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Information on EC 3.2.1.177 - alpha-D-xyloside xylohydrolase and Organism(s) Escherichia coli and UniProt Accession P31434

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IUBMB 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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This record set is specific for:
Escherichia coli
UNIPROT: P31434
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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Hydrolysis of terminal, non-reducing alpha-D-xylose residues with release of alpha-D-xylose.
Synonyms
alpha-xylosidase, atxyl1, mexyl31, cjxyl31a, xyl31a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha-xylosidase
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PATHWAY SOURCE
PATHWAYS
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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) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
show the reaction diagram
low activity
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-
?
4-nitrophenyl-alpha-D-xyloside + H2O
4-nitrophenol + alpha-D-xylose
show the reaction diagram
alpha-D-xylopyranosyl fluoride + H2O
alpha-D-xylose + fluoride
show the reaction diagram
isoprimeverose + H2O
alpha-D-xylose + beta-D-glucose
show the reaction diagram
xyloglucan oligosaccharide + H2O
alpha-D-xylose + ?
show the reaction diagram
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-
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?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
no effect on hydrolysis of 4-nitrophenyl-alpha-D-xyloside: Ca2+, Mg2+, Mn2+, Zn2+, Ni2+, Cu2+, and Co2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(5R)-5-fluoro-alpha-D-xylopyranosyl fluoride
mechanism-based inactivator
(5S)-5-fluoro-alpha-D-xylopyranosyl fluoride
mechanism-based inactivator
1-deoxynojirimycin
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1-deoxyxylonojirimycin
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xyloisofagomine
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.7
4-nitrophenyl-alpha-D-glucopyranoside
pH 7.0, 37°C
0.52 - 0.71
4-nitrophenyl-alpha-D-xyloside
0.17 - 0.97
alpha-D-xylopyranosyl fluoride
0.55
Isoprimeverose
pH 7.0, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.046
4-nitrophenyl-alpha-D-glucopyranoside
pH 7.0, 37°C
0.13 - 0.173
4-nitrophenyl-alpha-D-xyloside
75 - 195
alpha-D-xylopyranosyl fluoride
51.3
Isoprimeverose
pH 7.0, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0064
4-nitrophenyl-alpha-D-glucopyranoside
pH 7.0, 37°C
0.18 - 3.33
4-nitrophenyl-alpha-D-xyloside
77.3 - 1220
alpha-D-xylopyranosyl fluoride
93.3
Isoprimeverose
pH 7.0, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
0.13
1-deoxynojirimycin
pH 7.0, 37°C
0.0009
1-deoxyxylonojirimycin
pH 7.0, 37°C
0.17
xyloisofagomine
pH 7.0, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00126
isoprimeverose, pH 7.0, 37°C, mutant enzyme C307I
0.00545
isoprimeverose, pH 7.0, 37°C, mutant enzyme K414W
0.0187
4-nitrophenyl-alpha-D-xyloside, pH 7.0, 37°C, wild-type enzyme
0.0192
isoprimeverose, pH 7.0, 37°C, mutant enzyme W345I
0.0495
isoprimeverose, pH 7.0, 37°C, mutant enzyme F277Y
0.503
pH 7.0, 37°C
20.5
isoprimeverose, pH 7.0, 37°C, wild-type enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.4
hydrolysis of 4-nitrophenyl-alpha-D-xyloside
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
hydrolysis of 4-nitrophenyl-alpha-D-xyloside increases up to 50°C, activity is rapidly lost at higher temperatures
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
530000
gel filtration
88000
6 * 88000, SDS-PAGE
88079
6 * 88079, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop method, 2.2 A resolution structure
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C307I
isoprimeverose-hydrolyzing activity of the mutant enzyme is reduced 400fold compared to wild-type enzyme. alpha-Glucosidase activity is not detected
C307I/F308D
alpha-xylosidase activity of wild-type enzyme is converted into alpha-glucosidase activity. Mutant shows 140fold higher hydrolytic activity against p-nitrophenyl alpha-glucopyranoside than wild-type YicI. The mutant is able to hydrolyze nigerose [alpha-D-Glcp-(1->3)-D-Glcp] and kojibiose [alpha-D-Glcp-(1->2)-D-Glcp], which are not hydrolyzed by the wild-type enzyme. Isoprimeverose-hydrolyzing activity of the L1Chi mutant is decreased by about 3700fold, and that of C307I/F308D is diminished to below the limits of detection. alpha-Glucosidase activity with 4-nitrophenyl alpha-D-glucoside is increased 132fold compared to wild-type activity
F277Y
isoprimeverose-hydrolyzing activity of the mutant enzyme is reduced 20fold compared to wild-type enzyme. alpha-Glucosidase activity is not detected (alpha-glucosidase activity of the wild-type enzyme is 96244fold lower than specific activity with isoprimeverose)
K414W
isoprimeverose-hydrolyzing activity of the mutant enzyme is reduced 12000fold compared to wild-type enzyme. alpha-Glucosidase activity is not detected
W345I
isoprimeverose-hydrolyzing activity of the mutant enzyme is reduced 16000fold compared to wild-type enzyme. alpha-Glucosidase activity is not detected
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.7 - 10.1
4°C, 24 h, stable
716825
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
47
15 min, stable up to
55
15 min, about 70% loss of activity
7
37°C, retains full activity for 48 h
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, pH 7.0, retains full activity for several months
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Okuyama, M.; Kaneko, A.; Mori, H.; Chiba, S.; Kimura, A.
Structural elements to convert Escherichia coli alpha-xylosidase (YicI) into alpha-glucosidase
FEBS Lett.
580
2707-2711
2006
Escherichia coli (P31434), Escherichia coli
Manually annotated by BRENDA team
Lovering, A.L.; Lee, S.S.; Kim, Y.W.; Withers, S.G.; Strynadka, N.C.
Mechanistic and structural analysis of a family 31 alpha-glycosidase and its glycosyl-enzyme intermediate
J. Biol. Chem.
280
2105-2115
2005
Escherichia coli (P31434)
Manually annotated by BRENDA team
Okuyama, M.; Mori, H.; Chiba, S.; Kimura A.
Overexpression and characterization of two unknown proteins, YicI and YihQ, originated from Escherichia coli
Protein Expr. Purif.
37
170-179
2004
Escherichia coli (P31434), Escherichia coli
Manually annotated by BRENDA team