoprimeverose + H2O
alpha-D-xylose + beta-D-glucose
kcat/KM is 11.5% compared to the value for 4-nitrophenyl-beta-isoprimeveroside
-
-
?
isoprimeverose + H2O
alpha-D-xylose + beta-D-glucose
-
-
-
?
maltose + H2O
2 D-glucose
kcat/KM is 1% compared to the value for 4-nitrophenyl-beta-isoprimeveroside
-
-
?
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
-
-
?
xyloglucan + H2O
xylose + ?
-
xyloglucan oligosaccharide from tamarind seed xyloglucan
-
-
?
xyloglucan oligosaccharide + H2O
alpha-D-xylose + ?
-
-
-
?
xyloglucan oligosaccharide + H2O
alpha-D-xylose + ?
xyloglucan oligosaccharide from tamarind seed xyloglucan
-
-
?
xyloglucan oligosaccharide + H2O
alpha-D-xylose + ?
-
-
-
?
additional information
?
-
-
the enzyme promotes the release of free glucose and xylose from substrates containing alpha-linked xylose, including isoprimeverose, the heptasaccharide subunit of pea xyloglucan, and tamarind xyloglucan
-
-
?
additional information
?
-
CjXyl31A exhibits high regiospecificity for the hydrolysis of xylogluco-oligosaccharides, with a particular preference for longer substrates
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?
additional information
?
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CjXyl31A exhibits high regiospecificity for the hydrolysis of xylogluco-oligosaccharides, with a particular preference for longer substrates
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-
?
additional information
?
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-
the enzyme CjXyl31A demonstrates an exquisite regioselectivity for the terminal nonreducing-end alpha-(1->6)-xylose of xyloglucan oliogosaccharides
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-
?
additional information
?
-
specific activity of wild-type enzyme with 4-nitrophenyl-alpha-D-glucoside is 96244fold lower compared to specific activity with isoprimeverose
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-
?
additional information
?
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-
specific activity of wild-type enzyme with 4-nitrophenyl-alpha-D-glucoside is 96244fold lower compared to specific activity with isoprimeverose
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?
additional information
?
-
the enzyme alos shows transglycosylation activity
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-
?
additional information
?
-
-
the enzyme alos shows transglycosylation activity
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-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
substrate specificty, overview. The enzyme is not active with 0.16% tamarind seed xyloglucan, maltose, 4-nitrophenyl-beta-D-glucopyranoside, 4-nitrophenyl-alpha-D-mannopyranoside, 4-nitrophenyl-beta-D-mannopyranoside, 4-nitrophenyl-alpha-L-rhamnopyranoside, 4-nitrophenyl-beta-D-xylopyranoside, 4-nitrophenyl-alpha-L-arabinofuranoside, 4-nitrophenyl-alpha-L-arabinopyranoside, 4-nitrophenyl-beta-L-arabinopyranoside, 4-nitrophenyl-alpha-L-fucopyranoside, 4-nitrophenyl-beta-D-fucopyranoside, 4-nitrophenyl-beta-L-fucopyranoside, 4-nitrophenyl-alpha-D-galactopyranoside, and 4-nitrophenyl-beta-D-galactopyranoside
-
-
?
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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
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)-D-Glc + H2O
D-xylose + 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) D-Glc
-
-
-
-
?
additional information
?
-
-
the enzyme promotes the release of free glucose and xylose from substrates containing alpha-linked xylose, including isoprimeverose, the heptasaccharide subunit of pea xyloglucan, and tamarind xyloglucan
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
no effect on hydrolysis of 4-nitrophenyl-alpha-D-xyloside: Ca2+, Mg2+, Mn2+, Zn2+, Ni2+, Cu2+, and Co2+
additional information
poor effect on activity by 5 mM Mg2+, Mn2+ and Ca2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(5R)-5-fluoro-alpha-D-xylopyranosyl fluoride
mechanism-based inactivator
(5S)-5-fluoro-alpha-D-xylopyranosyl fluoride
mechanism-based inactivator
additional information
no effect on activity by 10 mM EDTA
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no effect on activity by 10 mM EDTA
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.39
4-nitrophenyl alpha-D-xylopyranoside
pH 5.5, 45°C, recombinant enzyme
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
154
4-nitrophenyl alpha-D-xylopyranoside
pH 5.5, 45°C, recombinant enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
64.4
4-nitrophenyl alpha-D-xylopyranoside
pH 5.5, 45°C, recombinant enzyme
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00045
(5R)-5-fluoro-alpha-D-xylopyranosyl fluoride
pH 7.0, 37°C, mechanism-based inactivator
0.0098
(5S)-5-fluoro-alpha-D-xylopyranosyl fluoride
pH 7.0, 37°C, mechanism-based inactivator
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0187
4-nitrophenyl-alpha-D-xyloside, pH 7.0, 37°C, wild-type enzyme
0.2
pH 5.5, 45°C, recombinant enzyme, substrate alpha-D-Xyl-(1->6)-beta-D-Glc-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-[alpha-D-Xyl-(1->6)]-beta-D-Glc
0.22
pH 5.5, 45°C, recombinant enzyme, substrate alpha-D-Xyl-(1->6)-beta-D-Glc-[alpha-D-Xyl-(1->6)]-beta-D-Glc-(1->4)-beta-D-Glc
0.54
pH 5.5, 45°C, recombinant enzyme, substrate 4-nitrophenyl alpha-D-glucopyranoside
2
pH 5.5, 45°C, recombinant enzyme, substrate isoprimeverose
69.5
pH 5.5, 45°C, recombinant enzyme, substrate 4-nitrophenyl alpha-D-xylopyranoside
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 8.5
pH 4.5: about 60% of maximal activity, pH 8.5: about 60% of maximal activity
5 - 8
pH 5.0: about 60% of maximal activity, pH 8.0: about 45% of maximal activity
5 - 9
pH 5.0: about 35% of maximal activity, pH 9.0: about 65% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
hydrolysis of 4-nitrophenyl-alpha-D-xyloside increases up to 50°C, activity is rapidly lost at higher temperatures
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
