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Information on EC 3.2.1.37 - xylan 1,4-beta-xylosidase

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EC Tree
IUBMB Comments
Also hydrolyses xylobiose. Some other exoglycosidase activities have been found associated with this enzyme in sheep liver.
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UNIPROT: Q09LX0
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
beta-xylosidase, alpha-l-arabinofuranosidase, xylosidase, beta-d-xylosidase, xyl i, xynb2, xyl3a, xln-dt, xynb3, xyl43a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,4-beta-D-xylan xylohydrolase
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beta-D-xylopyranosidase
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beta-xylosidase
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exo-1,4-beta-D-xylosidase
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exo-1,4-beta-xylosidase
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Exo-beta-(1,4)-xylanase
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Xylan 1,4-beta-xylosidase
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xylobiase
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additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini
show the reaction diagram
catalytic residues D15, D128, and E187 are essential for activity, reaction mechanism
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
4-beta-D-xylan xylohydrolase
Also hydrolyses xylobiose. Some other exoglycosidase activities have been found associated with this enzyme in sheep liver.
CAS REGISTRY NUMBER
COMMENTARY hide
9025-53-0
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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
2,5-dinitrophenyl-beta-D-xylopyranoside + H2O
2,5-dinitrophenol + beta-D-xylose
show the reaction diagram
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?
3,4-dinitrophenyl beta-D-xylopyranoside + H2O
3,4-dinitrophenol + beta-D-xylopyranose
show the reaction diagram
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?
3,5-dinitrophenyl beta-D-xylopyranoside + H2O
3,5-dinitrophenol + beta-D-xylose
show the reaction diagram
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?
4-bromophenyl-beta-D-xylopyranoside + H2O
4-bromophenol + beta-D-xylose
show the reaction diagram
low activity of mutant E178G, no activity of the wild-type enzyme
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?
4-methylumbelliferyl-beta-D-xylopyranoside + H2O
4-methylumbelliferol + beta-D-xylose
show the reaction diagram
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?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
show the reaction diagram
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?
additional information
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substrate specificity of wild-type enzyme and mutant E178G, the mutant enzyme shows residual activity with 2-naphthyl-beta-D-xylopyranoside, 3,4-dimethylphenyl-beta-D-xylopyranoside, and 3-nitrophenyl-beta-D-xylopyranoside, while the wild-type enzyme is inactive with these substrates, overview
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
the enzyme is not affected by 1 mM of Fe3+, Ca2+, Co2+, Mg2+, Ba2+, Ni2+, K+, Zn2+, Cu2+, or EDTA
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ag+
97% inhibition at 1 mM
Hg2+
complete inhibition at 1 mM, 93% inhibition at 0.1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
steady-state kinetics, recombinant wild-type and mutant enzymes
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
25 - 30
2,5-dinitrophenyl-beta-D-xylopyranoside
1.8 - 77
3,4-dinitrophenyl-beta-D-xylopyranoside
20
4-methylumbelliferyl-beta-D-xylopyranoside
pH 7.0, 40°C, recombinant wild-type enzyme
0.014 - 57
4-nitrophenyl-beta-D-xylopyranoside
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH profiles, wild-type and mutant enzymes, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
temperature profile and thermal stability
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
i.e. Bacillus stearothermophilus, strain T-6, gene xynB3
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q09LX0_GEOSE
535
0
61908
TrEMBL
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant wild-type and mutant D15G, D128G, and E178G XynB3s, 22-30 mg/ml protein, 0.005 ml protein solution is mixed with 0.005 ml reservoir solution and 0.001 ml detergent solution, equilibration to 0.5 ml with reservoir solution, X-ray diffraction structure determination and preliminary analysis at 2.2-2.5 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D128G
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme, nearly inactive mutant
D15G
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme, nearly inactive mutant
E178G
site-directed mutagenesis, the mutant shows an altered substrate specificity and highly reduced activity compared to the wild-type enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
temperature profile and thermal stability
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant soluble wild-type and mutant D15G, D128G, and E178G enzymes from Escherichia coli strain BL21(DE3) by heat treatment and gel filtration
recombinant soluble wild-type, 2.6fold to over 95% purity, and mutant enzymes from Escherichia coli strain BL21(DE3) by heat treatment and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene xynB3, expression of soluble wild-type and mutant D15G, D128G, and E178G enzymes in Escherichia coli strain BL21(DE3)
gene xynB3, expression of soluble wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bruex, C.; Niefind, K.; Ben-David, A.; Leon, M.; Shoham, G.; Shoham, Y.; Schomburg, D.
Crystallization and preliminary crystallographic analysis of a family 43 beta-D-xylosidase from Geobacillus stearothermophilus T-6
Acta Crystallogr. Sect. F
F61
1054-1057
2005
Geobacillus stearothermophilus (Q09LX0)
Manually annotated by BRENDA team
Shallom, D.; Leon, M.; Bravman, T.; Ben-David, A.; Zaide, G.; Belakhov, V.; Shoham, G.; Schomburg, D.; Baasov, T.; Shoham, Y.
Biochemical characterization and identification of the catalytic residues of a family 43 beta-D-xylosidase from Geobacillus stearothermophilus T-6
Biochemistry
44
387-397
2005
Geobacillus stearothermophilus (Q09LX0)
Manually annotated by BRENDA team