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Information on EC 3.2.1.37 - xylan 1,4-beta-xylosidase
for references in articles please use BRENDA:EC3.2.1.37
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EC Tree 3 Hydrolases
3.2 Glycosylases
3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
3.2.1.37 xylan 1,4-beta-xylosidase
IUBMB Comments
Also hydrolyses xylobiose. Some other exoglycosidase activities have been found associated with this enzyme in sheep liver.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
- 3.2.1.37
- xylans
- xylose
- arabinose
- arabinoxylans
- xylobiose
- xylooligosaccharides
- niger
- trichoderma
- p-nitrophenyl
-
xylanolytic
- cellulase
- xylanases
-
hemicellulases
- endoxylanase
- arabinans
- reesei
- spelt
- beta-d-xylopyranoside
- endoglucanase
-
saccharification
- cellobiohydrolase
- p-nitrophenyl-beta-d-xylopyranoside
- pumilus
- beta-d-galactosidase
-
xylan-degrading
- beta-xylanase
-
arabinosidase
- alpha-fucosidase
- avicel
-
birchwood
- beta-d-fucosidase
- cmcases
-
thermoanaerobacterium
- alpha-glucuronidase
- thermomonospora
-
xylopyranosyl
- saccharolyticum
- ruminantium
- xylotetraose
-
hemicellulolytic
-
feruloyl
- alpha-d-mannosidase
- fibrisolvens
- endo-1,4-beta-xylanase
-
selenomonas
- glucuronoxylans
-
hemicellulosic
- nutrition
- degradation
- synthesis
- food industry
- analysis
- biotechnology
-
xylanohydrolase
- biofuel production
- agriculture
- alpha-d-galactosidase
- industry
- l-arabitol
- pharmacology
showSynonyms
beta-xylosidase, alpha-l-arabinofuranosidase, xylosidase, beta-d-xylosidase, xyl i, xynb2, xyl3a, xln-dt, xynb3, axh-d3, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,4-beta-D-xylan xylohydrolase
-
-
-
-
1,4-beta-D-xylosidase
ABF3
alpha-L-arabinofuranosidase
alpha-L-arabinofuranosidase 3
alpha-L-arabinofuranoside arabinofuranohydrolase
arabinofuranosidase 3
Axy43A
BbXyl
beta-(1,2)-D-xylosidase
beta-1,4-xylosidase
beta-D-xylopyranosidase
-
-
-
-
beta-D-xylosidase
beta-glucosidase/xylosidase
bifunctional, belongs to to the glycoside hydrolase 3 familiy, GH3
beta-xylosidase
beta-xylosidase-1
beta-xylosidase-2
BfdXYL2
bifunctional beta-glucosidase/xylosidase
belongs to glycosyl hydrolase family 3, GH3
BlxA
BxTW1
ccxyl3a
DICTH_1792
Dt-Xyl3
DtXyl
exo-1,4-beta-D-xylosidase
-
-
-
-
exo-1,4-beta-xylosidase
Exo-beta-(1,4)-xylanase
-
-
-
-
GH 11 beta-xylosidase
GH 39 beta-xylosidase
GH3 beta-xylosidase
GH39 beta-xylosidase
GH43 beta-1,4-xylosidase
GH43 beta-xylosidase
GH43 family beta-xylosidase
GH43 xylosidase
GH43B6
GH5 beta-xylosidase
glycoside hydrolase family 3 beta-xylosidase
Pae1263
PxXyl43A
RrXyl43A
Rubg3A
gene name, together with Rubg3B, beta-glucosidase/xylosidase activity, EC 3.2.1.37 and 3.2.1.74
Rubg3B
gene name, together with Rubg3A, beta-glucosidase/xylosidase activity, EC 3.2.1.37 and 3.2.1.74
RuBGX1
gene name, beta-glucosidase/xylosidase activity, EC 3.2.1.37 and 3.2.1.21
SSO3032
T81Xyl5_22A
Tpexyl3
Xln-DT
Xyl
XYL1
XYL3
xyl43
Xylan 1,4-beta-xylosidase
xylanase
XylC
XylCD2
XYLO
xylobiase
-
-
-
-
xylosidase
XynB
XynB-DT
XynB2
additional information
ABF3
bifunctional enzyme having both alpha-L-arabinofuranosidase and xylobiohydrolase functionalities
ABF3
bifunctional enzyme having both alpha-L-arabinofuranosidase and xylobiohydrolase functionalities
-
arabinofuranosidase 3
bifunctional enzyme having both alpha-L-arabinofuranosidase and xylobiohydrolase functionalities
arabinofuranosidase 3
bifunctional enzyme having both alpha-L-arabinofuranosidase and xylobiohydrolase functionalities
-
beta-xylosidase
-
-
-
-
exo-1,4-beta-xylosidase
-
-
-
-
Xylan 1,4-beta-xylosidase
-
-
-
-
additional information
cf. EC 3.2.1.55, alpha-L-arabinofuranosidase
additional information
the enzyme belongs to the glycosyl hydrolase family 43, GH43
additional information
the enzyme belongs to the glycosyl hydrolase family 43, GH43
additional information
the enzyme belongs to the glycoside hydrolase family 52
additional information
-
the enzyme belongs to the glycosyl hydrolase family 3, GH3, cf. EC 3.2.1.55, alpha-L-arabinofuranosidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini
Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini
Also hydrolyses xylobiose. Some other exoglycosidase activities have been found associated with this enzyme in sheep liver
-
-
-
Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini
mechanism
-
Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini
Glu160 is the acid-base catalyst, kinetics
-
Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini
mechanism
-
Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini
kinetics
-
Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini
ordered bi-bi mechanism, kinetics
-
Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini
retention of anomeric configuration, two-step mechanism, SN2-like transition state
-
Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini
catalytic residues D15, D128, and E187 are essential for activity, reaction mechanism
Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini
hydrolysis of 4-nitrophenyl-beta-D-xylopyranoside with overall retention of substrate anomeric configuration, double-displacement mechanism. Deglycosylation is the rate-limiting step for the enzymatic hydrolysis
-
Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini
active site residues are D242 and E441
-
Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini
active site residues are D264 and E464
-
Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini
hydrolysis of 4-nitrophenyl-beta-D-xylopyranoside with overall retention of substrate anomeric configuration, double-displacement mechanism. Deglycosylation is the rate-limiting step for the enzymatic hydrolysis
-
-
Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini
Glu160 is the acid-base catalyst, kinetics
-
-
Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini
retention of anomeric configuration, two-step mechanism, SN2-like transition state
-
-
Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini
ordered bi-bi mechanism, kinetics
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
(1,4)-beta-D-xylan degradation
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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.
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CAS REGISTRY NUMBER
COMMENTARY
9025-53-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2-hydroxymethylphenyl)-beta-D-glucopyranoside + H2O
2-hydroxymethylphenol + beta-D-glucose
-
Substrates: low activity
Products: -
Products: -
?
1,4-beta-D-xylobiose + H2O
2 D-xylose
-
Substrates: thermodynamic parameters for hydrolysis. Rate enhancement kcat/knon, increases with decreasing temperature
Products: -
Products: -
?
2 D-xylose
xylobiose + H2O
-
Substrates: -
Products: and higher xylooligosaccharides, immobilized enzyme in presence of high concentration of xylose
Products: and higher xylooligosaccharides, immobilized enzyme in presence of high concentration of xylose
r
2,4-dinitrophenyl 2-deoxy-2-fluoro-beta-D-xyloside + H2O
2,4-dinitrophenol + 2-deoxy-2-fluoro-beta-D-xylose
-
Substrates: -
Products: -
Products: -
?
2,4-dinitrophenyl-1-thio-beta-D-xylopyranoside + H2O
2,4-dinitrophenol + 1-thio-beta-D-xylopyranose
Penicillium wortmanni
-
Substrates: -
Products: -
Products: -
?
2,5-dinitrophenyl-beta-D-xylopyranoside + H2O
2,5-dinitrophenol + beta-D-xylose
Substrates: -
Products: -
Products: -
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + beta-D-glucose
-
Substrates: 1.7% of the activity with 4-nitrophenyl-alpha-L-arabinofuranoside
Products: -
Products: -
?
2-nitrophenyl beta-D-glucoside + H2O
2-nitrophenol + D-glucose
-
Substrates: 6.4% activity compared to 4-nitrophenyl beta-D-xyloside
Products: -
Products: -
?
2-nitrophenyl xylopyranoside + H2O
2-nitrophenol + xylopyranose
-
Substrates: -
Products: -
Products: -
?
2-O-beta-D-glucopyranosyl-D-glucopyranoside + H2O
beta-D-glucose + D-glucose
-
Substrates: sophorose, low activity
Products: -
Products: -
?
3 xylotriose
xylotetraose + xylopentaose
-
Substrates: transxylosylation activity
Products: -
Products: -
?
3,4-dimethylphenyl-beta-D-xylopyranoside + H2O
3,4-dimethylphenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
3,4-dinitrophenyl beta-D-xylopyranoside + H2O
?
Substrates: -
Products: -
Products: -
?
3,4-dinitrophenyl beta-D-xyloside + H2O
3,4-dinitrophenol + D-xylose
Substrates: 48 activity compared to 4-nitrophenyl beta-D-xyloside
Products: -
Products: -
?
3,5-dichlorophenyl-beta-D-xylopyranoside + H2O
3,5-dichlorophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
3,5-dinitrophenyl beta-D-xylopyranoside + H2O
3,5-dinitrophenol + beta-D-xylose
Substrates: -
Products: -
Products: -
?
3-chlorophenyl-beta-D-xylopyranoside + H2O
3-chlorophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
3-nitrophenyl beta-D-xylopyranoside + H2O
3-nitrophenol + D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
3-O-beta-D-glucopyranosyl-D-glucopyranoside + H2O
beta-D-glucose + D-glucose
-
Substrates: laminaribiose, low activity
Products: -
Products: -
?
4-bromophenyl-beta-D-xylopyranoside + H2O
4-bromophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
4-bromophenyl-beta-D-xylopyranoside + H2O
4-bromophenol + beta-D-xylose
Substrates: low activity of mutant E178G, no activity of the wild-type enzyme
Products: -
Products: -
?
4-chloro-2-nitrophenyl beta-D-xylopyranoside + H2O
4-chloro-2-nitrophenol + beta-D-xylopyranose
4-cyanophenyl-beta-D-xylopyranoside + H2O
4-cyanophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-alpha-L-arabinofuranoside + H2O
4-methylumbelliferol + alpha-L-arabinofuranose
4-methylumbelliferyl-beta-D-xylopyranoside + H2O
4-methylumbelliferone + beta-D-xylopyranose
4-nitrophenyl alpha-D-galactoside + H2O
4-nitrophenol + D-galactose
-
Substrates: 0.3% activity compared to 4-nitrophenyl beta-D-xyloside
Products: -
Products: -
?
4-nitrophenyl alpha-D-mannoside + H2O
4-nitrophenol + mannose
-
Substrates: 0.4% activity compared to 4-nitrophenyl beta-D-xyloside
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinopyranoside + H2O
4-nitrophenol + alpha-L-arabinose
Substrates: 3.2% activity compared to 4-nitrophenyl alpha-D-xylopyranoside
Products: -
Products: -
?
4-nitrophenyl beta-D-xylopyranoside + methanol
4-nitrophenol + methyl beta-D-xylopyranoside
-
Substrates: transxylosylation activity, NMR study in the presence of 15% methanol, v/v
Products: very weak peaks of D-xylose-alpha-anomers, most D-xylose-beta-anomers
Products: very weak peaks of D-xylose-alpha-anomers, most D-xylose-beta-anomers
?
4-nitrophenyl beta-D-xylopyranoside + xylobiose
4-nitrophenol + xylotriose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-xylopyranoside + xylotriose
4-nitrophenol + xylotetraose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl xylopyranoside + H2O
4-nitrophenol + xylopyranose
-
Substrates: -
Products: -
Products: -
?
4-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
Substrates: cellobiose, 30% activity
Products: -
Products: -
?
6-bromo-2-naphthyl beta-D-xylopyranoside + H2O
6-bromo-2-naphthol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
Substrates: gentiobiose, low activity
Products: -
Products: -
?
anthocyanin + H2O
?
-
Substrates: the enzyme catalyzes the degradation of an anthocyanin component of Brunfelsia calycina, and the release of xylose and galactose due to hydrolysis of glycosidic bonds by BcXyl is detected
Products: -
Products: -
?
arabinoxylan + H2O
D-xylose + L-arabinose
-
Substrates: source of substrate: sugar beet
Products: -
Products: -
?
arabinoxylan + H2O
xylose + arabinose
-
Substrates: source of substrate: wheat
Products: -
Products: -
?
beechwood arabinoxylan + H2O
D-xylose + ?
Substrates: -
Products: -
Products: -
?
beechwood xylan + H2O
D-xylose + ?
Substrates: -
Products: -
Products: -
?
beta(1-4)xylobiose + H2O
beta-D-xylose + beta(1-3)xylobiose + beta(1-4)xylotriose + O-beta-D-xylopyranosyl(1-3)-O-beta-D-xylopyranosyl(1-4)-D-xylopyranose + O-beta-D-xylopyranosyl(1-4)[O-beta-D-xylopyranosyl(1-3)]O-beta-D-xylopyranosyl(1-4)-D-xylopyranose
Penicillium wortmanni
-
Substrates: -
Products: transxylosylation products
Products: transxylosylation products
?
beta-1,3-xylan + H2O
beta-D-xylose + ?
-
Substrates: complete hydrolysis after prolonged incubation
Products: -
Products: -
?
birchwood xylan + H2O
?
Substrates: 1.8% activity compared to 4-nitrophenyl alpha-D-xylopyranoside
Products: -
Products: -
?
cell wall polysaccharide from alfalfa root + H2O
xylose + arabinose
-
Substrates: -
Products: -
Products: -
?
corn straw raw hemicellulose + H2O
? + xylose
-
Substrates: -
Products: -
Products: -
?
Finger millet straw + H2O
?
-
Substrates: from Eleusine coracana from Thenur, Madurai district, Tamil Nadu, India. Two-step optimization of hemicellulose saccharification from the substrate, pretreated with 1% w/v NaOH combined with oven heating at 120°C for 20 min, by 1. endo-1,4-beta-xylanase (CtXyn11A) at 55°C and 2. exo-1,4-beta-xylosidase (BoGH43A) at 37°C, both at pH 7.5 by Box-Behnken design yielding the total reducing sugar yield (TRS) of 70 mg/g pretreated biomass. The percentage conversion of xylan to xylose by CtXyn11A and BoGH43A is 24.7%. Method optimization and evaluation, detailed overview. Thin layer chromatography (TLC) analysis of hydrolysed products of pretreated FMS by CtXyn11A and BoGH43A
Products: -
Products: -
?
laminaribose + H2O
?
-
Substrates: 17.5% activity compared to xylobiose
Products: -
Products: -
?
laminaritriose + H2O
?
-
Substrates: 14.4% activity compared to xylobiose
Products: -
Products: -
?
m-nitrophenyl beta-D-xyloside + H2O
m-nitrophenol + beta-D-xylose
Malbranchea pulchella var. sulfurea
-
Substrates: low activity
Products: -
Products: -
?
m-nitrophenyl-beta-D-xylopyranoside + H2O
m-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
Manalpha(1-6)[Manalpha(1-3)Xylbeta(1-2)]Manbeta(1-4)GlcNAcbeta(1-4)[Fucalpha(1-3)]GlcNAc--pyridylaminoside + H2O
beta-D-xylose + Manalpha(1-6)[Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)[Fucalpha(1-3)]GlcNAc-pyridylaminoside
-
Substrates: complete hydrolysis
Products: -
Products: -
?
methyl beta-D-xylopyranoside + H2O
methanol + beta-D-xylopyranose
Penicillium wortmanni
-
Substrates: -
Products: -
Products: -
?
n-pentyl beta-D-xylopyranoside + H2O
n-pentanol + beta-D-xylopyranose
Penicillium wortmanni
-
Substrates: -
Products: -
Products: -
?
o-N-acetylamino-phenyl-beta-D-xylopyranoside + H2O
o-N-acetylamino-phenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
o-nitrophenyl beta-D-galactopyranoside + H2O
o-nitrophenol + beta-D-galactose
-
Substrates: slight activity
Products: -
Products: -
?
p-chlorophenyl beta-D-xyloside + H2O
p-chlorophenol + beta-D-xylose
-
Substrates: -
Products: -
Products: -
?
p-methoxyphenyl-beta-D-xylopyranoside + H2O
p-methoxyphenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl alpha-L-arabinoside + H2O
4-nitrophenol + alpha-L-arabinose
Substrates: about 6% of the activity with 4-nitrophenyl beta-D-xylopyranoside
Products: -
Products: -
?
p-nitrophenyl alpha-L-arabinoside + H2O
p-nitrophenol + alpha-L-arabinose
-
Substrates: low activity
Products: -
Products: -
?
p-nitrophenyl beta-D-xylopyranoside + beta-D-xylopyranoside
p-nitrophenyl beta-(1-4)-D-xylooligosaccharide + H2O
-
Substrates: -
Products: 2-7 xylopyranose molecules per oligosaccharide
Products: 2-7 xylopyranose molecules per oligosaccharide
r
p-nitrophenyl-alpha-D-arabinoside + H2O
p-nitrophenol + alpha-D-arabinose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-alpha-L-arabinofuranoside + H2O
p-nitrophenol + alpha-L-arabinofuranose
-
Substrates: 5% of activity compared to p-nitrophenyl-beta-D-xylopyranoside
Products: -
Products: -
?
p-nitrophenyl-beta-D-arabinofuranoside + H2O
p-nitrophenol + beta-D-arabinofuranose
Substrates: 8.8% of the acticvity with p-nitrophenyl-beta-D-xylopyranoside
Products: -
Products: -
?
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + beta-D-cellobiose
-
Substrates: 6% of activity compared to p-nitrophenyl-beta-D-xylopyranoside
Products: -
Products: -
?
p-nitrophenyl-beta-D-fucoside + H2O
p-nitrophenol + beta-D-fucose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-beta-D-xyloside + H2O
p-nitrophenol + alpha-D-xylose
Malbranchea pulchella var. sulfurea
-
Substrates: beta-xylosidase-1
Products: inversion of anomeric configuration
Products: inversion of anomeric configuration
?
phenyl 4-O-beta-D-glucopyranosyl-D-glucopyranoside + H2O
phenyl beta-D-glucopyranoside + D-glucose
-
Substrates: 25% activity
Products: -
Products: -
?
phenyl beta-D-glucopyranoside + H2O
phenol + D-glucopyranose
-
Substrates: low activity
Products: -
Products: -
?
phenyl beta-D-xylopyranoside + H2O
phenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
phenyl beta-D-xylopyranoside + methanol
methyl beta-D-xylopyranoside + phenol
Penicillium wortmanni
-
Substrates: in the presence of 1 M methanol, transxylosylation activity
Products: -
Products: -
?
sophorose + H2O
?
-
Substrates: 19.9% activity compared to xylobiose
Products: -
Products: -
?
Xyl-beta-(1->4)-Xyl-beta-(1->4)-Xyl + H2O
3 D-xylose
-
Substrates: -
Products: -
Products: -
?
Xyl-beta-(1->4)-Xyl-beta-(1->4)-Xyl-beta-(1->4)-Xyl + H2O
4 D-xylose
-
Substrates: -
Products: -
Products: -
?
xylan + H2O
xylose
-
Substrates: lenzing xylan or wheat straw xylan
Products: -
Products: -
?
Xylbeta(1-2)Manbeta(1-4)GlcNAcbeta(1-4)[Fucalpha(1-3)]GlcNAc-pyridylaminoside + H2O
beta-D-xylose + Manbeta(1-4)GlcNAcbeta(1-4)[Fucalpha(1-3)]GlcNAc-pyridylaminoside
-
Substrates: complete hydrolysis
Products: -
Products: -
?
xylo-oligosaccharides + H2O
xylobiose + ?
-
Substrates: -
Products: major hydrolysis product
Products: major hydrolysis product
?
xylobiose + H2O
?
-
Substrates: and higher xylooligosaccharides
Products: -
Products: -
?
xylobiose + H2O
xylotriose + ?
-
Substrates: transxylosylation activity
Products: -
Products: -
?
xylooligosaccharide + H2O
beta-D-xylose + ?
Substrates: the enzyme hydrolyzes xylooligosaccharides, up to degree of polymerization 6, with higher activity towards longer xylooligosaccharide
Products: -
Products: -
?
xylopentaose + 4 H2O
5 D-xylose
Substrates: -
Products: -
Products: -
?
xylotetraose + H2O
xylotriose + D-xylose
-
Substrates: -
Products: -
Products: -
?
xylotriose + 2 H2O
3 beta-D-xylose
Substrates: -
Products: -
Products: -
?
[Manalpha(1-6)Manalpha(1-3)Xylbeta(1-2)]Manbeta(1-4)GlcNAcbeta(1-4)[Fucalpha(1-3)]GlcNAc-pyridylaminoside + H2O
beta-D-xylose + [Manalpha(1-6)Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)[Fucalpha(1-3)]GlcNAc-pyridylaminoside
-
Substrates: 50% hydrolysis
Products: -
Products: -
?
(xylooligosaccharide)n + H2O
(xylooligosaccharide)n-1 + D-xylose
Substrates: -
Products: -
Products: -
?
(xylooligosaccharide)n + H2O
(xylooligosaccharide)n-1 + D-xylose
-
Substrates: -
Products: -
Products: -
?
10-deacetyl-7-xylosyltaxol + H2O
10-deacetyl-taxol + D-xylose
Substrates: -
Products: -
Products: -
?
10-deacetyl-7-xylosyltaxol + H2O
10-deacetyl-taxol + D-xylose
Substrates: -
Products: -
Products: -
?
2,4-dinitrophenyl beta-D-xylopyranoside + H2O
2,4-dinitrophenol + beta-D-xylopyranose
Penicillium wortmanni
-
Substrates: -
Products: -
Products: -
?
2,4-dinitrophenyl beta-D-xylopyranoside + H2O
2,4-dinitrophenol + beta-D-xylopyranose
-
Substrates: broad tolerance for the aglycone portion of the substrate
Products: -
Products: -
?
2,4-dinitrophenyl-beta-D-xylopyranoside + H2O
2,4-dinitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
2,4-dinitrophenyl-beta-D-xylopyranoside + H2O
2,4-dinitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
2,5-dinitrophenyl-beta-D-xylopyranoside + H2O
2,5-dinitrophenol + D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
2,5-dinitrophenyl-beta-D-xylopyranoside + H2O
2,5-dinitrophenol + D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
2,5-dinitrophenyl-beta-D-xylopyranoside + H2O
2,5-dinitrophenol + D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
2,5-dinitrophenyl-beta-D-xylopyranoside + H2O
2,5-dinitrophenol + D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
2,5-dinitrophenyl-beta-D-xylopyranoside + H2O
2,5-dinitrophenol + D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
2-nitrophenyl beta-D-xylopyranoside + H2O
2-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
2-nitrophenyl beta-D-xylopyranoside + H2O
2-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
2-nitrophenyl beta-D-xylopyranoside + H2O
2-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
2-nitrophenyl beta-D-xylopyranoside + H2O
2-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
2-nitrophenyl beta-D-xylopyranoside + H2O
2-nitrophenol + D-xylose
-
Substrates: 3% of the activity with 4-nitrophenyl-alpha-L-arabinofuranoside
Products: -
Products: -
?
2-nitrophenyl beta-D-xylopyranoside + H2O
2-nitrophenol + D-xylose
Substrates: -
Products: -
Products: -
?
2-nitrophenyl beta-D-xylopyranoside + H2O
2-nitrophenol + D-xylose
Substrates: -
Products: -
Products: -
?
2-nitrophenyl beta-D-xylopyranoside + H2O
2-nitrophenol + D-xylose
-
Substrates: best substrate
Products: -
Products: -
?
3,4-dinitrophenyl beta-D-xylopyranoside + H2O
3,4-dinitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
3,4-dinitrophenyl beta-D-xylopyranoside + H2O
3,4-dinitrophenol + beta-D-xylopyranose
Substrates: -
Products: -
Products: -
?
3,4-dinitrophenyl beta-D-xylopyranoside + H2O
3,4-dinitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
3,4-dinitrophenyl beta-D-xylopyranoside + H2O
3,4-dinitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
3,4-dinitrophenyl beta-D-xylopyranoside + H2O
3,4-dinitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
3,4-dinitrophenyl beta-D-xylopyranoside + H2O
3,4-dinitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
4-chloro-2-nitrophenyl beta-D-xylopyranoside + H2O
4-chloro-2-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
4-chloro-2-nitrophenyl beta-D-xylopyranoside + H2O
4-chloro-2-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-alpha-L-arabinofuranoside + H2O
4-methylumbelliferol + alpha-L-arabinofuranose
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-alpha-L-arabinofuranoside + H2O
4-methylumbelliferol + alpha-L-arabinofuranose
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-beta-D-xylopyranoside + H2O
4-methylumbelliferol + beta-D-xylose
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-beta-D-xylopyranoside + H2O
4-methylumbelliferol + beta-D-xylose
Substrates: substrate inhibition
Products: -
Products: -
?
4-methylumbelliferyl-beta-D-xylopyranoside + H2O
4-methylumbelliferol + beta-D-xylose
Substrates: substrate inhibition
Products: -
Products: -
?
4-methylumbelliferyl-beta-D-xylopyranoside + H2O
4-methylumbelliferone + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-beta-D-xylopyranoside + H2O
4-methylumbelliferone + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-D-glucoside + H2O
4-nitrophenol + D-glucose
-
Substrates: 1.5% activity compared to 4-nitrophenyl beta-D-xyloside
Products: -
Products: -
?
4-nitrophenyl alpha-D-glucoside + H2O
4-nitrophenol + D-glucose
-
Substrates: 1.5% activity compared to 4-nitrophenyl beta-D-xyloside
Products: -
Products: -
?
4-nitrophenyl alpha-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-D-xylopyranoside + H2O
4-nitrophenol + D-xylopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-D-xylopyranoside + H2O
4-nitrophenol + D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
-
Substrates: activity is 20% compared to activity with 4-nitrophenyl-beta-D-xylopyranoside
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
Aspergillus niger ADH-11
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
Aspergillus niger DSM 22593
-
Substrates: activity is 20% compared to activity with 4-nitrophenyl-beta-D-xylopyranoside
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
Substrates: 38.5% of the activity with 4-nitrophenyl beta-D-xylopyranoside
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
Aureobasidium melanogenum ATCC 20524
Substrates: 38.5% of the activity with 4-nitrophenyl beta-D-xylopyranoside
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
-
Substrates: activity is lower compared to 4-nitrophenyl-beta-D-xylopyranoside
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
-
Substrates: activity is lower compared to 4-nitrophenyl-beta-D-xylopyranoside
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
Substrates: greater catalytic efficiency for hydrolysis of 4-nitrophenyl-alpha-L-arabinofuranoside than of 4-nitrophenyl-beta-D-xylopyranoside
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
Substrates: greater catalytic efficiency for hydrolysis of 4-nitrophenyl-alpha-L-arabinofuranoside than of 4-nitrophenyl-beta-D-xylopyranoside
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
Substrates: low activity
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
Irpex lacteus CD2
Substrates: low activity
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
Substrates: low activity
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
Rhizophlyctis rosea NBRC 105426
Substrates: low activity
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
-
Substrates: thermodynamic parameters for hydrolysis. Rate enhancement kcat/knon, increases with decreasing temperature
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
Substrates: low activity
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
Substrates: low activity
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
Substrates: poor substrate
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + L-arabinofuranose
-
Substrates: 14.4% activity compared to 4-nitrophenyl beta-D-xyloside
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + L-arabinofuranose
-
Substrates: 14.4% activity compared to 4-nitrophenyl beta-D-xyloside
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + L-arabinofuranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + L-arabinofuranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + L-arabinofuranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + L-arabinose
Substrates: 44.4% activity compared to 4-nitrophenyl beta-D-xyloside
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + L-arabinose
Substrates: 44.4% activity compared to 4-nitrophenyl beta-D-xyloside
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + L-arabinose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinopyranoside + H2O
4-nitrophenol + alpha-L-arabinopyranose
Substrates: -
Products: less than 2% activity with 4-nitrophenyl alpha-L-arabinopyranoside
Products: less than 2% activity with 4-nitrophenyl alpha-L-arabinopyranoside
?
4-nitrophenyl alpha-L-arabinopyranoside + H2O
4-nitrophenol + alpha-L-arabinopyranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinopyranoside + H2O
4-nitrophenol + alpha-L-arabinopyranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinopyranoside + H2O
4-nitrophenol + L-arabinopyranose
Substrates: 4.9% activity compared to 4-nitrophenyl beta-D-xyloside
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinopyranoside + H2O
4-nitrophenol + L-arabinopyranose
Substrates: 4.9% activity compared to 4-nitrophenyl beta-D-xyloside
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinopyranoside + H2O
4-nitrophenol + L-arabinopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinopyranoside + H2O
4-nitrophenol + L-arabinopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl alpha-L-arabinopyranoside + H2O
4-nitrophenol + L-arabinopyranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
-
Substrates: xylan-inducible enzyme shows 10% of activity with 4-nitrophenyl-beta-D-xylopyranoside, and xylose-inducible enzyme 2%
Products: -
Products: -
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + D-galactose
-
Substrates: 1.4% activity compared to 4-nitrophenyl beta-D-xyloside
Products: -
Products: -
?
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + D-galactose
-
Substrates: 1.4% activity compared to 4-nitrophenyl beta-D-xyloside
Products: -
Products: -
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
-
Substrates: activity is 20% compared to activity with 4-nitrophenyl-beta-D-xylopyranoside
Products: -
Products: -
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
Aspergillus niger ADH-11
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
Aspergillus niger DSM 22593
-
Substrates: activity is 20% compared to activity with 4-nitrophenyl-beta-D-xylopyranoside
Products: -
Products: -
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
-
Substrates: 11.1% activity compared to beta-D-xylopyranoside
Products: -
Products: -
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
Ceratocystis fimbriata RM 35
-
Substrates: 11.1% activity compared to beta-D-xylopyranoside
Products: -
Products: -
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
-
Substrates: 11.1% activity compared to beta-D-xylopyranoside
Products: -
Products: -
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
-
Substrates: activity is lower compared to 4-nitrophenyl-beta-D-xylopyranoside
Products: -
Products: -
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
-
Substrates: activity is lower compared to 4-nitrophenyl-beta-D-xylopyranoside
Products: -
Products: -
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
Substrates: xylan-inducible enzyme shows 18% of activity with 4-nitrophenyl-beta-D-xylopyranoside, and xylose-inducible enzyme 8%
Products: -
Products: -
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
Substrates: 9% of the activity with 4-nitrophenyl-alpha-L-arabinofuranoside
Products: -
Products: -
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4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
Substrates: low activity
Products: -
Products: -
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4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
Substrates: 23% of activity compared to p-nitrophenyl-beta-D-xylopyranoside
Products: -
Products: -
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4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
Substrates: 2.5% of the acticvity with p-nitrophenyl-beta-D-xylopyranoside
Products: -
Products: -
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4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
Substrates: activity is 11.1% compared to activity with 4-nitrophenyl-beta-D-xylopyranoside. The enzyme shows selectivity for beta configuration
Products: -
Products: -
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4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
Ceratocystis fimbriata RM 35
-
Substrates: activity is 11.1% compared to activity with 4-nitrophenyl-beta-D-xylopyranoside. The enzyme shows selectivity for beta configuration
Products: -
Products: -
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4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
Substrates: activity is 11.1% compared to activity with 4-nitrophenyl-beta-D-xylopyranoside. The enzyme shows selectivity for beta configuration
Products: -
Products: -
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4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + D-glucose
Substrates: 0.7% activity compared to 4-nitrophenyl beta-D-xyloside
Products: -
Products: -
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4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + D-glucose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + D-glucose
Substrates: 0.7% activity compared to 4-nitrophenyl beta-D-xyloside
Products: -
Products: -
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4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + D-glucose
-
Substrates: 9.6% activity compared to 4-nitrophenyl beta-D-xyloside
Products: -
Products: -
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4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + D-glucose
-
Substrates: 9.6% activity compared to 4-nitrophenyl beta-D-xyloside
Products: -
Products: -
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4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + D-glucose
Substrates: low activity
Products: -
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4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + D-glucose
Substrates: 25.9% activity compared to 4-nitrophenyl beta-D-xyloside
Products: -
Products: -
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4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + D-glucose
Substrates: 25.9% activity compared to 4-nitrophenyl beta-D-xyloside
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: preferred substrate of the purified enzyme
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: hydrolysis with overall retention of substrate anomeric configuration
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: hydrolysis with overall retention of substrate anomeric configuration
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
Aspergillus niger ADH-11
-
Substrates: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
Aspergillus niger DSM 22593
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
Aureobasidium melanogenum ATCC 20524
Substrates: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: substrate for isoform AbfA
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
Substrates: 100% activity
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
Substrates: 100% activity
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: 100% activity
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: the enzyme shows selectivity for beta configuration
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
Ceratocystis fimbriata RM 35
-
Substrates: 100% activity
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
Ceratocystis fimbriata RM 35
-
Substrates: the enzyme shows selectivity for beta configuration
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: 100% activity
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: the enzyme shows selectivity for beta configuration
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
Substrates: greater catalytic efficiency for hydrolysis of 4-nitrophenyl-alpha-L-arabinofuranoside than of 4-nitrophenyl-beta-D-xylopyranoside
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
Substrates: greater catalytic efficiency for hydrolysis of 4-nitrophenyl-alpha-L-arabinofuranoside than of 4-nitrophenyl-beta-D-xylopyranoside
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
Irpex lacteus CD2
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: 46% of the activity with 4-nitrophenyl-beta-D-glucopyranoside
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: low activity levels, measured in whole fly homogenates, substrate concentration of 60 mM in acetate phosphate buffer
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: highest activity
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: highest activity
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
Rhizophlyctis rosea NBRC 105426
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: thermodynamic parameters for hydrolysis. Rate enhancement kcat/knon, increases with decreasing temperature
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: highest activity
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
Weissella cibaria FB069
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
Substrates: preferred substrate, specific for, xylan-inducible enzyme and xylose-inducible enzyme
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
Substrates: 39.36% of the activitzy compared to 4-nitrophenyl beta-D-galactopyranoside
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
Substrates: specific for
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
Substrates: specific for
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
Substrates: 14% of the activity with 4-nitrophenyl-alpha-L-arabinofuranoside
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
Substrates: best substrate
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
Substrates: best substrate
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylopyranose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylopyranose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylose
Substrates: preferred substrate
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylose
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylose
Substrates: 29% of its beta-glucosidase activity against p-nitrophenyl-beta-D-glucopyranoside
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylose
Substrates: 21.1% relative activity compared to the beta-glucosidase activity with 4-nitrophenyl beta-D-glucopyranoside as substrate
Products: -
Products: -
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4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylose
Substrates: 15.7% relative activity compared to the beta-glucosidase activity with 4-nitrophenyl beta-D-glucopyranoside as substrate
Products: -
Products: -
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4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + beta-D-xylose
-
Substrates: the enzyme displays high catalytic activity (60%) in presence of 5-35% NaCl (w/v) or 1-20% ionic liquid (w/v) or 1-50 mM xylose
Products: -
Products: -
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4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + beta-D-xylose
Aureobasidium pullulans CBS 135684
-
Substrates: the enzyme displays high catalytic activity (60%) in presence of 5-35% NaCl (w/v) or 1-20% ionic liquid (w/v) or 1-50 mM xylose
Products: -
Products: -
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4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + beta-D-xylose
W0BU85
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + beta-D-xylose
Enterobacter ludwigii LY-62
W0BU85
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + beta-D-xylose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + beta-D-xylose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + beta-D-xylose
Substrates: the enzyme displays high catalytic activity (60%) in presence of 5-35% NaCl (w/v) or 1-20% ionic liquid (w/v) or 1-50 mM xylose
Products: -
Products: -
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4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + D-xylose
Substrates: 100% activity
Products: -
Products: -
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4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + D-xylose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + D-xylose
Substrates: 100% activity
Products: -
Products: -
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4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + D-xylose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + D-xylose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + D-xylose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + D-xylose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + D-xylose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + D-xylose
-
Substrates: 100% activity
Products: -
Products: -
?
4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + D-xylose
-
Substrates: 100% activity
Products: -
Products: -
?
4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + D-xylose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + D-xylose
Substrates: high activity
Products: -
Products: -
?
4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + D-xylose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + D-xylose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + D-xylose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + D-xylose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + D-xylose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + D-xylose
Substrates: -
Products: -
Products: -
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4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + D-xylose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + D-xylose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + D-xylose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + D-xylose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + D-xylose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + D-xylose
Shouchella clausii TCCC 11004
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + D-xylose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + D-xylose
A0A1L3GYC8
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-arabinofuranoside + H2O
4-nitrophenol + L-arabinofuranose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-arabinofuranoside + H2O
4-nitrophenol + L-arabinofuranose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-arabinofuranoside + H2O
4-nitrophenol + L-arabinofuranose
Shouchella clausii TCCC 11004
-
Substrates: -
Products: -
Products: -
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4-nitrophenyl-alpha-L-arabinopyranoside + H2O
4-nitrophenol + alpha-L-arabinose
-
Substrates: xylan-inducible enzyme shows 18% of activity with 4-nitrophenyl-beta-D-xylopyranoside, and xylose-inducible enzyme 26%
Products: -
Products: -
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4-nitrophenyl-alpha-L-arabinopyranoside + H2O
4-nitrophenol + alpha-L-arabinose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl-alpha-L-arabinopyranoside + H2O
4-nitrophenol + alpha-L-arabinose
-
Substrates: 46% of the activity with 4-nitrophenyl-alpha-L-arabinofuranoside
Products: -
Products: -
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astragaloside IV + H2O
cycloastragenol + D-xylose
Substrates: notoginsenoside ASI
Products: -
Products: -
?
astragaloside IV + H2O
cycloastragenol + D-xylose
Substrates: notoginsenoside ASI
Products: -
Products: -
?
astragaloside IV + H2O
cycloastragenol + D-xylose
Substrates: notoginsenoside ASI
Products: -
Products: -
?
astragaloside IV + H2O
cycloastragenol + D-xylose
Substrates: notoginsenoside ASI
Products: -
Products: -
?
beechwood xylan + H2O
?
-
Substrates: the purified enzyme acts synergistically with Aspergillus niger endo-1,4-beta-xylanase in the hydrolysis of beechwood xylan
Products: -
Products: -
?
beechwood xylan + H2O
?
Aspergillus niger DSM 22593
-
Substrates: the purified enzyme acts synergistically with Aspergillus niger endo-1,4-beta-xylanase in the hydrolysis of beechwood xylan
Products: -
Products: -
?
beechwood xylan + H2O
?
Substrates: 1.8% activity compared to 4-nitrophenyl alpha-D-xylopyranoside
Products: -
Products: -
?
beechwood xylan + H2O
D-xylose
Substrates: -
Products: -
Products: -
?
beechwood xylan + H2O
D-xylose
Substrates: 1% substrate solution
Products: -
Products: -
?
beechwood xylan + H2O
D-xylose
Substrates: -
Products: -
Products: -
?
beechwood xylan + H2O
D-xylose
Substrates: 1% substrate solution
Products: -
Products: -
?
beechwood xylan + H2O
xylobiose + ?
Substrates: -
Products: -
Products: -
?
benzyl-beta-D-xyloside + H2O
phenol + beta-D-xylose
-
Substrates: low activity
Products: -
Products: -
?
benzyl-beta-D-xyloside + H2O
phenol + beta-D-xylose
Penicillium wortmanni
-
Substrates: low activity for xylosidases-2,-3,-4, 45% activity for xylosidase-1
Products: -
Products: -
?
beta-1,4-xylan + H2O
beta-D-xylose + ?
-
Substrates: -
Products: -
Products: -
?
beta-1,4-xylan + H2O
beta-D-xylose + ?
-
Substrates: complete hydrolysis after prolonged incubation
Products: -
Products: -
?
birch arabinoxylan + H2O
D-xylose + ?
Substrates: -
Products: -
Products: -
?
birch arabinoxylan + H2O
D-xylose + ?
Substrates: -
Products: -
Products: -
?
birchwood xylan + H2O
D-xylose + ?
Substrates: -
Products: initial product, after prolonged hydrolysis, xylo-oligosaccharides are obeserved, too
Products: initial product, after prolonged hydrolysis, xylo-oligosaccharides are obeserved, too
?
birchwood xylan + H2O
D-xylose + ?
Substrates: -
Products: initial product, after prolonged hydrolysis, xylo-oligosaccharides are obeserved, too
Products: initial product, after prolonged hydrolysis, xylo-oligosaccharides are obeserved, too
?
butyl-beta-D-xyloside
butanol + beta-D-xylose
-
Substrates: low activity
Products: -
Products: -
?
butyl-beta-D-xyloside
butanol + beta-D-xylose
Penicillium wortmanni
-
Substrates: low activity
Products: -
Products: -
?
butyl-beta-D-xyloside
butanol + beta-D-xylose
-
Substrates: low activity
Products: -
Products: -
?
cyclohexyl-beta-D-xyloside + H2O
cyclohexanol + beta-D-xylose
-
Substrates: low activity
Products: -
Products: -
?
cyclohexyl-beta-D-xyloside + H2O
cyclohexanol + beta-D-xylose
Penicillium wortmanni
-
Substrates: 50% activity compared to that for xylobiose
Products: -
Products: -
?
cyclohexyl-beta-D-xyloside + H2O
cyclohexanol + beta-D-xylose
-
Substrates: low activity
Products: -
Products: -
?
epimedin B + H2O
icariin + D-xylose
Substrates: high activity, reaction method optimization for icariin production, overview
Products: -
Products: -
?
epimedin B + H2O
icariin + D-xylose
Substrates: high activity, reaction method optimization for icariin production, overview
Products: -
Products: -
?
ginsenoside Ra1 + H2O
ginsenoside Rb2 + D-xylose
Substrates: -
Products: -
Products: -
?
ginsenoside Ra1 + H2O
ginsenoside Rb2 + D-xylose
Substrates: 5.2% activity compared to 4-nitrophenyl beta-D-xylopyranoside
Products: -
Products: -
?
ginsenoside Ra1 + H2O
ginsenoside Rb2 + D-xylose
Substrates: -
Products: -
Products: -
?
ginsenoside Ra1 + H2O
ginsenoside Rb2 + D-xylose
Substrates: 5.2% activity compared to 4-nitrophenyl beta-D-xylopyranoside
Products: -
Products: -
?
ginsenoside Ra2 + H2O
ginsenoside Rc + D-xylose
Substrates: 4.2% activity compared to 4-nitrophenyl beta-D-xylopyranoside
Products: -
Products: -
?
ginsenoside Ra2 + H2O
ginsenoside Rc + D-xylose
Substrates: 4.2% activity compared to 4-nitrophenyl beta-D-xylopyranoside
Products: -
Products: -
?
ginsenoside Rb2 + H2O
ginsenoside Rd + alpha-L-arabinopyranose
-
Substrates: -
Products: -
Products: -
?
ginsenoside Rb2 + H2O
ginsenoside Rd + alpha-L-arabinopyranose
-
Substrates: -
Products: -
Products: -
?
ginsenoside Rc + H2O
ginsenoside Rd + alpha-L-arabinofuranose
-
Substrates: -
Products: -
Products: -
?
ginsenoside Rc + H2O
ginsenoside Rd + alpha-L-arabinofuranose
-
Substrates: -
Products: -
Products: -
?
hemicellulose xylogalacturonan + H2O
hemicellulose xylogalacturonan + beta-D-xylose
Substrates: the enzyme is involved in reduction of hemicellulose glycan polymers during fruit ripening
Products: -
Products: -
?
hemicellulose xylogalacturonan + H2O
hemicellulose xylogalacturonan + beta-D-xylose
Substrates: release of single beta-D-xylose monomer from the xylogalacturonan backbone of hemicellulose
Products: -
Products: -
?
kakkalide + H2O
kakkalidone + D-xylose
Substrates: -
Products: -
Products: -
?
kakkalide + H2O
kakkalidone + D-xylose
Substrates: -
Products: -
Products: -
?
methyl-beta-D-xyloside + H2O
?
Penicillium wortmanni
-
Substrates: very low activity
Products: -
Products: -
?
methyl-beta-D-xyloside + H2O
?
-
Substrates: very low activity
Products: -
Products: -
?
methyl-beta-D-xyloside + H2O
beta-D-xylose + methanol
-
Substrates: very low activity
Products: -
Products: -
?
methyl-beta-D-xyloside + H2O
beta-D-xylose + methanol
-
Substrates: -
Products: -
Products: -
?
methyl-beta-D-xyloside + H2O
beta-D-xylose + methanol
Penicillium wortmanni
-
Substrates: very low activity
Products: -
Products: -
?
methyl-beta-D-xyloside + H2O
beta-D-xylose + methanol
-
Substrates: -
Products: -
Products: -
?
methyl-beta-D-xyloside + H2O
beta-D-xylose + methanol
-
Substrates: very low activity
Products: -
Products: -
?
notoginsenoside R1 + H2O
?
Substrates: hydrolysis of a beta-1,2-glycosidic bond. Notoginsenoside-R1 binding in DtXyl active site, docking and modelling, molecular dynamics, overview
Products: -
Products: -
?
notoginsenoside R1 + H2O
?
Substrates: hydrolysis of a beta-1,2-glycosidic bond. Notoginsenoside-R1 binding in DtXyl active site, docking and modelling, molecular dynamics, overview
Products: -
Products: -
?
notoginsenoside R1 + H2O
?
Substrates: hydrolysis of a beta-1,2-glycosidic bond. Notoginsenoside-R1 binding in DtXyl active site, docking and modelling, molecular dynamics, overview
Products: -
Products: -
?
notoginsenoside R1 + H2O
?
Substrates: hydrolysis of a beta-1,2-glycosidic bond. Notoginsenoside-R1 binding in DtXyl active site, docking and modelling, molecular dynamics, overview
Products: -
Products: -
?
notoginsenoside R1 + H2O
ginsenoside Rg1 + D-xylose
Substrates: -
Products: -
Products: -
?
notoginsenoside R1 + H2O
ginsenoside Rg1 + D-xylose
Substrates: high activity
Products: -
Products: -
?
notoginsenoside R1 + H2O
ginsenoside Rg1 + D-xylose
Substrates: -
Products: -
Products: -
?
notoginsenoside R1 + H2O
ginsenoside Rg1 + D-xylose
Substrates: high activity
Products: -
Products: -
?
notoginsenoside R1 + H2O
ginsenoside Rg1 + D-xylose
Substrates: -
Products: -
Products: -
?
notoginsenoside R1 + H2O
ginsenoside Rg1 + D-xylose
Substrates: high activity
Products: -
Products: -
?
notoginsenoside R1 + H2O
ginsenoside Rg1 + D-xylose
Substrates: -
Products: -
Products: -
?
notoginsenoside R1 + H2O
ginsenoside Rg1 + D-xylose
Substrates: high activity
Products: -
Products: -
?
notoginsenoside R1 + H2O
ginsenoside Rg1 + D-xylose
-
Substrates: -
Products: -
Products: -
?
notoginsenoside R1 + H2O
ginsenoside Rg1 + D-xylose
-
Substrates: complete conversion within 4 h
Products: -
Products: -
?
notoginsenoside R2 + H2O
ginsenoside Rh1 + D-xylose
-
Substrates: -
Products: -
Products: -
?
notoginsenoside R2 + H2O
ginsenoside Rh1 + D-xylose
-
Substrates: complete conversion within 18 h
Products: -
Products: -
?
o-chlorophenyl beta-D-xyloside + H2O
o-chlorophenol + beta-D-xylose
-
Substrates: -
Products: -
Products: -
?
o-chlorophenyl beta-D-xyloside + H2O
o-chlorophenol + beta-D-xylose
-
Substrates: -
Products: -
Products: -
?
o-methoxyphenyl beta-D-xyloside
o-methoxyphenol + beta-D-xylose
-
Substrates: -
Products: -
Products: -
?
o-methoxyphenyl beta-D-xyloside
o-methoxyphenol + beta-D-xylose
-
Substrates: -
Products: -
Products: -
?
o-methylphenyl beta-D-xyloside + H2O
o-methylphenol + beta-D-xylose
-
Substrates: -
Products: -
Products: -
?
o-methylphenyl beta-D-xyloside + H2O
o-methylphenol + beta-D-xylose
-
Substrates: -
Products: -
Products: -
?
o-nitrophenyl beta-D-xylopyranoside + H2O
o-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
o-nitrophenyl beta-D-xylopyranoside + H2O
o-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
o-nitrophenyl beta-D-xylopyranoside + H2O
o-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
o-nitrophenyl beta-D-xylopyranoside + H2O
o-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
o-nitrophenyl beta-D-xylopyranoside + H2O
o-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
o-nitrophenyl beta-D-xylopyranoside + H2O
o-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
o-nitrophenyl-beta-D-xylopyranoside + H2O
o-nitrophenol + beta-D-xylopyranose
-
Substrates: 9% of activity compared to p-nitrophenyl-beta-D-xylopyranoside
Products: -
Products: -
?
o-nitrophenyl-beta-D-xylopyranoside + H2O
o-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
o-nitrophenyl-beta-D-xylopyranoside + H2O
o-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
o-nitrophenyl-beta-D-xyloside + H2O
o-nitrophenol + beta-D-xylose
-
Substrates: -
Products: -
Products: -
?
o-nitrophenyl-beta-D-xyloside + H2O
o-nitrophenol + beta-D-xylose
-
Substrates: -
Products: -
Products: -
?
p-methoxyphenyl beta-D-xyloside + H2O
p-methoxyphenol + beta-D-xylose
-
Substrates: -
Products: -
Products: -
?
p-methoxyphenyl beta-D-xyloside + H2O
p-methoxyphenol + beta-D-xylose
-
Substrates: -
Products: -
Products: -
?
p-methylphenyl beta-D-xyloside + H2O
p-methylphenol + beta-D-xylose
-
Substrates: -
Products: -
Products: -
?
p-methylphenyl beta-D-xyloside + H2O
p-methylphenol + beta-D-xylose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl alpha-L-arabinofuranoside + H2O
p-nitrophenol + alpha-L-arabinofuranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl alpha-L-arabinofuranoside + H2O
p-nitrophenol + alpha-L-arabinofuranose
-
Substrates: low activity
Products: -
Products: -
?
p-nitrophenyl alpha-L-arabinofuranoside + H2O
p-nitrophenol + alpha-L-arabinofuranose
-
Substrates: highest activity
Products: -
Products: -
?
p-nitrophenyl alpha-L-arabinofuranoside + H2O
p-nitrophenol + alpha-L-arabinofuranose
-
Substrates: low affinity, 70% activity of that for p-nitrophenyl beta-D-xylopyranose
Products: -
Products: -
?
p-nitrophenyl alpha-L-arabinopyranoside + H2O
p-nitrophenol + alpha-L-arabinopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl alpha-L-arabinopyranoside + H2O
p-nitrophenol + alpha-L-arabinopyranose
Penicillium wortmanni
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl alpha-L-arabinopyranoside + H2O
p-nitrophenol + alpha-L-arabinopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl alpha-L-arabinopyranoside + H2O
p-nitrophenol + alpha-L-arabinopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
-
Substrates: activity after immobililization on alumina or silica
Products: -
Products: -
?
p-nitrophenyl beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
-
Substrates: high activity
Products: -
Products: -
?
p-nitrophenyl beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
-
Substrates: activity depends on carbon source, on which cells are grown
Products: -
Products: -
?
p-nitrophenyl beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
Penicillium wortmanni
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
-
Substrates: more rapidly hydrolyzed than o-nitrophenyl beta-D-xylopyranoside
Products: -
Products: -
?
p-nitrophenyl beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
-
Substrates: high specificity, transxylosylation activity
Products: -
Products: -
?
p-nitrophenyl beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-xyloside + H2O
p-nitrophenol + beta-D-xylose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-xyloside + H2O
p-nitrophenol + beta-D-xylose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-xyloside + H2O
p-nitrophenol + beta-D-xylose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-xyloside + H2O
p-nitrophenol + beta-D-xylose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-xyloside + H2O
p-nitrophenol + beta-D-xylose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-xyloside + H2O
p-nitrophenol + beta-D-xylose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-xyloside + H2O
p-nitrophenol + beta-D-xylose
Malbranchea pulchella var. sulfurea
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-xyloside + H2O
p-nitrophenol + beta-D-xylose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-xyloside + H2O
p-nitrophenol + beta-D-xylose
Penicillium wortmanni
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-xyloside + H2O
p-nitrophenol + beta-D-xylose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-xyloside + H2O
p-nitrophenol + beta-D-xylose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-xyloside + H2O
p-nitrophenol + beta-D-xylose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl beta-D-xyloside + H2O
p-nitrophenol + beta-D-xylose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
Phlebia radiata 79 / ATCC 64658
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
r
phenyl beta-D-xyloside + H2O
phenol + beta-D-xylose
-
Substrates: with retention of configuration
Products: -
Products: -
?
phenyl beta-D-xyloside + H2O
phenol + beta-D-xylose
Malbranchea pulchella var. sulfurea
-
Substrates: -
Products: -
Products: -
?
phenyl beta-D-xyloside + H2O
phenol + beta-D-xylose
-
Substrates: with retention of configuration
Products: -
Products: -
?
phenyl-beta-D-xylopyranoside + H2O
phenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
phenyl-beta-D-xylopyranoside + H2O
phenol + beta-D-xylopyranose
-
Substrates: -
Products: -
Products: -
?
poplar sawdust xylan + H2O
xylooligosaccharides + D-xylose
Substrates: the enzyme beta-xylosidase catalyzes the hydrolysis of poplar sawdust xylan with recombinant endo-1,4-beta-xylanase MxynB-8 leading to production of xylooligosaccharides and D-xylose
Products: -
Products: -
?
poplar sawdust xylan + H2O
xylooligosaccharides + D-xylose
Substrates: the enzyme beta-xylosidase catalyzes the hydrolysis of poplar sawdust xylan with recombinant endo-1,4-beta-xylanase MxynB-8 leading to production of xylooligosaccharides and D-xylose. Optimized conditions are 50°C, pH 6.0, dosage of 500 U/g enzyme, substrate concentration of 2 mg/ml
Products: -
Products: -
?
poplar sawdust xylan + H2O
xylooligosaccharides + D-xylose
Substrates: the enzyme beta-xylosidase catalyzes the hydrolysis of poplar sawdust xylan with recombinant endo-1,4-beta-xylanase MxynB-8 leading to production of xylooligosaccharides and D-xylose
Products: -
Products: -
?
poplar sawdust xylan + H2O
xylooligosaccharides + D-xylose
Substrates: the enzyme beta-xylosidase catalyzes the hydrolysis of poplar sawdust xylan with recombinant endo-1,4-beta-xylanase MxynB-8 leading to production of xylooligosaccharides and D-xylose. Optimized conditions are 50°C, pH 6.0, dosage of 500 U/g enzyme, substrate concentration of 2 mg/ml
Products: -
Products: -
?
rye arabinoxylan + H2O
?
Substrates: 1% substrate solution
Products: -
Products: -
?
rye arabinoxylan + H2O
?
Substrates: 1% substrate solution
Products: -
Products: -
?
sagittatoside B + H2O
? + D-xylose
Substrates: -
Products: -
Products: -
?
vinasse + H2O
D-xylose + ?
-
Substrates: by-product of ethanol fermentation
Products: 12.1% release of xylose by enzyme alone, combination of enzyme and the multicomponent enzyme product Ultraflo L results in 41.9% release of xylose
Products: 12.1% release of xylose by enzyme alone, combination of enzyme and the multicomponent enzyme product Ultraflo L results in 41.9% release of xylose
?
vinasse + H2O
D-xylose + ?
Substrates: -
Products: hydrolysis by an enzyme cocktail containing a 20%:20%:20%:40% mixture and a 25%:25%:25%:25% mixture, respectively, of the GH43 alpha-L-arabinofuranosidase from Humicola insolens, the GH51 alpha-L-arabinofuranosidase from M. giganteus, a GH10 endo-1,4-beta-xylanase from H. insolens, and a GH3 beta-xylosidase from Trichoderma reesei
Products: hydrolysis by an enzyme cocktail containing a 20%:20%:20%:40% mixture and a 25%:25%:25%:25% mixture, respectively, of the GH43 alpha-L-arabinofuranosidase from Humicola insolens, the GH51 alpha-L-arabinofuranosidase from M. giganteus, a GH10 endo-1,4-beta-xylanase from H. insolens, and a GH3 beta-xylosidase from Trichoderma reesei
?
vinasse + H2O
D-xylose + ?
-
Substrates: by-product of ethanol fermentation
Products: 7.7% release of xylose by enzyme alone, combination of enzyme and the multicomponent enzyme product Ultraflo L results in 40.8% relaese of xylose
Products: 7.7% release of xylose by enzyme alone, combination of enzyme and the multicomponent enzyme product Ultraflo L results in 40.8% relaese of xylose
?
wheat arabinoxylan + H2O
D-xylose + ?
Substrates: -
Products: hydrolysis by an enzyme cocktail containing a 20%:20%:20%:40% mixture and a 25%:25%:25%:25% mixture, respectively, of the GH43 alpha-L-arabinofuranosidase from Humicola insolens, the GH51 alpha-L-arabinofuranosidase from M. giganteus, a GH10 endo-1,4-beta-xylanase from H. insolens, and a GH3 beta-xylosidase from Trichoderma reesei
Products: hydrolysis by an enzyme cocktail containing a 20%:20%:20%:40% mixture and a 25%:25%:25%:25% mixture, respectively, of the GH43 alpha-L-arabinofuranosidase from Humicola insolens, the GH51 alpha-L-arabinofuranosidase from M. giganteus, a GH10 endo-1,4-beta-xylanase from H. insolens, and a GH3 beta-xylosidase from Trichoderma reesei
?
xylan + H2O
?
Substrates: 0.4% activity compared to 4-nitrophenyl beta-D-xylopyranoside
Products: -
Products: -
?
xylan + H2O
?
Substrates: 0.4% activity compared to 4-nitrophenyl beta-D-xylopyranoside
Products: -
Products: -
?
xylan + H2O
?
-
Substrates: from corncob, complete hydrolysis to beta-D-xylose in concert with xylanase
Products: -
Products: -
?
xylan + H2O
beta-D-xylose
Substrates: from oat spelt or birchwood, low activity
Products: -
Products: -
?
xylan + H2O
beta-D-xylose
Substrates: from oat spelt or birchwood, low activity
Products: -
Products: -
?
xylan + H2O
beta-D-xylose + ?
-
Substrates: traces of xylanase activity
Products: -
Products: -
?
xylan + H2O
beta-D-xylose + ?
-
Substrates: when combining this beta-xylosidase with xylanase from the same Aureobasidium pullulans strain, the rate of black liquor xylan hydrolysis is significantly improved by up to 1.6fold
Products: -
Products: -
?
xylan + H2O
beta-D-xylose + ?
Aureobasidium pullulans CBS 135684
-
Substrates: when combining this beta-xylosidase with xylanase from the same Aureobasidium pullulans strain, the rate of black liquor xylan hydrolysis is significantly improved by up to 1.6fold
Products: -
Products: -
?
xylan + H2O
beta-D-xylose + ?
Substrates: low levels of activity on commercial xylan were also observed, mainly on the soluble fraction
Products: -
Products: -
?
xylan + H2O
beta-D-xylose + ?
-
Substrates: complete degration of xylan requires synergistic action of two types of enzyme, endo-1,4-xylanase to form xylooligosaccharides and beta-D-xylosidase, which hydrolyses xylooligosaccharides to xylose
Products: -
Products: -
?
xylan + H2O
beta-D-xylose + ?
Malbranchea pulchella var. sulfurea
-
Substrates: -
Products: -
Products: -
?
xylan + H2O
beta-D-xylose + ?
Malbranchea pulchella var. sulfurea
-
Substrates: low activity
Products: -
Products: -
?
xylan + H2O
beta-D-xylose + ?
-
Substrates: complete degration of xylan requires synergistic action of two types of enzyme, endo-1,4-xylanase to form xylooligosaccharides and beta-D-xylosidase, which hydrolyses xylooligosaccharides to xylose
Products: -
Products: -
?
xylan + H2O
beta-D-xylose + ?
-
Substrates: complete degration of xylan requires synergistic action of two types of enzyme, endo-1,4-xylanase to form xylooligosaccharides and beta-D-xylosidase, which hydrolyses xylooligosaccharides to xylose
Products: -
Products: -
?
xylan + H2O
beta-D-xylose + ?
-
Substrates: low activity
Products: -
Products: -
?
xylan + H2O
beta-D-xylose + ?
-
Substrates: complete degration of xylan requires synergistic action of two types of enzyme, endo-1,4-xylanase to form xylooligosaccharides and beta-D-xylosidase, which hydrolyses xylooligosaccharides to xylose
Products: -
Products: -
?
xylan + H2O
beta-D-xylose + ?
-
Substrates: source of substrate: beechwood. Incubation with enzyme gives 32.8% hydrolysis in 4 h, hydrolysis by enzyme combined with xylanase from Anoxybacillus flavithermus BC gives 63.6% conversion after 4 h
Products: -
Products: -
?
xylan + H2O
beta-D-xylose + ?
Saccharolobus solfataricus Oalpha
-
Substrates: source of substrate: beechwood. Incubation with enzyme gives 32.8% hydrolysis in 4 h, hydrolysis by enzyme combined with xylanase from Anoxybacillus flavithermus BC gives 63.6% conversion after 4 h
Products: -
Products: -
?
xylan + H2O
beta-D-xylose + ?
-
Substrates: limited capability to produce xylose due to synergistic action of xylanase and beta-xylosidase, synergistic action also needed for libration of acidic substituents
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
-
Substrates: -
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
-
Substrates: derived from xylan
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
-
Substrates: -
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
-
Substrates: derived from xylan
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
-
Substrates: decrease of activity with increasing polymerization of substrates
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
-
Substrates: derived from xylan
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
-
Substrates: -
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
-
Substrates: beta-xylosidase A
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
-
Substrates: derived from xylan
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
-
Substrates: derived from xylan
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
-
Substrates: high transferase activity
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
Penicillium wortmanni
-
Substrates: operating by a double-inversion mechanism
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
-
Substrates: derived from xylan
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
-
Substrates: -
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
-
Substrates: derived from xylan
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
-
Substrates: -
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
-
Substrates: smaller xylooligosaccharides from 2-5mers less rapidly hydrolyzed
Products: -
Products: -
?
xylobiose + H2O
2 beta-D-xylopyranose
Substrates: 30.8% of the activity with 4-nitrophenyl beta-D-xylopyranoside
Products: -
Products: -
?
xylobiose + H2O
2 beta-D-xylopyranose
Aureobasidium melanogenum ATCC 20524
Substrates: 30.8% of the activity with 4-nitrophenyl beta-D-xylopyranoside
Products: -
Products: -
?
xylobiose + H2O
2 beta-D-xylose
Substrates: -
Products: -
Products: -
?
xylobiose + H2O
2 beta-D-xylose
-
Substrates: -
Products: hydrolysis via retention of anomeric configuration
Products: hydrolysis via retention of anomeric configuration
?
xylobiose + H2O
2 beta-D-xylose
Substrates: -
Products: -
Products: -
?
xylobiose + H2O
2 beta-D-xylose
Substrates: 25% of the activity with 4-nitrophenyl beta-D-xylopyranoside
Products: -
Products: -
?
xylobiose + H2O
2 beta-D-xylose
-
Substrates: -
Products: -
Products: -
r
xylobiose + H2O
2 beta-D-xylose
-
Substrates: -
Products: hydrolysis via retention of anomeric configuration
Products: hydrolysis via retention of anomeric configuration
?
xylobiose + H2O
2 D-xylose
-
Substrates: the enzyme is highly active on xylobiose
Products: -
Products: -
?
xylobiose + H2O
2 D-xylose
Substrates: 0.4% activity compared to 4-nitrophenyl beta-D-xyloside
Products: -
Products: -
?
xylobiose + H2O
2 D-xylose
Substrates: -
Products: -
Products: -
?
xylobiose + H2O
2 D-xylose
-
Substrates: best substrate
Products: -
Products: -
?
xylobiose + H2O
2 D-xylose
Substrates: -
Products: -
Products: -
?
xylobiose + H2O
beta-D-xylose + D-xylose
-
Substrates: transxylosylation activity
Products: -
Products: -
?
xylobiose + H2O
beta-D-xylose + D-xylose
-
Substrates: -
Products: -
Products: -
?
xylobiose + H2O
beta-D-xylose + D-xylose
-
Substrates: 90% degradation within 6 to 9 h
Products: -
Products: -
?
xylobiose + H2O
beta-D-xylose + D-xylose
-
Substrates: transxylosylation activity
Products: -
Products: -
?
xylobiose + H2O
beta-D-xylose + D-xylose
-
Substrates: most rapidly hydrolyzed
Products: -
Products: -
?
xylobiose + H2O
beta-D-xylose + D-xylose
-
Substrates: -
Products: -
Products: -
?
xylobiose + H2O
beta-D-xylose + D-xylose
-
Substrates: -
Products: -
Products: -
?
xylobiose + H2O
beta-D-xylose + D-xylose
Malbranchea pulchella var. sulfurea
-
Substrates: -
Products: -
Products: -
?
xylobiose + H2O
beta-D-xylose + D-xylose
Malbranchea pulchella var. sulfurea
-
Substrates: without forming any xylooligosaccharides
Products: -
Products: -
?
xylobiose + H2O
beta-D-xylose + D-xylose
Penicillium wortmanni
-
Substrates: transxylosylation activity
Products: -
Products: -
?
xylobiose + H2O
beta-D-xylose + D-xylose
Penicillium wortmanni
-
Substrates: four isoenzymes divided into three groups of action patterns
Products: -
Products: -
?
xylobiose + H2O
beta-D-xylose + D-xylose
-
Substrates: -
Products: -
Products: -
?
xylobiose + H2O
beta-D-xylose + D-xylose
-
Substrates: -
Products: -
Products: -
?
xylobiose + H2O
beta-D-xylose + D-xylose
-
Substrates: -
Products: -
Products: -
?
xylobiose + H2O
beta-D-xylose + D-xylose
-
Substrates: -
Products: -
Products: -
?
xylobiose + H2O
beta-D-xylose + D-xylose
-
Substrates: -
Products: -
Products: -
?
xylobiose + H2O
D-xylose
Substrates: high activity
Products: -
Products: -
?
xylobiose + H2O
D-xylose
Substrates: -
Products: -
Products: -
?
xylobiose + H2O
D-xylose
Substrates: high activity
Products: -
Products: -
?
xylobiose + H2O
D-xylose
Substrates: -
Products: -
Products: -
?
xylobiose + H2O
D-xylose
Substrates: high activity
Products: -
Products: -
?
xylobiose + H2O
D-xylose
Substrates: high activity
Products: -
Products: -
?
xylohexaose + H2O
6 D-xylose
Substrates: -
Products: predominant release of xylose
Products: predominant release of xylose
?
xylohexaose + H2O
6 D-xylose
Substrates: -
Products: predominant release of xylose
Products: predominant release of xylose
?
xylohexaose + H2O
6 D-xylose
Substrates: sole products released are xylose monomers
Products: -
Products: -
?
xylohexaose + H2O
beta-D-xylose
-
Substrates: 80% of the activity with xylobiose
Products: -
Products: -
r
xylohexaose + H2O
xylose + ?
-
Substrates: compared to xylobiose, relative rate of xylose release is 74%
Products: -
Products: -
?
xylohexaose + H2O
xylose + ?
-
Substrates: compared to xylobiose, relative rate of xylose release is 74%
Products: -
Products: -
?
xylopentaose + H2O
5 D-xylose
Substrates: -
Products: -
Products: -
?
xylopentaose + H2O
5 D-xylose
Substrates: sole products released are xylose monomers
Products: -
Products: -
?
xylopentaose + H2O
beta-D-xylose
-
Substrates: 83% of the activity with xylobiose
Products: -
Products: -
r
xylopentaose + H2O
beta-D-xylose + ?
Malbranchea pulchella var. sulfurea
-
Substrates: -
Products: -
Products: -
?
xylopentaose + H2O
beta-D-xylose + ?
-
Substrates: extend of hydrolysis varies with chain length of the substrate
Products: -
Products: -
?
xylopentaose + H2O
beta-D-xylose + ?
-
Substrates: lower activity than on xylobiose
Products: -
Products: -
?
xylopentaose + H2O
beta-D-xylose + ?
-
Substrates: -
Products: -
Products: -
?
xylopentaose + H2O
xylose + ?
-
Substrates: compared to xylobiose, relative rate of xylose release is 75%
Products: -
Products: -
?
xylopentaose + H2O
xylose + ?
-
Substrates: compared to xylobiose, relative rate of xylose release is 75%
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xylotetraose + 3 H2O
4 D-xylose
Substrates: -
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xylotetraose + 3 H2O
4 xylose
-
Substrates: compared to xylobiose, relative rate of xylose release is 81%
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xylotetraose + 3 H2O
4 xylose
-
Substrates: compared to xylobiose, relative rate of xylose release is 81%
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xylotetraose + H2O
4 D-xylose
Substrates: -
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xylotetraose + H2O
xylotriose + beta-D-xylose
Substrates: -
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xylotetraose + H2O
xylotriose + beta-D-xylose
-
Substrates: no transferase activity
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xylotetraose + H2O
xylotriose + beta-D-xylose
-
Substrates: -
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xylotetraose + H2O
xylotriose + beta-D-xylose
-
Substrates: 20-30% degradation after 16 h
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xylotetraose + H2O
xylotriose + beta-D-xylose
-
Substrates: -
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xylotetraose + H2O
xylotriose + beta-D-xylose
Substrates: -
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xylotetraose + H2O
xylotriose + beta-D-xylose
Substrates: -
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xylotetraose + H2O
xylotriose + beta-D-xylose
Malbranchea pulchella var. sulfurea
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Substrates: -
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xylotetraose + H2O
xylotriose + beta-D-xylose
-
Substrates: -
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xylotetraose + H2O
xylotriose + beta-D-xylose
-
Substrates: acts by inverting the anomeric configuration
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xylotetraose + H2O
xylotriose + beta-D-xylose
-
Substrates: -
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xylotetraose + H2O
xylotriose + beta-D-xylose
Substrates: 21% of the activity with 4-nitrophenyl beta-D-xylopyranoside
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xylotetraose + H2O
xylotriose + beta-D-xylose
-
Substrates: 86% of the activity with xylobiose
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xylotetraose + H2O
xylotriose + beta-D-xylose
-
Substrates: -
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xylotetraose + H2O
xylotriose + beta-D-xylose
-
Substrates: -
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xylotriose + 2 H2O
3 beta-D-xylopyranose
Substrates: 32.8% of the activity with 4-nitrophenyl beta-D-xylopyranoside
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xylotriose + 2 H2O
3 beta-D-xylopyranose
Aureobasidium melanogenum ATCC 20524
Substrates: 32.8% of the activity with 4-nitrophenyl beta-D-xylopyranoside
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xylotriose + 2 H2O
3 D-xylose
Substrates: about 12.1% of the activity with 4-nitrophenyl beta-D-xylopyranoside
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xylotriose + 2 H2O
3 D-xylose
-
Substrates: 92% of the activity with xylobiose
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xylotriose + 2 H2O
3 xylose
-
Substrates: compared to xylobiose, relative rate of xylose release is 90%
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xylotriose + 2 H2O
3 xylose
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Substrates: compared to xylobiose, relative rate of xylose release is 90%
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xylotriose + H2O
3 D-xylose
Substrates: -
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xylotriose + H2O
beta-D-xylose + xylobiose
-
Substrates: -
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xylotriose + H2O
beta-D-xylose + xylobiose
-
Substrates: 70-80% degradation after 16 h
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xylotriose + H2O
beta-D-xylose + xylobiose
-
Substrates: -
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xylotriose + H2O
beta-D-xylose + xylobiose
-
Substrates: also transxylosylation activity to xylotetraose
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xylotriose + H2O
beta-D-xylose + xylobiose
Malbranchea pulchella var. sulfurea
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Substrates: -
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xylotriose + H2O
beta-D-xylose + xylobiose
-
Substrates: -
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xylotriose + H2O
beta-D-xylose + xylobiose
-
Substrates: -
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xylotriose + H2O
xylobiose + D-xylose
-
Substrates: 100% activity compared to xylobiose
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xylotriose + H2O
xylobiose + D-xylose
Substrates: -
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additional information
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Substrates: no detectable alpha-L-arabinofuranosidase, alpha- and beta-D-glucosidase activities are observed. The enzyme hydrolyzes xylooligomers into xylose and catalyzes transxylosilation reactions also in presence of alcohols as acceptors, producing xylo-oligosaccharides and alkyl-xylosides
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Substrates: xylotriose is a poor substrate
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Substrates: xylotriose is a poor substrate
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additional information
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Substrates: xylotriose is a poor substrate, the bifunctional enzyme shows two catalytic activities: alpha-L-arabinofuranosidase and beta-D-xylosidase activities
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Substrates: xylotriose is a poor substrate, the bifunctional enzyme shows two catalytic activities: alpha-L-arabinofuranosidase and beta-D-xylosidase activities
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Substrates: the enzyme also performs transxylosylation reactions producing xylopentaose, xylotetraose, and xylotriose from xylobiose and xylose, the enzyme is active with various acceptors, e.g. alcohols, sugar alcohols, phenols, hydroxybenzylalcohols, and disaccharides, detailed overview
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additional information
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-
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Substrates: no substrate: 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl-alpha-D-glucopyranoside, 4-nitrophenyl-beta-D-xylopyranoside
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additional information
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Substrates: the enzyme also performs transxylosylation reactions producing xylopentaose, xylotetraose, and xylotriose from xylobiose and xylose, the enzyme is active with various acceptors, e.g. alcohols, sugar alcohols, phenols, hydroxybenzylalcohols, and disaccharides, detailed overview
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additional information
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Substrates: the enzyme also performs transxylosylation reactions producing xylopentaose, xylotetraose, and xylotriose from xylobiose and xylose, the enzyme is active with various acceptors, e.g. alcohols, sugar alcohols, phenols, hydroxybenzylalcohols, and disaccharides, detailed overview
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additional information
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Substrates: no substrate: 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl-alpha-D-glucopyranoside, 4-nitrophenyl-beta-D-xylopyranoside
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additional information
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Substrates: the beta-xylosidase exhibits synergism with endoxylanase upon hydrolysis of glucuronoxylan as well as with alpha-L-arabinofuranosidase and endoxylanase upon hydrolysis of arabinoxylan. Addition of beta-xylosidases increases efficiency of hydrolysis of plant raw materials with high hemicellulose content such as maize cobs by the enzymic preparation Celloviridine G20x depleted of its own beta-xylosidase
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Substrates: no substrate: xyloglucan
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Substrates: during hydrolysis of pretreated straw lignocellulose at 70 °C using a commercial lignocellulosic enzyme cocktail, inclusion of the purified enzyme results in a 19fold increase in the amount of xylose produced after 6 h. No activity is detected on 4-nitrophenyl beta-D-cellobioside
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Substrates: use of different enzyme activity detection methods, overview. 1H-NMR experiments are performed to determine the anomeric configuration of the reaction products of the wild-type AnBX and the E88A and E500A mutants with 4-nitrophenyl beta-D-xyloside in the presence of sodium azide
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Aspergillus niger DSM 22593
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Substrates: during hydrolysis of pretreated straw lignocellulose at 70 °C using a commercial lignocellulosic enzyme cocktail, inclusion of the purified enzyme results in a 19fold increase in the amount of xylose produced after 6 h. No activity is detected on 4-nitrophenyl beta-D-cellobioside
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additional information
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Substrates: no substrate: 4-nitrophenyl-beta-D-xylopyranoside, 4-nitrophenyl-alpha-D-galactopyranoside, 4-nitrophenyl-alpha-L-arabinofuranoside, 4-nitrophenyl-alpha-L-arabinopyranoside, 4-nitrophenyl-beta-L-arabinopyranoside, 4-nitrophenyl-beta-D-galactopyranoside, 4-nitrophenyl-beta-D-glucopyranoside and 4-nitrophenyl-beta-D-mannopyranoside
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additional information
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Substrates: no substrate: 4-nitrophenyl-beta-D-xylopyranoside, 4-nitrophenyl-alpha-D-galactopyranoside, 4-nitrophenyl-alpha-L-arabinofuranoside, 4-nitrophenyl-alpha-L-arabinopyranoside, 4-nitrophenyl-beta-L-arabinopyranoside, 4-nitrophenyl-beta-D-galactopyranoside, 4-nitrophenyl-beta-D-glucopyranoside and 4-nitrophenyl-beta-D-mannopyranoside
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additional information
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Substrates: no substrate: 4-nitrophenyl-alpha-D-xylopyranoside, 4-nitrophenyl-beta-D-glucopyranoside, 4-nitrophenyl-alpha-D-glucopyranoside, 4-nitrophenyl-beta-D-galactopyranoside, 4-nitrophenyl-alpha-D-galactopyranoside, 4-nitrophenyl-alpha-L-arabinopyranoside, cellobiose, oat spelt xylan, birch wood xylan, carboxymethyl cellulose, avicel, and soluble starch
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additional information
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Aureobasidium melanogenum ATCC 20524
Substrates: no substrate: 4-nitrophenyl-alpha-D-xylopyranoside, 4-nitrophenyl-beta-D-glucopyranoside, 4-nitrophenyl-alpha-D-glucopyranoside, 4-nitrophenyl-beta-D-galactopyranoside, 4-nitrophenyl-alpha-D-galactopyranoside, 4-nitrophenyl-alpha-L-arabinopyranoside, cellobiose, oat spelt xylan, birch wood xylan, carboxymethyl cellulose, avicel, and soluble starch
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additional information
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Substrates: enzyme activity detection via thin layer chromatography (TLC) and 3,5-dinitrosalicylic acid (DNS) method. Enzyme rHJ14GH43 also exhibits low activity against 4-nitrophenyl-alpha-L-arabinofuranoside. The enzyme hydrolyses xylooligosaccharides, yielding xylose as the end product. But certain substrates, including birchwood xylan, beechwood xylan, arabinoxylan, carboxymethyl cellulose sodium salt, pullulan, and barley beta-glucan, cannot be degraded by rHJ14GH43
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additional information
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Substrates: the enzyme does not act on 4-nitrophenyl alpha-L-arabinofuranoside, 4-nitrophenyl beta-D-glucopyranoside, or 4-nitrophenyl beta-D-fucopyranoside
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additional information
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Substrates: the enzyme does not act on 4-nitrophenyl alpha-L-arabinofuranoside, 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-fucopyranoside, 4-nitrophenyl alpha-D-glucopyranoside, 4-nitrophenyl beta-D-glucopyranoside, maltose, cellobiose, ginsenoside Rb2, and ginsenoside Rc
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additional information
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Substrates: substrate specificity BbXyL, the enzyme exhibits only xylosidase activity. No activity with 4-nitrophenyl-alpha-L-arabinopyranoside, 4-nitrophenyl-beta-D-galactopyranoside, 4-nitrophenyl-alpha-L-rhamnopyranoside, 4-nitrophenyl-beta-D-glucopyranoside, and astragaloside A, and also no activity with icariin, poor activity with notoginsenoside R1 (beta-1,2-glycodie hydrolysis) and 4-nitrophenyl-alpha-L-arabinofuranoside
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additional information
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Substrates: the enzyme does not act on 4-nitrophenyl alpha-L-arabinofuranoside, 4-nitrophenyl beta-D-glucopyranoside, or 4-nitrophenyl beta-D-fucopyranoside
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additional information
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Substrates: the enzyme does not act on 4-nitrophenyl alpha-L-arabinofuranoside, 4-nitrophenyl beta-D-glucopyranoside, or 4-nitrophenyl beta-D-fucopyranoside
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additional information
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Substrates: the enzyme does not act on 4-nitrophenyl alpha-L-arabinofuranoside, 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-fucopyranoside, 4-nitrophenyl alpha-D-glucopyranoside, 4-nitrophenyl beta-D-glucopyranoside, maltose, cellobiose, ginsenoside Rb2, and ginsenoside Rc
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additional information
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-
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Substrates: the enzyme does not act on 4-nitrophenyl alpha-L-arabinofuranoside, 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-fucopyranoside, 4-nitrophenyl alpha-D-glucopyranoside, 4-nitrophenyl beta-D-glucopyranoside, maltose, cellobiose, ginsenoside Rb2, and ginsenoside Rc
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additional information
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Substrates: substrate specificity BbXyL, the enzyme exhibits only xylosidase activity. No activity with 4-nitrophenyl-alpha-L-arabinopyranoside, 4-nitrophenyl-beta-D-galactopyranoside, 4-nitrophenyl-alpha-L-rhamnopyranoside, 4-nitrophenyl-beta-D-glucopyranoside, and astragaloside A, and also no activity with icariin, poor activity with notoginsenoside R1 (beta-1,2-glycodie hydrolysis) and 4-nitrophenyl-alpha-L-arabinofuranoside
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additional information
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Substrates: no activity to 4-nitrophenyl beta-D-glucopyranoside or 4-nitrophenyl-beta-D-mannopyranoside. Based on fragment sequences of the enzyme detected by tandem mass spectrometry and their identical hits from other plant species the purified enzyme is a beta-xylosidase
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additional information
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Substrates: no activity with gentiobiose, cellobiose, and cellotriose
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additional information
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Substrates: no activity with 4-nitrophenyl alpha -L-arabinopyranoside, 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl alpha-D-glucopyranoside, 4-nitrophenyl alpha-D-mannopyranoside, or 4-nitrophenyl beta-D-mannopyranoside
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additional information
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Ceratocystis fimbriata RM 35
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Substrates: no activity with 4-nitrophenyl alpha -L-arabinopyranoside, 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl alpha-D-glucopyranoside, 4-nitrophenyl alpha-D-mannopyranoside, or 4-nitrophenyl beta-D-mannopyranoside
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additional information
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-
Substrates: no activity with 4-nitrophenyl alpha -L-arabinopyranoside, 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl alpha-D-glucopyranoside, 4-nitrophenyl alpha-D-mannopyranoside, or 4-nitrophenyl beta-D-mannopyranoside
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additional information
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Substrates: no substrate: p-nitrophenyl-alpha-L-rhamnopyranoside, p-nitrophenyl-alpha-D-xylopyranoside
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additional information
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-
-
Substrates: no activity towards 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl alpha-L-arabinofuranoside, 4-nitrophenyl alpha-L-rhamnopyranoside or 2-nitrophenyl beta-D-glucopyranoside
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additional information
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Substrates: product identification by TLC. No activity with 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl alpha-L-arabinofuranoside, 4-nitrophenyl alpha-L-arabinopyranoside, and 4-nitrophenyl alpha-L-rhamnopyranoside
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additional information
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-
-
Substrates: no activity towards 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl alpha-L-arabinofuranoside, 4-nitrophenyl alpha-L-rhamnopyranoside or 2-nitrophenyl beta-D-glucopyranoside
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additional information
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Substrates: no activity with 4-nitrophenyl alpha-L-rhamnopyranoside
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additional information
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Substrates: no substrate: xylan
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additional information
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Substrates: 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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additional information
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Substrates: no activity with 4-nitrophenyl beta-D-glucopyranoside 4-nitrophenyl beta-D-galactopyranoside, debranched arabinan (sugar beet), arabinan (sugar beet), rye arabinoxylan (high viscosity), wheat flour arabinoxylan, xylan (beechwood), rhamnogalacturonan I (potato), xyloglucan (tamarind), barley beta-glucan (low viscosity), and carob galactomannan (low viscosity). Poor activity with 4-nitrophenyl alpha-L-arabinofuranoside
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additional information
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Substrates: enzyme has transxylosylation activity leading to formation of O-glycosidic linkages as in 4-nitrophenyl-3-O-beta-D-xylopyranosyl-beta-D-xylopyranoside, 4-nitrophenyl-2-O-beta-D-xylopyranosyl-beta-D-xylopyranoside, 4-nitrophenyl-(4-O-beta-D-xylopyranosyl-2-O-beta-D-xylopyranosyl)-beta-D-xylopyranoside from substrate 4-nitrophenyl-beta-D-xylopyranoside. Compared to xylobiose, xylotriose is a better donor molecule for XylB-mediated transxylosylation of primary alcohols presenting chain length from 1- to 5-carbon atoms
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additional information
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Substrates: recombinant XylRBM26 exhibits beta-xylosidase and alpha-L-arabinofuranosidase activities. XylRBM26 is a bifunctional of beta-D-xylosidase/alpha-L-arabinofuranosidase. No activity with arabinobiose, arabinotriose, and arabinotetraose
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Substrates: enzyme is implicated in cell wall turnover of arabinose and xylose
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additional information
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Substrates: cleavage of beta-1,4-linked D-xylo-oligosaccharides and alpha-1,5-linked L-arabino-oligosaccharides. Xylan from oat spelt is not a substrate
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additional information
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Substrates: specific enzyme, no activity with 4-nitrophenyl-beta-D-galactopyranoside, 4-nitrophenyl-alpha-L-arabinopyranoside, 2-nitrophenyl-beta-D-galactopyranoside, carboxymethyl-cellulose, avicel, or xylan
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additional information
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Substrates: no substrate: 4-nitrophenyl-alpha-L-arabinofuranoside
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additional information
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Substrates: specific enzyme, no activity with 4-nitrophenyl-beta-D-galactopyranoside, 4-nitrophenyl-alpha-L-arabinopyranoside, 2-nitrophenyl-beta-D-galactopyranoside, carboxymethyl-cellulose, avicel, or xylan
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additional information
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Substrates: the enzyme is active on beechwood xylan and arabinoxylan from wheat
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additional information
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Substrates: enzyme shows exo-beta-xylanase EC 3.2.1.37, endoxylanase EC 3.2.1.8 and alpha-L-arabinofuranosidase EC 3.2.1.55 activities
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additional information
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Substrates: enzyme shows exo-beta-xylanase EC 3.2.1.37, endoxylanase EC 3.2.1.8 and alpha-L-arabinofuranosidase EC 3.2.1.55 activities
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additional information
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Substrates: recombinant PxXyl43A exhibits hydrolysis activity against both 4-nitrophenyl beta-D-xylopyranoside and 4-nitrophenyl alpha-L-arabinofuranoside at specific activities of 250 and 310 mU/mg, respectively. With xylooligosaccharides as substrates, the enzyme shows activity with xylobiose and xylose is released as a product of PxXyl43A after 2 h reaction with incresing activity every hour. When xylotriose is used as a substrate, xylose is released slowly and detected after 4 h reaction. On the other hand, when xylotetraose, xylopentaose, and xylohexaose are used as substrates, no reaction products are detected. These results suggest that PxXyl43A is an exo-acting enzyme which releases xylose from small xylooligosaccharides up to DP 3. PxXyl43A shows activity with both 4-nitrophenyl beta-D-xylopyranoside and 4-nitrophenyl alpha-L-arabinofuranoside, but not for 4-nitrophenyl beta-D-glucopyranoside and 4-nitrophenyl beta-D-galactopyranoside. The specific activity for 4-nitrophenyl alpha-L-arabinofuranoside is slightly higher than the activity for 4-nitrophenyl beta-D-xylopyranoside. PxXyl43A is a GH43 enzyme that acts on both pNPX and pNPAf, but does not show hydrolytic activity for pNPGal and pNPG, similar to most other reported GH43 enzymes
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additional information
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Substrates: recombinant PxXyl43A exhibits hydrolysis activity against both 4-nitrophenyl beta-D-xylopyranoside and 4-nitrophenyl alpha-L-arabinofuranoside at specific activities of 250 and 310 mU/mg, respectively. With xylooligosaccharides as substrates, the enzyme shows activity with xylobiose and xylose is released as a product of PxXyl43A after 2 h reaction with incresing activity every hour. When xylotriose is used as a substrate, xylose is released slowly and detected after 4 h reaction. On the other hand, when xylotetraose, xylopentaose, and xylohexaose are used as substrates, no reaction products are detected. These results suggest that PxXyl43A is an exo-acting enzyme which releases xylose from small xylooligosaccharides up to DP 3. PxXyl43A shows activity with both 4-nitrophenyl beta-D-xylopyranoside and 4-nitrophenyl alpha-L-arabinofuranoside, but not for 4-nitrophenyl beta-D-glucopyranoside and 4-nitrophenyl beta-D-galactopyranoside. The specific activity for 4-nitrophenyl alpha-L-arabinofuranoside is slightly higher than the activity for 4-nitrophenyl beta-D-xylopyranoside. PxXyl43A is a GH43 enzyme that acts on both pNPX and pNPAf, but does not show hydrolytic activity for pNPGal and pNPG, similar to most other reported GH43 enzymes
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additional information
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Substrates: no activity with 4-nitrophenyl-beta-D-glucopyranoside, 4-nitrophenyl-L-arabinofuranoside, 4-nitrophenyl-D-cellobioside, sugarcane bagasse xylan, corncob xylan, beechwood xylan, glucan, mannan, polygalactose and arabinan
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additional information
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Substrates: no activity with 4-nitrophenyl-beta-D-glucopyranoside, 4-nitrophenyl-L-arabinofuranoside, 4-nitrophenyl-D-cellobioside, sugarcane bagasse xylan, corncob xylan, beechwood xylan, glucan, mannan, polygalactose and arabinan
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additional information
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Substrates: no activity with 4-nitrophenyl-beta-D-glucopyranoside, 4-nitrophenyl-L-arabinofuranoside, 4-nitrophenyl-D-cellobioside, sugarcane bagasse xylan, corncob xylan, beechwood xylan, glucan, mannan, polygalactose and arabinan
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additional information
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Substrates: no activity with 4-nitrophenyl-beta-D-glucopyranoside, 4-nitrophenyl-L-arabinofuranoside, 4-nitrophenyl-D-cellobioside, sugarcane bagasse xylan, corncob xylan, beechwood xylan, glucan, mannan, polygalactose and arabinan
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additional information
?
-
Substrates: alpha-L-arabinofuranosidase activity is about 10% of the beta-xylosidase activity. No substrates: 4-nitrophenyl-alpha-D-xylopyranoside, 4-nitrophenyl-beta-D-glucopyranoside. Very poor substrates: birchwood xylan, beechwood xylan, sugar beet arabinan, debranched arabinana, wheat arabinoxylan
Products: -
Products: -
?
additional information
?
-
-
Substrates: alpha-L-arabinofuranosidase activity is about 10% of the beta-xylosidase activity. No substrates: 4-nitrophenyl-alpha-D-xylopyranoside, 4-nitrophenyl-beta-D-glucopyranoside. Very poor substrates: birchwood xylan, beechwood xylan, sugar beet arabinan, debranched arabinana, wheat arabinoxylan
Products: -
Products: -
?
additional information
?
-
Substrates: no substrates: 4-nitrophenyl-beta-D-glucopyranoside, 4-nitrophenyl-alpha-D-xylopyranoside, 4-nitrophenyl-alpha-L-arabinofuranoside, 4-nitrophenyl-alpha-D-mannopyranoside, 4-nitrophenyl-beta-D-mannoside, carboxymethylcellulose, barley glucan, glucomannan, laminarin. Very poor substrates: xyloglucan, locust bean gum, xylans. Enzyme can perform transglycosylation of xylose and alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme hydrolyses alkali-catalyzed glycerol pretreated lignocellulose in corncob and sugarcane bagasse at 85°C for 6h
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme hydrolyses alkali-catalyzed glycerol pretreated lignocellulose in corncob and sugarcane bagasse at 85°C for 6h
Products: -
Products: -
-
additional information
?
-
-
Substrates: no activity with 4-nitrophenyl beta-glucopyranoside and 4-nitrophenyl alpha-L-arabinopyranoside
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with 4-nitrophenyl beta-glucopyranoside and 4-nitrophenyl alpha-L-arabinopyranoside
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: cellulose, starch, maltose, cellobiose
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme hydrolysates wheat and rice straw, corn stover, corncob and sugarcane bagasse producing D-xylose when combined with beta-xylanase (EC 3.2.1.8). To study the impact of enzymes on hydrolyzing substrate for producing xylose, rXYLO and XynG1-1 are reacted with the alkali-extracted xylan from agro-industrial residues at pH 8.0 and 50°C for 8 h
Products: -
Products: -
-
additional information
?
-
-
Substrates: recombinant XYLO is an enzyme with the bifunctional activities of beta-xylosidase and alpha-L-arabinofuranosidase, which can degrade arabinose to reduce its influence on the endo-xylanase activity
Products: -
Products: -
-
additional information
?
-
Shouchella clausii TCCC 11004
-
Substrates: the enzyme hydrolysates wheat and rice straw, corn stover, corncob and sugarcane bagasse producing D-xylose when combined with beta-xylanase (EC 3.2.1.8). To study the impact of enzymes on hydrolyzing substrate for producing xylose, rXYLO and XynG1-1 are reacted with the alkali-extracted xylan from agro-industrial residues at pH 8.0 and 50°C for 8 h
Products: -
Products: -
-
additional information
?
-
Shouchella clausii TCCC 11004
-
Substrates: recombinant XYLO is an enzyme with the bifunctional activities of beta-xylosidase and alpha-L-arabinofuranosidase, which can degrade arabinose to reduce its influence on the endo-xylanase activity
Products: -
Products: -
-
additional information
?
-
Substrates: no activity with 4-nitrophenyl beta-D-glucopyranoside, 2-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl alpha-D-glucopyranoside, 4-nitrophenyl alpha-L-rhamnopyranoside, 4-nitrophenyl beta-D-galactopyranoside, and 4-nitrophenyl beta-D-fucopyranoside
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with 4-nitrophenyl beta-D-glucopyranoside, 2-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl alpha-D-glucopyranoside, 4-nitrophenyl alpha-L-rhamnopyranoside, 4-nitrophenyl beta-D-galactopyranoside, and 4-nitrophenyl beta-D-fucopyranoside
Products: -
Products: -
?
additional information
?
-
Substrates: less than 2% activity with 4-nitrophenyl alpha-L-arabinopyranoside, 2-nitrophenyl beta-D-xylopyranoside, 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-mannopyranoside, 4-nitrophenyl alpha-D-glucopyranoside, 4-nitrophenyl beta-D-fucopyranoside, 4-nitrophenyl alpha-D-galactopyranoside, and 4-nitrophenyl beta-D-galctopyranoside. Only small amounts of xylose are released from oligosaccharides. Smaller oligosaccharides are produced when xylotriose through xylopentaose are used as substrates, suggesting a possible xylobiohydrolase activity. No transglycosylation is detected
Products: -
Products: -
?
additional information
?
-
-
Substrates: less than 2% activity with 4-nitrophenyl alpha-L-arabinopyranoside, 2-nitrophenyl beta-D-xylopyranoside, 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-mannopyranoside, 4-nitrophenyl alpha-D-glucopyranoside, 4-nitrophenyl beta-D-fucopyranoside, 4-nitrophenyl alpha-D-galactopyranoside, and 4-nitrophenyl beta-D-galctopyranoside. Only small amounts of xylose are released from oligosaccharides. Smaller oligosaccharides are produced when xylotriose through xylopentaose are used as substrates, suggesting a possible xylobiohydrolase activity. No transglycosylation is detected
Products: -
Products: -
?
additional information
?
-
Substrates: less than 2% activity with 4-nitrophenyl alpha-L-arabinopyranoside, 2-nitrophenyl beta-D-xylopyranoside, 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-mannopyranoside, 4-nitrophenyl alpha-D-glucopyranoside, 4-nitrophenyl beta-D-fucopyranoside, 4-nitrophenyl alpha-D-galactopyranoside, and 4-nitrophenyl beta-D-galctopyranoside. Only small amounts of xylose are released from oligosaccharides. Smaller oligosaccharides are produced when xylotriose through xylopentaose are used as substrates, suggesting a possible xylobiohydrolase activity. No transglycosylation is detected
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme produces beta-xylose from beta-xylopyranosides while retaining the anomeric configuration of the xylose in the substrate. Enzyme shows transglycosylation activities in the presence of alcohols as acceptors. No substrate: 4-nitrophenyl-alpha-L-arabinofuranoside, 4-nitrophenyl-alpha-D-xylopyranoside, 4-nitrophenyl-alpha-D-glucopyranoside, and 4-nitrophenyl-beta-D-glucopyranoside, oat spelt xylan, birch wood xylan, or carboxymethyl cellulose
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme produces beta-xylose from beta-xylopyranosides while retaining the anomeric configuration of the xylose in the substrate. Enzyme shows transglycosylation activities in the presence of alcohols as acceptors. No substrate: 4-nitrophenyl-alpha-L-arabinofuranoside, 4-nitrophenyl-alpha-D-xylopyranoside, 4-nitrophenyl-alpha-D-glucopyranoside, and 4-nitrophenyl-beta-D-glucopyranoside, oat spelt xylan, birch wood xylan, or carboxymethyl cellulose
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is only active for notoginsenosides R1 and R2 amongst various ginsenosides
Products: -
Products: -
-
additional information
?
-
Substrates: no activity is found for beechwood xylan and cellobiose
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity is found for beechwood xylan and cellobiose
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme activity is quantified using the 3,5-dinitrosalicylic acid (DNS) reagent method by measuring absorbance at 535 nm in addition to assays measuring 4-nitrophenol absorbance measured at 405 nm
Products: -
Products: -
-
additional information
?
-
Substrates: enzyme activity is quantified using the 3,5-dinitrosalicylic acid (DNS) reagent method by measuring absorbance at 535 nm in addition to assays measuring 4-nitrophenol absorbance measured at 405 nm
Products: -
Products: -
-
additional information
?
-
-
Substrates: enzyme cleaves beta-1,4-linked xylo-oligosaccharides with chain length from 2 to 6, releasing xylose from the non-reducing end. When using high donor concentration, the enzyme catalyses the condensation reaction. No substrate: xylan
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl alpha-L-rhamnopyranoside, 2-nitrophenyl beta-D-glucopyranoside
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: xylan, beta-mannan, carboxymethyl cellulose, filter paper, 4-nitrophenyl-beta-D-glucopyranoside
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme hydrolyses glycosidic linkages of beta-1,4-xylooligosaccharides, but is also active with 4-nitrophenyl-alpha-L-arabinofuranoside
Products: -
Products: -
?
additional information
?
-
-
Substrates: the beta-xylosidase exhibits synergism with endoxylanase upon hydrolysis of glucuronoxylan as well as with alpha-L-arabinofuranosidase and endoxylanase upon hydrolysis of arabinoxylan. Addition of beta-xylosidases increases efficiency of hydrolysis of plant raw materials with high hemicellulose content such as maize cobs by the enzymic preparation Celloviridine G20x depleted of its own beta-xylosidase
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: xyloglucan
Products: -
Products: -
?
additional information
?
-
A0A1L3GYC8
Substrates: XYL21 has a wide substrate specificity to catalyze xylan and xylo-oligosaccharides, and it significantly cooperates with xylanase to improve the hydrolysis efficiency with 1.52fold
Products: -
Products: -
-
additional information
?
-
Substrates: the hydrolysis of xylooligosaccharide substrates is investigated using an endoxylanase-coupled assay, functions synergistically to promote the degradation of hemicellulosic xylans
Products: -
Products: -
?
additional information
?
-
Substrates: RuBG3A or RuBG3B alone do not release any reducing sugars from xylan. The addition of each enzyme into the reaction mixture of xylanase XynR8 improves the liberation of reducing sugars. The addition of RuBG3A with an activity ratio of 10:1 (xylosidase/xylanase) increases the liberation to 218% of that in the presence of XynR8 alone
Products: -
Products: -
?
additional information
?
-
Substrates: RuBG3A or RuBG3B alone do not release any reducing sugars from xylan. The addition of each enzyme into the reaction mixture of xylanase XynR8 improves the liberation of reducing sugars. The addition of RuBG3A with an activity ratio of 10:1 (xylosidase/xylanase) increases the liberation to 218% of that in the presence of XynR8 alone
Products: -
Products: -
?
additional information
?
-
Substrates: RuBG3A or RuBG3B alone do not release any reducing sugars from xylan. The addition of each enzyme into the reaction mixture of xylanase XynR8 improves the liberation of reducing sugars. The addition of RuBG3B with an activity ratio of 5:1 (xylosidase/xylanase) increases the liberation to 169% of that in the presence of XynR8 alone. RuBG3B shows no synergism with xylanase XynR8 at the optimal pH 7.5, but at pH 5.5, indicating that RuBG3B may have different pH preferences between aryl xylosidic substrate 4-nitrophenyl-beta-D-xylopyranoside and xylooligisaccharide xylan
Products: -
Products: -
?
additional information
?
-
Substrates: RuBG3A or RuBG3B alone do not release any reducing sugars from xylan. The addition of each enzyme into the reaction mixture of xylanase XynR8 improves the liberation of reducing sugars. The addition of RuBG3B with an activity ratio of 5:1 (xylosidase/xylanase) increases the liberation to 169% of that in the presence of XynR8 alone. RuBG3B shows no synergism with xylanase XynR8 at the optimal pH 7.5, but at pH 5.5, indicating that RuBG3B may have different pH preferences between aryl xylosidic substrate 4-nitrophenyl-beta-D-xylopyranoside and xylooligisaccharide xylan
Products: -
Products: -
?
additional information
?
-
Substrates: no substrate: 4-nitrophenly-beta-D-glucopyranoside. When incubated in combination with bifunctional xylanase-ferulic acid esterase Xyn10D-Fae1A, Xyl3A improves the release of xylose monomers from a hemicellulosic xylan substrate, suggesting that these two enzymes function synergistically to depolymerize xylan
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(xylooligosaccharide)n + H2O
(xylooligosaccharide)n-1 + D-xylose
-
Substrates: -
Products: -
Products: -
?
beta-1,3-xylan + H2O
beta-D-xylose + ?
-
Substrates: complete hydrolysis after prolonged incubation
Products: -
Products: -
?
hemicellulose xylogalacturonan + H2O
hemicellulose xylogalacturonan + beta-D-xylose
Substrates: the enzyme is involved in reduction of hemicellulose glycan polymers during fruit ripening
Products: -
Products: -
?
notoginsenoside R2 + H2O
ginsenoside Rh1 + D-xylose
-
Substrates: -
Products: -
Products: -
?
xylobiose + H2O
xylotriose + ?
-
Substrates: transxylosylation activity
Products: -
Products: -
?
astragaloside IV + H2O
cycloastragenol + D-xylose
Substrates: notoginsenoside ASI
Products: -
Products: -
?
astragaloside IV + H2O
cycloastragenol + D-xylose
Substrates: notoginsenoside ASI
Products: -
Products: -
?
astragaloside IV + H2O
cycloastragenol + D-xylose
Substrates: notoginsenoside ASI
Products: -
Products: -
?
astragaloside IV + H2O
cycloastragenol + D-xylose
Substrates: notoginsenoside ASI
Products: -
Products: -
?
beechwood xylan + H2O
D-xylose
Substrates: -
Products: -
Products: -
?
beechwood xylan + H2O
D-xylose
Substrates: -
Products: -
Products: -
?
beta-1,4-xylan + H2O
beta-D-xylose + ?
-
Substrates: -
Products: -
Products: -
?
beta-1,4-xylan + H2O
beta-D-xylose + ?
-
Substrates: complete hydrolysis after prolonged incubation
Products: -
Products: -
?
ginsenoside Ra1 + H2O
ginsenoside Rb2 + D-xylose
Substrates: -
Products: -
Products: -
?
ginsenoside Ra1 + H2O
ginsenoside Rb2 + D-xylose
Substrates: -
Products: -
Products: -
?
notoginsenoside R1 + H2O
ginsenoside Rg1 + D-xylose
Substrates: -
Products: -
Products: -
?
notoginsenoside R1 + H2O
ginsenoside Rg1 + D-xylose
Substrates: -
Products: -
Products: -
?
notoginsenoside R1 + H2O
ginsenoside Rg1 + D-xylose
Substrates: -
Products: -
Products: -
?
notoginsenoside R1 + H2O
ginsenoside Rg1 + D-xylose
Substrates: -
Products: -
Products: -
?
notoginsenoside R1 + H2O
ginsenoside Rg1 + D-xylose
-
Substrates: -
Products: -
Products: -
?
xylan + H2O
beta-D-xylose + ?
-
Substrates: traces of xylanase activity
Products: -
Products: -
?
xylan + H2O
beta-D-xylose + ?
-
Substrates: complete degration of xylan requires synergistic action of two types of enzyme, endo-1,4-xylanase to form xylooligosaccharides and beta-D-xylosidase, which hydrolyses xylooligosaccharides to xylose
Products: -
Products: -
?
xylan + H2O
beta-D-xylose + ?
Malbranchea pulchella var. sulfurea
-
Substrates: -
Products: -
Products: -
?
xylan + H2O
beta-D-xylose + ?
Malbranchea pulchella var. sulfurea
-
Substrates: low activity
Products: -
Products: -
?
xylan + H2O
beta-D-xylose + ?
-
Substrates: complete degration of xylan requires synergistic action of two types of enzyme, endo-1,4-xylanase to form xylooligosaccharides and beta-D-xylosidase, which hydrolyses xylooligosaccharides to xylose
Products: -
Products: -
?
xylan + H2O
beta-D-xylose + ?
-
Substrates: complete degration of xylan requires synergistic action of two types of enzyme, endo-1,4-xylanase to form xylooligosaccharides and beta-D-xylosidase, which hydrolyses xylooligosaccharides to xylose
Products: -
Products: -
?
xylan + H2O
beta-D-xylose + ?
-
Substrates: low activity
Products: -
Products: -
?
xylan + H2O
beta-D-xylose + ?
-
Substrates: complete degration of xylan requires synergistic action of two types of enzyme, endo-1,4-xylanase to form xylooligosaccharides and beta-D-xylosidase, which hydrolyses xylooligosaccharides to xylose
Products: -
Products: -
?
xylan + H2O
beta-D-xylose + ?
-
Substrates: limited capability to produce xylose due to synergistic action of xylanase and beta-xylosidase, synergistic action also needed for libration of acidic substituents
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
-
Substrates: -
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
-
Substrates: derived from xylan
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
-
Substrates: -
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
-
Substrates: derived from xylan
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
-
Substrates: decrease of activity with increasing polymerization of substrates
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
-
Substrates: derived from xylan
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
-
Substrates: -
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
-
Substrates: beta-xylosidase A
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
-
Substrates: derived from xylan
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
-
Substrates: derived from xylan
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
-
Substrates: high transferase activity
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
Penicillium wortmanni
-
Substrates: operating by a double-inversion mechanism
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
-
Substrates: derived from xylan
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
-
Substrates: -
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
-
Substrates: derived from xylan
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
-
Substrates: -
Products: -
Products: -
?
xylo-oligosaccharides + H2O
beta-D-xylose + ?
-
Substrates: smaller xylooligosaccharides from 2-5mers less rapidly hydrolyzed
Products: -
Products: -
?
xylobiose + H2O
beta-D-xylose + D-xylose
-
Substrates: transxylosylation activity
Products: -
Products: -
?
xylobiose + H2O
beta-D-xylose + D-xylose
-
Substrates: -
Products: -
Products: -
?
xylobiose + H2O
beta-D-xylose + D-xylose
-
Substrates: 90% degradation within 6 to 9 h
Products: -
Products: -
?
xylobiose + H2O
beta-D-xylose + D-xylose
-
Substrates: transxylosylation activity
Products: -
Products: -
?
xylobiose + H2O
beta-D-xylose + D-xylose
-
Substrates: most rapidly hydrolyzed
Products: -
Products: -
?
xylobiose + H2O
beta-D-xylose + D-xylose
-
Substrates: -
Products: -
Products: -
?
xylobiose + H2O
beta-D-xylose + D-xylose
-
Substrates: -
Products: -
Products: -
?
xylobiose + H2O
beta-D-xylose + D-xylose
Malbranchea pulchella var. sulfurea
-
Substrates: -
Products: -
Products: -
?
xylobiose + H2O
beta-D-xylose + D-xylose
Malbranchea pulchella var. sulfurea
-
Substrates: without forming any xylooligosaccharides
Products: -
Products: -
?
xylobiose + H2O
beta-D-xylose + D-xylose
Penicillium wortmanni
-
Substrates: transxylosylation activity
Products: -
Products: -
?
xylobiose + H2O
beta-D-xylose + D-xylose
Penicillium wortmanni
-
Substrates: four isoenzymes divided into three groups of action patterns
Products: -
Products: -
?
xylobiose + H2O
beta-D-xylose + D-xylose
-
Substrates: -
Products: -
Products: -
?
xylobiose + H2O
beta-D-xylose + D-xylose
-
Substrates: -
Products: -
Products: -
?
xylobiose + H2O
beta-D-xylose + D-xylose
-
Substrates: -
Products: -
Products: -
?
xylobiose + H2O
beta-D-xylose + D-xylose
-
Substrates: -
Products: -
Products: -
?
xylobiose + H2O
beta-D-xylose + D-xylose
-
Substrates: -
Products: -
Products: -
?
xylobiose + H2O
D-xylose
Substrates: -
Products: -
Products: -
?
xylobiose + H2O
D-xylose
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is implicated in cell wall turnover of arabinose and xylose
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme hydrolysates wheat and rice straw, corn stover, corncob and sugarcane bagasse producing D-xylose when combined with beta-xylanase (EC 3.2.1.8). To study the impact of enzymes on hydrolyzing substrate for producing xylose, rXYLO and XynG1-1 are reacted with the alkali-extracted xylan from agro-industrial residues at pH 8.0 and 50°C for 8 h
Products: -
Products: -
-
additional information
?
-
Shouchella clausii TCCC 11004
-
Substrates: the enzyme hydrolysates wheat and rice straw, corn stover, corncob and sugarcane bagasse producing D-xylose when combined with beta-xylanase (EC 3.2.1.8). To study the impact of enzymes on hydrolyzing substrate for producing xylose, rXYLO and XynG1-1 are reacted with the alkali-extracted xylan from agro-industrial residues at pH 8.0 and 50°C for 8 h
Products: -
Products: -
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
CaCl2
Co2+
CoCl2
CuCl2
D-fructose
D-glucose
D-xylose
Fe2+
Fe3+
K+
Mg2+
MgCl2
Mn2+
MnCl2
Na+
NaCl
NiCl2
SDS
5 mM, 70% residual activity with substrate 4-nitrophenyl beta-D-xylopyranoside, 112% activity with substrate 4-nitrophenyl alpha-L-arabinofuranoside
Sr2+
Zn2+
ZnSO4
additional information
Ca2+
-
addition of 10 mM CaCl2 enhances the beta-xylosidase activity by 10.22%
Ca2+
W0BU85
2 mM, about 1.8fold activation of N-terminal His-tagged fusions protein, about 2.2fold activation of C-terminal His-tagged fusions protein
Ca2+
-
5 mM, 45% stimulation of native enzyme, 20% of immobilized enzyme
CaCl2
5 mM, 99% activity compared to activity without addition of MgCl2, 1.25 mM 4-nitrophenyl beta-D-xylopyranoside as substrate, pH 4.6, 40°C
CaCl2
5 mM, 92.8% activity compared to activity without addition of MgCl2, 1.25 mM 4-nitrophenyl beta-D-xylopyranoside as substrate, pH 4.6, 42°C
Co2+
-
5 mM, 22% stimulation of native enzyme, 11% of immobilized enzyme
CoCl2
5 mM, 89.1% activity compared to activity without addition of MgCl2, 1.25 mM 4-nitrophenyl beta-D-xylopyranoside as substrate, pH 4.6, 40°C
CoCl2
5 mM, 91.3% activity compared to activity without addition of MgCl2, 1.25 mM 4-nitrophenyl beta-D-xylopyranoside as substrate, pH 4.6, 42°C
CuCl2
5 mM, 87.8% activity compared to activity without addition of MgCl2, 1.25 mM 4-nitrophenyl beta-D-xylopyranoside as substrate, pH 4.6, 40°C
CuCl2
5 mM, 96.4% activity compared to activity without addition of MgCl2, 1.25 mM 4-nitrophenyl beta-D-xylopyranoside as substrate, pH 4.6, 42°C
D-fructose
5 mM, 86.6% activity compared to activity without addition of MgCl2, 1.25 mM 4-nitrophenyl beta-D-xylopyranoside as substrate, pH 4.6, 40°C
D-fructose
5 mM, 76.8% activity compared to activity without addition of MgCl2, 1.25 mM 4-nitrophenyl beta-D-xylopyranoside as substrate, pH 4.6, 42°C
D-glucose
5 mM, 4.3% activity compared to activity without addition of MgCl2, 1.25 mM 4-nitrophenyl beta-D-xylopyranoside as substrate, pH 4.6, 40°C
D-glucose
5 mM, 54.4% activity compared to activity without addition of MgCl2, 1.25 mM 4-nitrophenyl beta-D-xylopyranoside as substrate, pH 4.6, 42°C
D-xylose
5 mM, 81.8% activity compared to activity without addition of MgCl2, 1.25 mM 4-nitrophenyl beta-D-xylopyranoside as substrate, pH 4.6, 40°C
D-xylose
5 mM, 97.4% activity compared to activity without addition of MgCl2, 1.25 mM 4-nitrophenyl beta-D-xylopyranoside as substrate, pH 4.6, 42°C
Fe3+
5 mM, 170% residual activity with substrate 4-nitrophenyl beta-D-xylopyranoside, 49% activity with substrate 4-nitrophenyl alpha-L-arabinofuranoside
MgCl2
5 mM, 94.8% activity compared to activity without addition of MgCl2, 1.25 mM 4-nitrophenyl beta-D-xylopyranoside as substrate, pH 4.6, 40°C
MgCl2
5 mM, 87.6% activity compared to activity without addition of MgCl2, 1.25 mM 4-nitrophenyl beta-D-xylopyranoside as substrate, pH 4.6, 42°C
Mn2+
-
5 mM, 30% stimulation of native enzyme, 28% of immobilized enzyme
MnCl2
5 mM, 98.5% activity compared to activity without addition of MgCl2, 1.25 mM 4-nitrophenyl beta-D-xylopyranoside as substrate, pH 4.6, 40°C
MnCl2
5 mM, 93.2% activity compared to activity without addition of MgCl2, 1.25 mM 4-nitrophenyl beta-D-xylopyranoside as substrate, pH 4.6, 42°C
NaCl
the recombinant enzyme displays high tolerance to salts with 60.8% activity in 20% w/v NaCl
NaCl
purified XylRBM26 presents good salt tolerance and retains 96.6% activity in 3.5 M NaCl and 77.9% initial activity even in 4.0 M NaCl
NaCl
the enzyme displays high catalytic activity (60%) in presence of 5-35% NaCl (w/v)
NaCl
A0A1L3GYC8
GH39 xylosidase XYL21 has excellent tolerance to salts, its activity is not inhibited but slightly increased in 0.50-1.50 M NaCl
NiCl2
5 mM, 98.5% activity compared to activity without addition of MgCl2, 1.25 mM 4-nitrophenyl beta-D-xylopyranoside as substrate, pH 4.6, 40°C
NiCl2
5 mM, 96.3% activity compared to activity without addition of MgCl2, 1.25 mM 4-nitrophenyl beta-D-xylopyranoside as substrate, pH 4.6, 42°C
Zn2+
enzyme activity can be enhanced more than 1.63times by addition of 0.1 mM Zn2+
ZnSO4
5 mM, 101.1% activity compared to activity without addition of MgCl2, 1.25 mM 4-nitrophenyl beta-D-xylopyranoside as substrate, pH 4.6, 40°C
ZnSO4
5 mM, 99.1% activity compared to activity without addition of MgCl2, 1.25 mM 4-nitrophenyl beta-D-xylopyranoside as substrate, pH 4.6, 42°C
additional information
recombinant enzyme HJ14GH43 shows moderate or high activity, but poor stability in NaCl, KCl, NaNO3, KNO3, Na2SO4, and (NH4)2SO4 at concentrations from 3.0 to 30.0% w/v. Approximately one-third of the surface of rHJ14GH43 is positively charged, which may be the primary factor responsible for poor stability in high neutral salt environments. No significant effect on enzyme activity by EDTA, Pb(CH3COO), Fe3+, 2-mercaptoethanol, Mn2+, Ca2+, Mg2+, and Co2+
additional information
poor effects of Na+, Ca2+, K+, and Ba2+ at 1-5 mM
additional information
no significant effect on enzyme activity by 5 mM of Al3+, Na+, Mg2+, K+, and NH4+
additional information
poor effects by NH4+, Ba2+, Li+, and Ca2+ at 1-5 mM
additional information
-
no metal ions required for activity and stability
additional information
the enzyme is not affected by 1 mM of Fe3+, Ca2+, Co2+, Mg2+, Ba2+, Ni2+, K+, Zn2+, Cu2+, or EDTA
additional information
enzyme GtXyl is not significantly influenced by the tested ions (CaCl2, CoCl2, CuCl2, FeCl2, KCl2, MnCl2, MgSO4, NaCl, NiCl2 and ZnSO4) and the EDTA chelating agent, suggesting that there is no dependence on metal ions for its catalytic activity
additional information
-
active within 0-30% of NaCl with culture broth
additional information
no or poor effects by 1-10 mM of Mn2+, Co2+, K+, Pb2+, and Mn2+
additional information
-
the enzyme is not affected by Mg2+, Al3+, Co2+, Mn2+, Cu2+, K+, Ba2+, and Fe2+
additional information
Mn2+, Ca2+, Fe3+, Co2+ and Zn2+ have no effects on enzyme activity
additional information
-
Mn2+, Ca2+, Fe3+, Co2+ and Zn2+ have no effects on enzyme activity
additional information
-
no or poor effects on enzyme activity by Ca2+, Mg2+, Mn2+, EDTA, Tris, and Tween 60
additional information
activity is not affected by K+, Mg2+, Fe2+, Fe3+, Ca2+, Co2+, Ba2+
additional information
-
activity is not affected by K+, Mg2+, Fe2+, Fe3+, Ca2+, Co2+, Ba2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-ethyl-3-(3-dimethylaminopropyl) carbodiimide
-
strong inhibition, 69% residual activity at 200 mM
2,3-epoxypropyl beta-D-xylobioside
-
irreversible inactivation
4-methylumbelliferyl-alpha-L-arabinofuranoside
substrate inhibition
4-methylumbelliferyl-beta-D-xylopyranoside
substrate inhibition
5,5'-dithiobis(2-nitrobenzoic acid)
-
rapid inactivation by modification of an essential thiol group
5-bromosuccinimide
-
strong inhibition, 84.7% complete inhibition at 0.1 mM
beta-D-xylopyranosyl azide
-
competitive, protects against inactivation by N-bromoacetyl-beta-D-xylopyranosylamine
diethyldicarbonate
-
inactivation indicates a carbethoxylation of histidine residues
methylmethanethiolsulfonate
-
rapid decrease in activity, treatment with dithiothreitol restores activity to about 75%
n-butyl beta-D-xylopyranoside
-
pH above 7.5 affects the binding of the competitive inhibitor
o-nitrophenyl beta-D-xylopyranoside
-
substrate inhibition if concentration higher than 0.5 mM
p-nitrophenyl alpha-L-arabinofuranoside
-
substrate inhibition if concentration higher than 12 mM
p-nitrophenyl alpha-L-arabinopyranoside
-
substrate inhibition if concentration higher than 9 mM
p-nitrophenyl beta-D-xylopyranoside
-
substrate inhibition if concentration higher than 0.1-0.2 mM
Al3+
-
80% inhibition of xylan-inducible enzyme, 10% of xylose-inducible enzyme, at 1 mM
arabinose
-
full activity is observed in the presence of up to 50 mM arabinose. Activity is reduced to 88%, 80% and 70% of maximum activity at 100 mM, 150 mM and 200 mM arabinose, respectively
Cu2+
-
64% inhibition of xylan-inducible enzyme, 79% of xylose-inducible enzyme, at 1 mM
Cu2+
about 75% residual activity at 5 mM in acetate buffer
Cu2+
-
5 mM, 70% residual activity of native enzyme, 96% of immobilized enzyme
D-xylose
-
competitive inhibition, about 65% residual activity at 1 mM
D-xylose
the purified recombinant enzyme shows high tolerance to xylose, with a relative activity of 55.4% at 400 mM
D-xylose
-
PxXyl43A retains 85% of its beta-xylosidase activity in the presence of 100 mM of xylose and 74% of its activity at 200 mM xylose. PxXyl43A possesses high tolerance for product inhibition by D-xylose
D-xylose
about 55% residual activity in the presence of 20 mM xylose
D-xylose
this enzyme shows low product inhibition and retained 51% activity in the presence of 100 mM xylose
EDTA
0.1 mM, 60% loss of activity. 1 mM, 10% loss of activity
EDTA
5 mM, 79% residual activity with substrate 4-nitrophenyl beta-D-xylopyranoside, 68% activity with substrate 4-nitrophenyl alpha-L-arabinofuranoside
EDTA
-
5 mM, 55% residual activity of native enzyme, 63% of immobilized enzyme
Fe2+
5 mM, 57% residual activity with substrate 4-nitrophenyl beta-D-xylopyranoside, 12% activity with substrate 4-nitrophenyl alpha-L-arabinofuranoside
Fe2+
-
5 mM, 20% residual activity of native enzyme, 42% of immobilized enzyme
Fe3+
5 mM, 170% residual activity with substrate 4-nitrophenyl beta-D-xylopyranoside, 49% activity with substrate 4-nitrophenyl alpha-L-arabinofuranoside
Hg2+
-
complete inhibition of xylan-inducible enzyme and xylose-inducible enzyme, at 1 mM
Hg2+
complete inhibition at 1 mM, 93% inhibition at 0.1 mM
Hg2+
about 10% residual activity at 5 mM in acetate buffer
Hg2+
-
5 mM, 49% residual activity of native enzyme, 64% of immobilized enzyme
Mg2+
W0BU85
2 mM, about 60% inhibition of N-terminal His-tagged fusions protein, about 55% inhibition of C-terminal His-tagged fusions protein
N-bromoacetyl-beta-D-xylopyranosylamine
-
pseudo-first-order inactivation
Ni2+
about 75% residual activity at 5 mM in acetate buffer
Pb2+
about 90% residual activity at 5 mM in citrate buffer
SDS
5 mM, 70% residual activity with substrate 4-nitrophenyl beta-D-xylopyranoside, 112% activity with substrate 4-nitrophenyl alpha-L-arabinofuranoside
SDS
-
5 mM, 44% residual activity of native enzyme, 65% of immobilized enzyme
xylose
not inhibitory up to 70 mM, 70% of its activity is retained in the presence of 200 mM xylose
xylose
A0A1L3GYC8
activates up to 0.3 M, inhibits the enzyme above, 80% inhibition at 2.1 M
Zn2+
-
5 mM, 34% residual activity of native enzyme, 56% of immobilized enzyme
additional information
-
upon inclusion of glucose (10-200 mM) in the beta-xylosidase assay reaction mixture, the purified enzyme exhibits full activity relative to the control reaction without added glucose
-
additional information
-
addition of glucose to the growth medium suppresses enzyme expression
-
additional information
-
10 mM Mg2+, Cu2+, Mn2+ and Ca2+ show no inhibition
-
additional information
-
not inhibited by CoCl2, KCl, MgSO4, CaCl2, EDTA, D-glucose, arabinose, and fructose
-
additional information
recombinant enzyme Xln-DT displays high tolerance to xylose, with 60% activity remaining in the presence of 3 M xylose
-
additional information
no or poor effects by 1-10 mM of EDTA, 2-mercaptoethanol, and Triton X-100
-
additional information
-
the enzyme is very tolerant to inhibition by D-xylose and is not affected up to 200 mM D-xylose
-
additional information
no inhibition by EDTA, no significant effects by 1-10 mM of Mg2+, Mn2+, Ba2+, Ni2+, K+, Li+, Zn2+, Ca2+, and Cu2+
-
additional information
not inhibited by glucose, arabinose, mannose, and galactose
-
additional information
-
not inhibited by glucose, arabinose, mannose, and galactose
-
additional information
-
not inhibited by diethyl dicarbonate, phenylmethyl sulfonide, phenyl-glyoxal, N-ethylmaleimide, iodoacetate, citraconic anhydride, and trinotrobenzene sulfonic acid. Ethanol has no effect on enzyme activity at 20% (v/v).
-
additional information
absence of inhibition in the presence of EDTA, dithiothreitol, and 2-mercaptoethanol
-
additional information
-
absence of inhibition in the presence of EDTA, dithiothreitol, and 2-mercaptoethanol
-
additional information
-
EDTA is not inhibitory up to 10 mM
-
additional information
EDTA is not inhibitory up to 10 mM
-
additional information
-
not inhibitory: alkyl epoxides derived from D-xylose
-
additional information
-
inhibition by various metal ions, no inhibition by D-xylose
-
additional information
A0A1L3GYC8
XYL21 is insensitive to the final lignocellulose hydrolysis products including glucose, xylose, arabinose, mannose and galactose. The enzyme retains 111.36% and 53.49% relative activity in 0.30 and 0.90 M xylose, respectively
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ba2+
-
1.7fold activation of xylan-inducible enzyme, 1.1fold of xylose-inducible enzyme, at 0.25 mM
Co2+
-
1.4fold activation of xylan-inducible enzyme, 1.2fold of xylose-inducible enzyme, at 1 mM
Mg2+
-
1.65fold activation of xylan-inducible enzyme, 1.2fold of xylose-inducible enzyme, at 0.25 mM
Mn2+
-
1.2fold activation of xylan-inducible enzyme, 1.2fold of xylose-inducible enzyme, at 1 mM
xylose
A0A1L3GYC8
activates up to 0.3 M, inhibits the enzyme above, 80% inhibition at 2.1 M
Zn2+
-
1.2fold activation of xylan-inducible enzyme, 1.3fold of xylose-inducible enzyme, at 1 mM
Ca2+
-
2.2fold activation of xylan-inducible enzyme, 1.4fold of xylose-inducible enzyme, at 0.25 mM
ethanol
-
ethanol at 5, 10 and 15% (v/v) concentration enhances the enzyme activity
ethanol
-
activity is promoted to 116.6% by a concentration of methanol below 15%
ethanol
5% (v/v), 316.9% activity compared to activity without addition of ethanol, 1.25 mM 4-nitrophenyl-beta-D-xylopyranoside as substrate, pH 4.6, 42°C
methanol
-
activity is completely unaffected by low concentration of methanol and even enhanced by the concentration of methanol below 25%
methanol
-
activity is promoted to 128.9% by a concentration of methanol below 15%
methanol
5% (v/v), 167% activity compared to activity without addition of methanol, 1.25 mM 4-nitrophenyl-beta-D-xylopyranoside as substrate, pH 4.6, 42°C
SDS
-
activity is moderately stimulated. 10 mM, 33.6% increase inactivity
additional information
-
xylose and xylan as only carbon source induce expression of enzyme form 1 and enzyme form 2, respectively, prevented by cycloheximide
-
additional information
enzyme T81Xyl5_22A shows no effect on its enzymatic activity in the presence of K+, Na+ and Li+
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinoma, Hepatocellular
Serum and host liver activities of glycosidases and sialyltransferases in animals bearing transplantable tumors.
Gangliosidosis, GM1
Multiple carbohydrate-cleaving specificities in human acidic and neutral glycosidases.
Gaucher Disease
Demonstration of a deficiency of beta-xylosidase activity in various forms of Gaucher's disease.
Gaucher Disease
Identity of beta-glucosidase, beta-xylosidase and one of the beta-galactosidase activities in human liver when assayed with 4-methylumbelliferyl-beta-D-glycosides studies in cases of Gaucher's disease.
Gaucher Disease
Multiple carbohydrate-cleaving specificities in human acidic and neutral glycosidases.
Hypersensitivity
Allergy to Aspergillus-derived enzymes in the baking industry: identification of beta-xylosidase from Aspergillus niger as a new allergen (Asp n 14).
Leukemia
Serum and host liver activities of glycosidases and sialyltransferases in animals bearing transplantable tumors.
Lupus Erythematosus, Systemic
Studies on the activity of selected lysosomal exoglycosidases in patients with systemic lupus erythematosus.
Neoplasms
Experiments to increase the selectivity of tumor chemotherapy by means of in vivo activation of transport forms of cancerostatics by exogenous enzymes.
Neoplasms
Selective tumor DNA synthesis inhibition: in vivo prodrug activation by an exogenous enzyme.
Neoplasms
[Distribution studies of alpha-L-arabinofuranosidase already unstable at pH 7.0 (37 degrees C) in tumor-bearing mice in connection with its possible use to enhance the selectivity of the chemotherapy of malignant tumors]
Neoplasms
[Experiments on the modification of the distribution of the activity of various alpha-L-arabinofuranosidases following i.v. application in tumor-bearing mice]
Neoplasms
[Histo- and cytochemical demonstration of exogenous alpha-L-arabinofuranosidase in tumor and tissues in mice (author's transl)]
Neoplasms
[Pharmacokinetic studies of the activity of a pH-labile alpha-L-arabinofuranosidase following i.v. injection into tumor-bearing mice]
Starvation
Glycosyl hydrolases of cell wall are induced by sugar starvation in Arabidopsis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8
(2-N-acetylamino)phenyl-beta-D-xylopyranoside
-
pH 5.5, 37°C
0.031
10-deacetyl-7-xylosyltaxol
recombinant enzyme, pH 4.5, 60°C
-
2.5
3,4-dimethylphenyl-beta-D-xylopyranoside
-
pH 5.5, 37°C
0.035
3,5-dichlorophenyl-beta-D-xylopyranoside
-
pH 5.5, 37°C
0.29
3-clorophenyl-beta-D-xylopyranoside
-
pH 5.5, 37°C
0.34
4-bromophenyl-beta-D-xylopyranoside
-
pH 5.5, 37°C
0.081
4-methylumbelliferyl-alpha-L-arabinofuranoside
pH 6.2, 40°C
2.394
4-nitrophenyl beta-D-glucopyranoside
recombinant enzyme, pH 6.0, 75°C
9.42
beechwood xylan
recombinant enzyme, pH 5.0, 65°C
-
4.76
ginsenoside Ra2
in 50 mM phosphate buffer (pH 7.0), at 37°C
0.22
p-methoxyphenyl-beta-D-xylopyranoside
-
pH 5.5, 37°C
7.4
p-nitrophenyl-beta-D-glucopyranoside
-
pH 5.5, 37°C
0.01
2,5-dinitrophenyl-beta-D-xylopyranoside
-
pH 5.5, 37°C
0.011
2,5-dinitrophenyl-beta-D-xylopyranoside
-
pH 5.5, 37°C
0.016
2,5-dinitrophenyl-beta-D-xylopyranoside
-
mutant E160A, pH 7.0, 40°C
0.049
2,5-dinitrophenyl-beta-D-xylopyranoside
-
pH 5.5, 37°C, presence of 20 mM dithiothreitol
0.057
2,5-dinitrophenyl-beta-D-xylopyranoside
-
pH 5.5, 37°C, presence of 62 mM dithiothreitol
0.146
2,5-dinitrophenyl-beta-D-xylopyranoside
-
pH 5.5, 37°C, presence of 169 mM dithiothreitol
0.95
2,5-dinitrophenyl-beta-D-xylopyranoside
-
wild type, pH 7.0, 40°C
0.15
2-nitrophenyl-beta-D-xylopyranoside
-
pH 5.5, 37°C
0.18
2-nitrophenyl-beta-D-xylopyranoside
-
mutant E160A, pH 7.0, 40°C
7.1
2-nitrophenyl-beta-D-xylopyranoside
-
wild type, pH 7.0, 40°C
0.09
3,4-dinitrophenyl beta-D-xylopyranoside
pH 4.0, 40°C, mutant E500A
0.39
3,4-dinitrophenyl beta-D-xylopyranoside
pH 4.0, 40°C, wild-type enzyme
1.27
3,4-dinitrophenyl beta-D-xylopyranoside
pH 4.0, 40°C, mutant E88A
2.6
3,4-dinitrophenyl beta-D-xylopyranoside
pH 4.0, 40°C, mutant D288A
0.0099
3,4-dinitrophenyl-beta-D-xylopyranoside
-
pH 5.5, 37°C
0.01
3,4-dinitrophenyl-beta-D-xylopyranoside
-
pH 5.5, 37°C
0.014
3,4-dinitrophenyl-beta-D-xylopyranoside
-
pH 5.5, 37°C
0.025
3,4-dinitrophenyl-beta-D-xylopyranoside
-
mutant E160A, pH 7.0, 40°C
0.8
3,4-dinitrophenyl-beta-D-xylopyranoside
-
wild type, pH 7.0, 40°C
0.366
4-methylumbelliferyl-beta-D-xylopyranoside
pH 6.2, 40°C
12
4-nitrophenyl alpha-D-xylopyranoside
in 50 mM sodium citrate buffer (pH 4.0), at 30°C
1.02
4-nitrophenyl alpha-L-arabinofuranoside
pH 6.0, 95°C, recombinant enzyme
2.014
4-nitrophenyl alpha-L-arabinofuranoside
recombinant enzyme, pH 6.0, 75°C
4.64
4-nitrophenyl alpha-L-arabinofuranoside
recombinant enzyme, pH 6.5, 50°C
5.8
4-nitrophenyl alpha-L-arabinofuranoside
at pH 3.0 and 50°C
2.4319
4-nitrophenyl alpha-L-arabinopyranoside
recombinant enzyme, pH 6.0, 75°C
3.6
4-nitrophenyl alpha-L-arabinopyranoside
at pH 3.0 and 50°C
1 - 4.5
4-nitrophenyl beta-D-glucoside
pH 4.0, 40°C, wild-type enzyme
3.67
4-nitrophenyl beta-D-glucoside
pH 6.0, 95°C, recombinant enzyme
0.03
4-nitrophenyl beta-D-xylopyranoside
pH 6.0, 50°C, compared to KM-value: 0.164 mM for 4-nitrophenyl-beta-D-glucopyranoside of the beta-glucosidase activity, suggesting that RuBGX1 prefers 4-nitrophenyl-beta-D-xylopyranoside substrate
0.1317
4-nitrophenyl beta-D-xylopyranoside
pH 4.6, 42°C
0.17
4-nitrophenyl beta-D-xylopyranoside
at pH 3.0 and 50°C
0.19
4-nitrophenyl beta-D-xylopyranoside
-
pH and temperature not specified in the publication
0.25
4-nitrophenyl beta-D-xylopyranoside
recombinant enzyme, pH 5.0, 65°C
0.45
4-nitrophenyl beta-D-xylopyranoside
-
pH and temperature not specified in the publication
1.2
4-nitrophenyl beta-D-xylopyranoside
-
recombinant enzyme, pH 7.0, 54°C
1.45
4-nitrophenyl beta-D-xylopyranoside
in sodium phosphate buffer (pH 7.0), at 37°C
1.54
4-nitrophenyl beta-D-xylopyranoside
in 50 mM phosphate buffer (pH 7.0), at 37°C
2.27
4-nitrophenyl beta-D-xylopyranoside
recombinant enzyme, pH 6.5, 50°C
3.43
4-nitrophenyl beta-D-xylopyranoside
-
in 50 mM phosphate/citrate buffer pH 7.0, at 40°C
0.33
4-nitrophenyl beta-D-xyloside
pH 4.0, 40°C, wild-type enzyme
0.54
4-nitrophenyl beta-D-xyloside
recombinant mutant H284R, pH 6.0, 75°C
0.57
4-nitrophenyl beta-D-xyloside
recombinant mutant Y283A, pH 6.0, 75°C
0.72
4-nitrophenyl beta-D-xyloside
pH 6.0, 32°C, recombinant enzyme
0.77
4-nitrophenyl beta-D-xyloside
recombinant mutant Y283H, pH 6.0, 75°C
0.8
4-nitrophenyl beta-D-xyloside
recombinant mutant H284S, pH 6.0, 75°C
0.8316
4-nitrophenyl beta-D-xyloside
recombinant enzyme, pH 6.0, 75°C
1.1
4-nitrophenyl beta-D-xyloside
recombinant mutant Y283T, pH 6.0, 75°C
1.53
4-nitrophenyl beta-D-xyloside
recombinant mutant Y283E, pH 6.0, 75°C
1.55
4-nitrophenyl beta-D-xyloside
W0BU85
pH 7.0, 50°C, N-terminal His-tagged fusions protein
1.55
4-nitrophenyl beta-D-xyloside
recombinant mutant H284A, pH 6.0, 75°C
1.66
4-nitrophenyl beta-D-xyloside
recombinant wild-type enzyme, pH 6.0, 75°C
1.66
4-nitrophenyl beta-D-xyloside
pH 6.0, 95°C, recombinant enzyme
2.47
4-nitrophenyl beta-D-xyloside
recombinant mutant H284D, pH 6.0, 75°C
2.8
4-nitrophenyl beta-D-xyloside
W0BU85
pH 7.0, 50°C, C-terminal His-tagged fusions protein
5.15
4-nitrophenyl beta-D-xyloside
recombinant mutant Y283D, pH 6.0, 75°C
9.56
4-nitrophenyl beta-D-xyloside
recombinant enzyme, pH 5.0, 60°C
66
4-nitrophenyl beta-D-xyloside
pH 6.0, 75°C, recombinant enzyme
0.133
4-nitrophenyl-alpha-L-arabinofuranoside
-
mutant E186A, pH 8.0, 25°C
0.152
4-nitrophenyl-alpha-L-arabinofuranoside
-
mutant E186A, pH 7.0, 25°C
0.177
4-nitrophenyl-alpha-L-arabinofuranoside
-
mutant E186A, pH 6.0, 25°C
0.497
4-nitrophenyl-alpha-L-arabinofuranoside
pH 6.2, 40°C
0.715
4-nitrophenyl-alpha-L-arabinofuranoside
-
wild-type, pH 6.0, 25°C
1.08
4-nitrophenyl-alpha-L-arabinofuranoside
-
wild-type, pH 7.0, 25°C
4.09
4-nitrophenyl-alpha-L-arabinofuranoside
-
wild-type, pH 8.0, 25°C
0.13
4-nitrophenyl-beta-D-xylopyranoside
-
pH 6.1, 90°C, recombinant enzyme
0.19
4-nitrophenyl-beta-D-xylopyranoside
-
pH 6.5, 45°C, xylan-inducible enzyme
0.27
4-nitrophenyl-beta-D-xylopyranoside
-
mutant E160A, pH 7.0, 40°C
0.32
4-nitrophenyl-beta-D-xylopyranoside
-
pH 5.6, 40°C, xylose-inducible enzyme
1.8
4-nitrophenyl-beta-D-xylopyranoside
wild-type, pH 5.0, 37°C
2
4-nitrophenyl-beta-D-xylopyranoside
mutant E594Q, pH 5.0, 37°C
2.57
4-nitrophenyl-beta-D-xylopyranoside
-
mutant E186A, pH 8.0, 25°C
2.82
4-nitrophenyl-beta-D-xylopyranoside
-
mutant E186A, pH 6.0, 25°C
3.27
4-nitrophenyl-beta-D-xylopyranoside
-
mutant E186A, pH 7.0, 25°C
3.42
4-nitrophenyl-beta-D-xylopyranoside
-
immobilized enzyme, pH 7.0, 50°C
3.9
4-nitrophenyl-beta-D-xylopyranoside
mutant Y237F, pH 5.0, 37°C
5.2
4-nitrophenyl-beta-D-xylopyranoside
-
wild type, pH 7.0, 40°C
18
4-nitrophenyl-beta-D-xylopyranoside
mutant E616A, pH 5.0, 37°C
28
4-nitrophenyl-beta-D-xylopyranoside
pH 6.0, 65°C
0.4
ginsenoside Ra1
in sodium phosphate buffer (pH 7.0), at 37°C
5.56
ginsenoside Ra1
in 50 mM phosphate buffer (pH 7.0), at 37°C
0.15
m-nitrophenyl-beta-D-xylopyranoside
-
pH 5.5, 37°C
0.046
o-nitrophenyl-beta-D-xylopyranoside
-
pH 5.5, 37°C
0.08
o-nitrophenyl-beta-D-xylopyranoside
-
pH 5.5, 37°C
0.036
p-nitrophenyl-beta-D-xylopyranoside
-
pH 5.5, 37°C
0.14
p-nitrophenyl-beta-D-xylopyranoside
-
pH 5.5, 37°C
additional information
additional information
steady-state kinetics, recombinant wild-type and mutant enzymes
-
additional information
additional information
A0A1L3GYC8
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.437
10-deacetyl-7-xylosyltaxol
recombinant enzyme, pH 4.5, 60°C
-
0.233
4-methylumbelliferyl-alpha-L-arabinofuranoside
pH 6.2, 40°C
253.3
4-nitrophenyl alpha-D-xylopyranoside
in 50 mM sodium citrate buffer (pH 4.0), at 30°C
25
2,5-dinitrophenyl-beta-D-xylopyranoside
pH 7.0, 40°C, recombinant wild-type enzyme
30
2,5-dinitrophenyl-beta-D-xylopyranoside
pH 7.0, 40°C, recombinant mutant E178G
0.00056
3,4-dinitrophenyl beta-D-xylopyranoside
pH 4.0, 40°C, mutant D288A
0.071
3,4-dinitrophenyl beta-D-xylopyranoside
pH 4.0, 40°C, mutant E500A
0.1
3,4-dinitrophenyl beta-D-xylopyranoside
pH 4.0, 40°C, mutant E88A
93.8
3,4-dinitrophenyl beta-D-xylopyranoside
pH 4.0, 40°C, wild-type enzyme
1.8
3,4-dinitrophenyl-beta-D-xylopyranoside
pH 7.0, 40°C, recombinant mutant E178G
77
3,4-dinitrophenyl-beta-D-xylopyranoside
pH 7.0, 40°C, recombinant wild-type enzyme
0.208
4-methylumbelliferyl-beta-D-xylopyranoside
pH 6.2, 40°C
20
4-methylumbelliferyl-beta-D-xylopyranoside
pH 7.0, 40°C, recombinant wild-type enzyme
2.04
4-nitrophenyl alpha-L-arabinofuranoside
recombinant enzyme, pH 6.5, 50°C
143
4-nitrophenyl alpha-L-arabinofuranoside
at pH 3.0 and 50°C
220
4-nitrophenyl alpha-L-arabinopyranoside
at pH 3.0 and 50°C
17.3
4-nitrophenyl beta-D-glucoside
pH 4.0, 40°C, wild-type enzyme
0.82
4-nitrophenyl beta-D-xylopyranoside
-
pH and temperature not specified in the publication
2.34
4-nitrophenyl beta-D-xylopyranoside
recombinant enzyme, pH 6.5, 50°C
2.8
4-nitrophenyl beta-D-xylopyranoside
-
recombinant enzyme, pH 7.0, 54°C
39.2
4-nitrophenyl beta-D-xylopyranoside
recombinant enzyme, pH 5.0, 65°C
76
4-nitrophenyl beta-D-xylopyranoside
-
in 50 mM phosphate/citrate buffer pH 7.0, at 40°C
135
4-nitrophenyl beta-D-xylopyranoside
pH 4.6, 40°C
173
4-nitrophenyl beta-D-xylopyranoside
at pH 3.0 and 50°C
453.29
4-nitrophenyl beta-D-xylopyranoside
-
pH and temperature not specified in the publication
0.47
4-nitrophenyl beta-D-xyloside
pH 6.0, 50°C, recombinant His-tagged enzyme
5.19
4-nitrophenyl beta-D-xyloside
recombinant mutant H284R, pH 6.0, 75°C
5.26
4-nitrophenyl beta-D-xyloside
recombinant mutant Y283A, pH 6.0, 75°C
5.51
4-nitrophenyl beta-D-xyloside
recombinant mutant Y283H, pH 6.0, 75°C
6.08
4-nitrophenyl beta-D-xyloside
recombinant mutant H284S, pH 6.0, 75°C
6.94
4-nitrophenyl beta-D-xyloside
W0BU85
pH 7.0, 50°C, C-terminal His-tagged fusions protein
8.51
4-nitrophenyl beta-D-xyloside
W0BU85
pH 7.0, 50°C, N-terminal His-tagged fusions protein
9.37
4-nitrophenyl beta-D-xyloside
recombinant mutant Y283T, pH 6.0, 75°C
11.63
4-nitrophenyl beta-D-xyloside
recombinant mutant Y283E, pH 6.0, 75°C
11.79
4-nitrophenyl beta-D-xyloside
recombinant mutant H284A, pH 6.0, 75°C
12.63
4-nitrophenyl beta-D-xyloside
recombinant wild-type enzyme, pH 6.0, 75°C
18.84
4-nitrophenyl beta-D-xyloside
recombinant mutant H284D, pH 6.0, 75°C
19.65
4-nitrophenyl beta-D-xyloside
recombinant mutant Y283D, pH 6.0, 75°C
29.28
4-nitrophenyl beta-D-xyloside
pH 6.0, 32°C, recombinant enzyme
133
4-nitrophenyl beta-D-xyloside
pH 4.0, 40°C, wild-type enzyme
193.22
4-nitrophenyl beta-D-xyloside
recombinant enzyme, pH 5.0, 60°C
0.0000036
4-nitrophenyl-alpha-L-arabinofuranoside
-
mutant E186A, pH 7.0, 25°C
0.0000044
4-nitrophenyl-alpha-L-arabinofuranoside
-
mutant E186A, pH 8.0, 25°C
0.0000045
4-nitrophenyl-alpha-L-arabinofuranoside
-
mutant E186A, pH 6.0, 25°C
3.05
4-nitrophenyl-alpha-L-arabinofuranoside
-
wild-type, pH 8.0, 25°C
3.13
4-nitrophenyl-alpha-L-arabinofuranoside
-
wild-type, pH 6.0, 25°C
3.28
4-nitrophenyl-alpha-L-arabinofuranoside
-
wild-type, pH 7.0, 25°C
3.34
4-nitrophenyl-alpha-L-arabinofuranoside
-
presence of tris(hydroxymethyl)aminomethane, pH 7.0, 25°C
0.0014
4-nitrophenyl-beta-D-xylopyranoside
-
mutant E186A, pH 6.0, 25°C
0.0016
4-nitrophenyl-beta-D-xylopyranoside
-
mutant E186A, pH 7.0, 25°C
0.0016
4-nitrophenyl-beta-D-xylopyranoside
-
mutant E186A, pH 8.0, 25°C
0.014
4-nitrophenyl-beta-D-xylopyranoside
pH 7.0, 40°C, recombinant mutant E178G
1.6
4-nitrophenyl-beta-D-xylopyranoside
mutant Y237F, pH 5.0, 37°C
3.3
4-nitrophenyl-beta-D-xylopyranoside
mutant E616A, pH 5.0, 37°C
9.7
4-nitrophenyl-beta-D-xylopyranoside
wild-type, pH 5.0, 37°C
10
4-nitrophenyl-beta-D-xylopyranoside
mutant E594Q, pH 5.0, 37°C
31.5
4-nitrophenyl-beta-D-xylopyranoside
-
presence of tris(hydroxymethyl)aminomethane, pH 7.0, 25°C
57
4-nitrophenyl-beta-D-xylopyranoside
pH 7.0, 40°C, recombinant wild-type enzyme
189.3
4-nitrophenyl-beta-D-xylopyranoside
pH 6.0, 65°C
2.24
beechwood xylan
recombinant enzyme, pH 5.0, 65°C
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
110.87
10-deacetyl-7-xylosyltaxol
recombinant enzyme, pH 4.5, 60°C
-
2.88
4-methylumbelliferyl-alpha-L-arabinofuranoside
pH 6.2, 40°C
0.57
4-methylumbelliferyl-beta-D-xylopyranoside
pH 6.2, 40°C
21.7
4-nitrophenyl alpha-D-xylopyranoside
in 50 mM sodium citrate buffer (pH 4.0), at 30°C
0.24
beechwood xylan
recombinant enzyme, pH 5.0, 65°C
-
0.00021
3,4-dinitrophenyl beta-D-xylopyranoside
pH 4.0, 40°C, mutant D288A
0.08
3,4-dinitrophenyl beta-D-xylopyranoside
pH 4.0, 40°C, mutant E88A
0.76
3,4-dinitrophenyl beta-D-xylopyranoside
pH 4.0, 40°C, mutant E500A
242
3,4-dinitrophenyl beta-D-xylopyranoside
pH 4.0, 40°C, wild-type enzyme
0.44
4-nitrophenyl alpha-L-arabinofuranoside
recombinant enzyme, pH 6.5, 50°C
25
4-nitrophenyl alpha-L-arabinofuranoside
at pH 3.0 and 50°C
62
4-nitrophenyl alpha-L-arabinopyranoside
at pH 3.0 and 50°C
1.19
4-nitrophenyl beta-D-glucoside
pH 4.0, 40°C, wild-type enzyme
1.03
4-nitrophenyl beta-D-xylopyranoside
recombinant enzyme, pH 6.5, 50°C
1.82
4-nitrophenyl beta-D-xylopyranoside
-
pH and temperature not specified in the publication
2.33
4-nitrophenyl beta-D-xylopyranoside
-
recombinant enzyme, pH 7.0, 54°C, calculated by BRENDA
8.1
4-nitrophenyl beta-D-xylopyranoside
-
in 50 mM phosphate/citrate buffer pH 7.0, at 40°C
156.8
4-nitrophenyl beta-D-xylopyranoside
recombinant enzyme, pH 5.0, 65°C
1000
4-nitrophenyl beta-D-xylopyranoside
at pH 3.0 and 50°C
2084
4-nitrophenyl beta-D-xylopyranoside
pH 4.6, 40°C
2322
4-nitrophenyl beta-D-xylopyranoside
-
pH and temperature not specified in the publication
54080
4-nitrophenyl beta-D-xylopyranoside
pH 4.6, 42°C
2.48
4-nitrophenyl beta-D-xyloside
W0BU85
pH 7.0, 50°C, C-terminal His-tagged fusions protein
5.49
4-nitrophenyl beta-D-xyloside
W0BU85
pH 7.0, 50°C, N-terminal His-tagged fusions protein
20.21
4-nitrophenyl beta-D-xyloside
recombinant enzyme, pH 5.0, 60°C
40.67
4-nitrophenyl beta-D-xyloside
pH 6.0, 32°C, recombinant enzyme
400
4-nitrophenyl beta-D-xyloside
pH 4.0, 40°C, wild-type enzyme
0.000024
4-nitrophenyl-alpha-L-arabinofuranoside
-
mutant E186A, pH 7.0, 25°C
0.000025
4-nitrophenyl-alpha-L-arabinofuranoside
-
mutant E186A, pH 6.0, 25°C
0.000033
4-nitrophenyl-alpha-L-arabinofuranoside
-
mutant E186A, pH 8.0, 25°C
0.746
4-nitrophenyl-alpha-L-arabinofuranoside
-
wild-type, pH 8.0, 25°C
2.72
4-nitrophenyl-alpha-L-arabinofuranoside
-
presence of tris(hydroxymethyl)aminomethane, pH 7.0, 25°C
3.03
4-nitrophenyl-alpha-L-arabinofuranoside
-
wild-type, pH 7.0, 25°C
4.38
4-nitrophenyl-alpha-L-arabinofuranoside
-
wild-type, pH 6.0, 25°C
0.0005
4-nitrophenyl-beta-D-xylopyranoside
-
mutant E186A, pH 7.0, 25°C
0.00051
4-nitrophenyl-beta-D-xylopyranoside
-
mutant E186A, pH 6.0, 25°C
0.00062
4-nitrophenyl-beta-D-xylopyranoside
-
mutant E186A, pH 8.0, 25°C
0.2
4-nitrophenyl-beta-D-xylopyranoside
mutant E616A, pH 5.0, 37°C
0.41
4-nitrophenyl-beta-D-xylopyranoside
mutant Y237F, pH 5.0, 37°C
5
4-nitrophenyl-beta-D-xylopyranoside
mutant E594Q, pH 5.0, 37°C
5.4
4-nitrophenyl-beta-D-xylopyranoside
wild-type, pH 5.0, 37°C
42.9
4-nitrophenyl-beta-D-xylopyranoside
-
presence of tris(hydroxymethyl)aminomethane, pH 7.0, 25°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4 - 10
1-aminopropane
-
substrate 4-nitrophenyl-beta-D-xylopyranoside, 25°C, pH 7.0
1000
2-hydroxypropane
-
substrate 4-nitrophenyl-beta-D-xylopyranoside, 25°C, pH 7.0
1900
ethanol
-
substrate 4-nitrophenyl-beta-D-xylopyranoside, 25°C, pH 7.0
460
ethylamine
-
substrate 4-nitrophenyl-beta-D-xylopyranoside, 25°C, pH 7.0
7
1,3-bis[tris(hydroxymethyl)methylamino]propane
-
substrate 4-nitrophenyl-alpha-L-arabinofuranoside, 25°C, pH 7.0
7.7
1,3-bis[tris(hydroxymethyl)methylamino]propane
-
substrate 4-nitrophenyl-beta-D-xylopyranoside, 25°C, pH 7.0
1.7
1-amino-2-propanol
-
substrate 4-nitrophenyl-beta-D-xylopyranoside, 25°C, pH 7.0
2.31
1-amino-2-propanol
-
substrate 4-nitrophenyl-alpha-L-arabinofuranoside, 25°C, pH 7.0
2
4-nitrophenyl-beta-D-xylopyranoside
-
pH 6.5, 45°C, xylan-inducible enzyme
5.3
4-nitrophenyl-beta-D-xylopyranoside
-
pH 5.6, 40°C, xylose-inducible enzyme
5.3
bis-(2-hydroxyethyl)amino-tris(hydroxymethyl)methane
-
substrate 4-nitrophenyl-beta-D-xylopyranoside, 25°C, pH 7.0
6.2
bis-(2-hydroxyethyl)amino-tris(hydroxymethyl)methane
-
substrate 4-nitrophenyl-alpha-L-arabinofuranoside, 25°C, pH 7.0
1.7
D-xylose
pH and temperature not specified in the publication
0.205
diethanolamine
-
substrate 4-nitrophenyl-beta-D-xylopyranoside, 25°C, pH 7.0
0.22
diethanolamine
-
substrate 4-nitrophenyl-alpha-L-arabinofuranoside, 25°C, pH 7.0
0.7
ethanolamine
-
substrate 4-nitrophenyl-beta-D-xylopyranoside, 25°C, pH 7.0
0.92
ethanolamine
-
substrate 4-nitrophenyl-alpha-L-arabinofuranoside, 25°C, pH 7.0
0.088
triethanolamine
-
wild-type, substrate 4-nitrophenyl-beta-D-xylopyranoside, pH 8.0, 25°C
0.109
triethanolamine
-
substrate 4-nitrophenyl-beta-D-xylopyranoside, 25°C, pH 7.0
0.111
triethanolamine
-
wild-type, substrate 4-nitrophenyl-beta-D-xylopyranoside, pH 7.0, 25°C
0.112
triethanolamine
-
substrate 4-nitrophenyl-alpha-L-arabinofuranoside, 25°C, pH 7.0
0.121
triethanolamine
-
wild-type, substrate 4-nitrophenyl-alpha-L-arabinofuranoside, pH 7.0, 25°C
0.54
triethanolamine
-
wild-type, substrate 4-nitrophenyl-beta-D-xylopyranoside, pH 6.0, 25°C
33.2
triethanolamine
-
mutant E186A, substrate 4-nitrophenyl-beta-D-xylopyranoside, pH 8.0, 25°C
47
triethanolamine
-
mutant E186A, substrate 4-nitrophenyl-alpha-L-arabinofuranoside, pH 8.0, 25°C
145
triethanolamine
-
mutant E186A, substrate 4-nitrophenyl-beta-D-xylopyranoside, pH 7.0, 25°C
418
triethanolamine
-
mutant E186A, substrate 4-nitrophenyl-beta-D-xylopyranoside, pH 6.0, 25°C
815
triethanolamine
-
mutant E186A, substrate 4-nitrophenyl-alpha-L-arabinofuranoside, pH 7.0, 25°C
5.9
Tris(hydroxymethyl)aminomethane
-
substrate 4-nitrophenyl-beta-D-xylopyranoside, 25°C, pH 7.0
6
Tris(hydroxymethyl)aminomethane
-
substrate 4-nitrophenyl-alpha-L-arabinofuranoside, 25°C, pH 7.0
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.03
purified recombinant enzyme, pH 7.0, 25°C, substrate 4-nitrophenyl-alpha-L-arabinofuranoside
0.031
crude extract, in sodium phosphate buffer (pH 7.0), at 37°C
0.1
0.25
-
substrate 4-nitrophenyl beta-D-xylopyranoside, pH 7.0, 54°C, recombinant enzyme
1.3
-
purified recombinant enzyme, substrate 4-nitrophenyl-alpha-L-arabinofuranoside, pH 8.0, 60°C
1.33
purified recombinant enzyme, pH 5.0, 55°C, substrate xylohexaose
1.51
purified recombinant enzyme, pH 5.0, 55°C, substrate xylotriose
1.56
purified recombinant enzyme, pH 5.0, 55°C, substrate xylopentaose
1.83
purified recombinant enzyme, pH 5.0, 55°C, substrate xylotetraose
12.1
4-nitrophenyl beta-D-xylopyranoside as substrate, pH 4.6, 42°C
12.4
purified recombinant enzyme, pH 5.0, 55°C, substrate 4-nitrophenyl beta-D-xyloside
1797
substrate 4-nitrophenyl beta-D-xylopyranoside, pH 5.0, 40°C
18.33
purified recombinant enzyme, substrate 4-nitrophenyl beta-D-xyloside, pH 5.0, 60°C
2.37
purified recombinant enzyme, pH 7.0, 25°C, substrate 4-nitrophenyl beta-D-xyloside
22
223.14
-
substrate: 4-nitrophenyl alpha-L-arabinopyranoside, pH 6.0, 90°C
25
26.6
27.12
purified recombinant enzyme, pH 6.0, 95°C, substrate 4-nitrophenyl beta-D-xyloside
275
-
purified recombinant enzyme, substrate 4-nitrophenyl-beta-D-xylopyranoside
29
-
purified recombinant enzyme, substrate 4-nitrophenyl-beta-D-glucopyranoside
3.32
purified enzyme, in sodium phosphate buffer (pH 7.0), at 37°C
3.6
-
substrate: 4-nitrophenyl-4-O-beta-D-xylopyranosyl-beta-D-xylopyranose, pH 5, 50°C, xylanase II
312.84
-
substrate: 4-nitrophenyl alpha-L-arabinofuranoside, pH 6.0, 90°C
347.3
substrate 4-nitrophenyl alpha-L-arabinofuranoside, pH 7.0, 45°C
4.43
purified recombinant enzyme, pH 5.0, 55°C, substrate xylobiose
4.85
purified recombinant enzyme, substrate 4-nitrophenyl beta-D-xyloside, pH 6.0, 40°C
5.5
4-nitrophenyl beta-D-xylopyranoside as substrate, pH 4.6, 40°C
50
-
purified recombinant enzyme, substrate 4-nitrophenyl-alpha-L-arabinofuranoside
51.82
1036fold purified enzyme, in 50 mM phosphate buffer (pH 7.0), at 37°C
659.9
substrate 4-nitrophenyl beta-D-xylopyranoside, pH 6.5, 50°C
7.9
-
purified recombinant enzyme, substrate 4-nitrophenyl beta-D-xyloside, pH 8.0, 60°C
8.46
purified recombinant enzyme, pH 6.0, 75°C, substrate 4-nitrophenyl beta-D-xyloside
8.56
purified recombinant enzyme, pH 6.0, 95°C, substrate 4-nitrophenyl-beta-D-xyloside
89.5
pH 4.0, 30°C, substrate 4-nitrophenyl alpha-L-arabinopyranoside
additional information
additional information
-
the xylan-inducible enzyme shows higher catalytic efficiency than the xylose-inducible enzyme
additional information
-
assay described, enzyme activity measured in homogenates of 10 to 15 male and female flies before and after sucrose meals, monitoring by spectroscopy, values of relative activity shown
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 3.5
3 - 4
3.5
4 - 4.5
4.5
4.5 - 5
5 - 5.2
-
at optimal temperature of 82°C and hydrolysis of p-nitrophenyl beta-D-xylopyranoside
5 - 6
5.5
5.8 - 6
-
at optimal temperature of 93°C and hydrolysis of p-nitrophenyl beta-D-xylopyranoside
6 - 6.5
6.5
7.5
4.5
recombinant enzyme, with substrate 10-deacetyl-7-xylosyltaxol
5
recombinant enzyme, with substrate 4-nitrophenyl beta-D-xyloside
5.5
optimal, with 4-nitrophenyl beta-D-xylopyranoside as substrate
6
-
hydrolysis of p-nitrophenyl alpha-L-arabinofuranoside, p-nitrophenyl alpha-L-arabinopyranoside, o-nitrophenyl beta-D-xylopyranoside
7.5
optimal, with 4-nitrophenyl beta-D-xylopyranoside as substrate
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.2 - 5.5
about 95% activity at pH 2.2, 100% activity at pH 3.0, about 90% activity at pH 4.0, about 55% activity at pH 5.5, about 42% activity at pH 6.0, about 12% activity at pH 7.0
3 - 6
-
about 60% activity at pH 3.0, about 80% activity at pH 4.0, 100% activity at pH 4.5, about 90% activity at pH 5.0, about 45% activity at pH 6.0
3.4 - 5.5
-
over 69% of maximum activity is observed in the pH range 3.4 to 5.5
3.5 - 4.5
-
pH 3.5: 73% of maximal activity, pH 4.5: 78% of maximal activity
3.8 - 5
-
the enzyme retains more than 90% of its maximum activity at a pH range from pH 3.8 to pH 4.3 at 50°C. At pH 5.0 the enzyme maintains about 60% of its maximal activity
4 - 10
activity range, recombinant enzyme, low activity above pH 8.0, no activity above pH 10.0 or below pH 4.0. Over 60% of maximal activity at pH 4.0-7.0
4 - 10.6
the enzyme is notably active at pH 4-6 and pH 9-10. At pH 8.0 about 65% and 90% relative activity is detected in citrate buffer and borate buffer respectively. At pH 8.6 and 9.0 less than 65% relative activity is observed in borate buffer, while more than 85% is found in Gly-NaOH buffer. More than 60% relative activity is noted at pH 10.6
4 - 6
4 - 7.5
A0A1L3GYC8
recombinant enzyme, 45 C, over 80% of maximal activity at pH 5.0-6.5, below 20% at pH 4.0, and 40% at pH 7.0, inactivation above pH 7.5
4.5 - 6
-
pH 4.5: about 65% of maximal activity, pH 6.0: about 40% of maximal activity
4.5 - 7
4.5 - 7.5
5 - 8
5 - 9
5.5 - 7
recombinant enzyme, at pH 6.0 activity is optimal, outside of this pH range activity decreases rapidly
5.5 - 7.5
pH 5.5: about 60% of maximal activity, pH 7.5: about 50% of maximal activity, enzyme entrapped in calcium alginate beads
6 - 7
6 - 7.5
less than 10% of maximal activity at pH 5.5, pH 6.0: maximal activity, pH 7.5: about 60% of maximal activity, soluble enzyme
6 - 9
6.8 - 8
W0BU85
at pH values ranging from pH 6.8 to 8.0, the relative activities are preserved at levels greater than 80%
additional information
pH profiles, wild-type and mutant enzymes, overview
4 - 6
-
pH 4.0: about 45% of maximal activity, pH 6.0: about 62% of maximal activity
4 - 6
-
enzyme coated with polyethylenimine shows optimum activity in the pH range 4.06.0
4.5 - 7
-
pH 4.5: 46% of maximal activity, pH 7.0: 50% of maximal activity
4.5 - 7
recombinant enzyme, over 60% of maximum activity within this pH range
4.5 - 7
over 60% of maximal activity within this range, 50% at pH 7.5
4.5 - 7
-
the enzyme retains over 60% of its optimum pH activity between pH 4.5 and pH 7.0
4.5 - 7.5
-
the activity drops sharply below pH 4.5 and above pH 7.0
5 - 8
about 5% activity at pH 5.0, about 90% activity at pH 5.5, 100% activity at pH 6.0, about 90% activity at pH 6.5, about 80% activity at pH 7.0, about 70% activity at pH 7.5, about 65% activity at pH 8.0
5 - 8
pH 5.0: about 60% of maximal activity, pH 8.0: about 30% of maximal activity, substrate: 4-nitrophenyl beta-D-xylopyranoside. pH 5.0: about 60% of maximal activity, pH 8.0: about 40% of maximal activity, substrate: 4-nitrophenyl alpha-L-arabinofuranoside
5 - 8
over 40% of maximal activity within this range, recombinant enzyme, profile overview
5 - 8
-
pH 5.0: about 50% of maximal activity, pH 7.0: about 90% of maximal activity, pH 8.0: about 80% of maximal activity
5 - 8
-
over 80% of maximal activity within this range, recombinant enzyme, profile overview
5 - 9
-
active over a relatively wide pH range (5.0-9.0) with more than 80% of the maximum activity
6 - 9
the enzyme retains 76.35% and 55.85% of catalytic activities at pH 6.0 and 9.0, respectively
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
35
37
40
45
50
55
60
60 - 65
65
70
75
75 - 80
80
82
-
at optimal pH 5.0-5.2 and hydrolysis of p-nitrophenyl beta-D-xylopyranoside
90
93
-
at optimal pH 5.8-6.0 and hydrolysis of p-nitrophenyl beta-D-xylopyranoside
35
optimal, with 4-nitrophenyl-beta-D-xylopyranoside as substrate
40
optimal, with 4-nitrophenyl-beta-D-xylopyranoside
55
-
enzyme coated with polyethylenimine shows optimum activity at 55°C
60
recombinant enzyme, with substrate 10-deacetyl-7-xylosyltaxol
75
recombinant enzyme, with sbstrate 4-nitrophenyl beta-D-xyloside
75 - 80
-
hydrolysis of p-nitrophenyl alpha-L-arabinofuranoside and p-nitrophenyl alpha-L-arabinopyranoside
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 40
activity range, profile overview. Approximately 15, 45, and 88% of maximal activity at 0, 10, and 20°C, respectively, maimal activity at 25°C
10 - 60
A0A1L3GYC8
over 20% of maximal activity within this range, recombinant enzyme
15 - 60
15°C: 27 % of maximal activity, 25°C: 40% of maximal activity, 60°C: 60% of maximal activity
20 - 45
W0BU85
20°C: about 40% of maximal activity, 45°C: about 60% of maximal activity
30 - 50
30 - 60
30 - 65
over 40% of maximal activity within this range, profile overview
40 - 50
40 - 60
40 - 70
50 - 70
65 - 100
65°C: about 60% of maximal activity, 100°C: about 85% of maximal activity, enzyme entrapment in calcium alginate beads
65 - 90
over 60% of maximal activity within this range, 50% at 90°C
70 - 90
75 - 100
-
activity is more than 50% of the maximum activity in the temperature range from 75°C to 100°C
additional information
30 - 50
recombinant enzyme, 80% of maximum activity within this temperature range
30 - 50
-
30°C: about 55% of maximal activity, 50°C: about 75% of maximal activity
30 - 50
about 80% activity at 30°C, about 98% activity at 35°C, 100% activity at 40°C, about 60% activity at 45°C, about 37% activity at 50°C
30 - 50
30°C: optimum, 50°C: about 50% of maximal activity, substrate: 4-nitrophenyl beta-D-xylopyranoside. 30°C: optimum, 50°C: about 25% of maximal activity, substrate: 4-nitrophenyl alpha-L-arabinofuranoside
30 - 60
-
30°C: about 20% of maximal activity, 60°C: about 60% of maximal activity
40 - 50
the enzyme activity is stable within the temperature range 40 to 50°C, but is rapidly lost above 50°C
40 - 60
-
over 50% of maximal activity within this range, recombinant enzyme, profile overview
40 - 70
-
about 45% activity at 40°C, about 70% activity at 50°C, about 85% activity at 55°C, 100% activity at 60°C, about 90% activity at 65°C, about 45% activity at 70°C
40 - 70
50% of maximal activity at 40°C and 70°C, recombinant enzyme
50 - 70
-
significant enzyme activity in the range of 5565 °C.At 50°C and 70°C, the enzyme activity is reduced, reaching about 40% and 50% of its maximum activity, respectively. Considerable inactivation is detected below 35°C and above 75°C
50 - 70
-
50°C: about 40% of maximal activity, 70°C: about 50% of maximal activity
50 - 70
-
about 60% activity at 50°C, 100% activity at 60°C, about 90% activity at 70°C, about 10% activity at 75°C
70 - 90
-
70°C: about 50% of maximal activity, 90°C: about 65% of maximal activity
70 - 90
70°C: about 50% of maximal activity, 90°C: about 25% of maximal activity, soluble enzyme
additional information
temperature profile and thermal stability
additional information
temperature optimum of 32°C for Xyl43Nc, on both sides of the optimum, enzyme activity decreases rapidly
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.2
6.9
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
multifunctional enzyme with glucosidase, xylosidase, arabinosidase and cellobiosidase activities
-
-
brenda
bifunctional beta-xylosidase/alpha-arabinofuranosidase
UniProt
brenda
bifunctional beta-xylosidase/alpha-arabinofuranosidase
UniProt
brenda
isolated as a xylanolytic bacterium from sludge in an anaerobic digester fed with pineapple wastes in a pineapple processing factory in Thailand
-
-
brenda
isolated as a xylanolytic bacterium from sludge in an anaerobic digester fed with pineapple wastes in a pineapple processing factory in Thailand
-
-
brenda
AHT-1, optimum production of enzyme in medium containing oat-spelt xylan at 30°C, pH 7.0 after 6 days
-
-
brenda
Penicillium wortmanni
desert and oasis flies studied, male and female, Neot Hakikar (oasis), Jordan Valley spring (wet), Kfar Adumim starved (arid), Jordan Valley autumn (arid)
-
-
brenda
bifunctional alpha-L-arabinofuranosidase/beta-D-xylosidase
TrEMBL
brenda
isolated from continental solfataric springs in Lac Abbe, Djibouti
-
-
brenda
isolated from continental solfataric springs in Lac Abbe, Djibouti
-
-
brenda
mutant strain NP54376 exhibiting high xylanolytic activity when grown on various xylan sources, maximal enzyme production by growth on xylan as the sole carbon source
-
-
brenda
production of enzyme when grown in liquid-state cultures on media containing oat spelt xylan as the carbon source
-
-
brenda
Bxl1; bifunctional beta-D-xylosidase/alpha-L-arabinofuranosidase
SwissProt
brenda
coexpression of enzyme with Trichoderma reesei xylanayse II in Saccharomyces cerevisiae
SwissProt
brenda
i.e. Bacillus stearothermophilus, strain T-6
SwissProt
brenda
i.e. Bacillus stearothermophilus, strain T-6, gene xynB3
SwissProt
brenda
bifunctional beta-xylosidase/alpha-L-arabinofuranosidase, EC 3.2.1.37/EC 3.2.1.55
UniProt
brenda
OPC-520, growth on xylan or xylooligosaccharides
SwissProt
brenda
bifunctional alpha-L-arabinofuranosidase/xylobiohydrolase
UniProt
brenda
bifunctional alpha-L-arabinofuranosidase/xylobiohydrolase
UniProt
brenda
Rubg3A, together with Rubg3B, beta-glucosidase/xylosidase activity, EC 3.2.1.37 and 3.2.1.74; isolated from rumen from a yak rumen metagenomic library, chinese yak, Bos grunniens
UniProt
brenda
Rubg3B, together with Rubg3A, beta-glucosidase/xylosidase activity, EC 3.2.1.37 and 3.2.1.74; isolated from rumen from a yak rumen metagenomic library, chinese yak, Bos grunniens
UniProt
brenda
RuBGX1, beta-glucosidase/xylosidase activity, EC 3.2.1.37 and 3.2.1.21, three catalytic amino acids of RuBGX1 are identified , as D272 is the catalytic nucleophile, and E167 and E481 are the catalytic acids; isolated from rumen from a yak rumen metagenomic library, chinese yak, Bos grunniens
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
zoospore culture, induction of enzyme production highest in cellubiose/xylan medium
brenda
additional information
-
synthesis of enzyme only in xylose or methyl-beta-D-xylopyranoside media
brenda
-
enzyme production induced in xylan or xylose media
brenda
-
induction of enzyme synthesis by xylose or xylan not required
brenda
Penicillium wortmanni
-
synthesis induced by methyl-beta- or methyl-alpha-D-xylopyranoside
brenda
-
enzyme production most induced in xylan medium
brenda
-
highest enzyme synthesis in sucrose/xylose medium
brenda
transcript levels are relatively high at the end of S1, i.e. fruit set, and at S3-E, i.e. beginning of the cell expansion. Transcripts reach a maximum when fruit firmness is 22-26 N, with a slight decline during the melting stage. Bifunctional alpha-L-arabinofuranosidase/beta-D-xylosidase and alpha-L-arabinofuranosidase are expressed differently in three fruit tissue types as well as in other plant tissues
brenda
-
xylose and xylan as only carbon source induce expression of enzyme form 1 and enzyme form 2, respectively, addition of glucose suppresses enzyme expression
brenda
-
induced enzyme production by addition of 1% xylan and 0.1% xylose in the medium
brenda
additional information
the enzyme is identified in the secretome after growth of the bacterium on cellulose as a sole carbon source
brenda
additional information
-
the enzyme is identified in the secretome after growth of the bacterium on cellulose as a sole carbon source
-
brenda
additional information
isolated from rumen from a yak rumen metagenomic library, chinese yak, Bos grunniens
brenda
additional information
isolated from rumen from a yak rumen metagenomic library, chinese yak, Bos grunniens
brenda
additional information
isolated from rumen from a yak rumen metagenomic library, chinese yak, Bos grunniens
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
enzyme HJ14GH43 has no signal peptide
-
brenda
additional information
the enzyme sequence harbors no signal peptide sequence
-
brenda
additional information
-
the enzyme sequence harbors no signal peptide sequence
-
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
the enzyme belongs to the glycoside hydrolase family 11, GH11
evolution
the enzyme belongs to the glycoside hydrolase family 43, GH43, subfamily 1. Enzyme Xyl43Nc shares common ancestry with enzymes from Spirochaetes and groups separately from Ascomycete sequences in our phylogeny, highlighting the importance of horizontal gene transfer in the evolution of the anaerobic fungi
evolution
A0A1L3GYC8
the enzyme belongs to the glycoside hydrolase family 39, GH39
evolution
-
the enzyme belongs to the glycoside hydrolase family 43, GH43, subfamily 12
evolution
the enzyme belongs to the glycoside hydrolase family 43, GH43
evolution
the enzyme belongs to the glycoside hydrolase family 5, GH5, subfamily 22
evolution
the enzyme belongs to the glycoside hydrolase family 39, GH39
evolution
the N-terminal domain of AnBX (Pro25-Gly358) adopts a TIM-barrel fold, but lacks the equivalent of first two beta-strands and two alpha-helices present in the structure of HvExoI
evolution
the enzyme belongs to the glycoside hydrolase family 39, GH39, clade II
evolution
-
the enzyme belongs to the glycoside hydrolase family 39, GH39
evolution
the enzyme belongs to the glycoside hydrolase family 43, GH43
evolution
the enzyme belongs to the glycoside hydrolase family 3, GH3, clade I
evolution
the enzyme belongs to the glycoside hydrolase family 43, GH43
evolution
the enzyme belongs to the glycoside hydrolase family 39, GH39
evolution
the enzyme belongs to the glycoside hydrolase family 43, GH43, subfamily 11
evolution
-
the enzyme belongs to the glycoside hydrolase family 3, GH3
evolution
the enzyme belongs to the glycoside hydrolase family 39, GH39
evolution
-
the enzyme belongs to the glycoside hydrolase family 43, GH43
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 3, GH3, clade I
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 3, GH3
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 39, GH39
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 39, GH39, clade II
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 11, GH11
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 39, GH39
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 39, GH39, clade II
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 5, GH5, subfamily 22
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 39, GH39
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 39, GH39, clade II
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 43, GH43, subfamily 12
-
evolution
Shouchella clausii TCCC 11004
-
the enzyme belongs to the glycoside hydrolase family 43, GH43
-
metabolism
-
beta-xylosidase combined with a xylanase had an additive effect on beechwood xylan hydrolysis, generating xylose as a final product
metabolism
the biotransformation pathway from notoginsenoside R1 to ginsenoside Rg1 cleaves the outer xylose moiety at position C-6 of notoginsenoside R1 via beta-xylosidase
metabolism
-
xylanase (EC 3.2.1.8) randomly degrade the internal beta-1,4-backbone of xylan by converting it into oligosaccharides, while beta-xylosidase further cleaves oligosaccharides into xylose, and simultaneously prevents xylanases from being inhibited by the end products of their hydrolysis. Synergistic effect of Xyn and XynB on xylan degradation
metabolism
-
xylanase (EC 3.2.1.8) randomly degrade the internal beta-1,4-backbone of xylan by converting it into oligosaccharides, while beta-xylosidase further cleaves oligosaccharides into xylose, and simultaneously prevents xylanases from being inhibited by the end products of their hydrolysis. Synergistic effect of Xyn and XynB on xylan degradation
-
metabolism
-
beta-xylosidase combined with a xylanase had an additive effect on beechwood xylan hydrolysis, generating xylose as a final product
-
metabolism
-
the biotransformation pathway from notoginsenoside R1 to ginsenoside Rg1 cleaves the outer xylose moiety at position C-6 of notoginsenoside R1 via beta-xylosidase
-
metabolism
-
the biotransformation pathway from notoginsenoside R1 to ginsenoside Rg1 cleaves the outer xylose moiety at position C-6 of notoginsenoside R1 via beta-xylosidase
-
metabolism
Ceratocystis fimbriata RM 35
-
beta-xylosidase combined with a xylanase had an additive effect on beechwood xylan hydrolysis, generating xylose as a final product
-
metabolism
-
the biotransformation pathway from notoginsenoside R1 to ginsenoside Rg1 cleaves the outer xylose moiety at position C-6 of notoginsenoside R1 via beta-xylosidase
-
physiological function
in T-DNA insertion mutant, mucilage release is both patchy and slow and seeds display delayed germination. Developmental analysis of mutant seeds reveals no change in mucilage secretory cell morphology, but changes in monosaccharide quantities are detected. Chemical and immunological analyses of mucilage extracted from bxl1 mutant seeds and antibody staining of developing seed coats reveal an increase in (1-5)-linked arabinans, suggesting that BXL1 is acting as an a-L-arabinofuranosidase in the seed coat
physiological function
-
the beta-xylosidase exhibits synergism with endoxylanase upon hydrolysis of glucuronoxylan as well as with alpha-L-arabinofuranosidase and endoxylanase upon hydrolysis of arabinoxylan. Addition of beta-xylosidases increases efficiency of hydrolysis of plant raw materials with high hemicellulose content such as maize cobs by the enzymic preparation Celloviridine G20x depleted of its own beta-xylosidase
physiological function
-
the beta-xylosidase exhibits synergism with endoxylanase upon hydrolysis of glucuronoxylan as well as with alpha-L-arabinofuranosidase and endoxylanase upon hydrolysis of arabinoxylan. Addition of beta-xylosidases increases efficiency of hydrolysis of plant raw materials with high hemicellulose content such as maize cobs by the enzymic preparation Celloviridine G20x depleted of its own beta-xylosidase
physiological function
when incubated in combination with bifunctional xylanase-ferulic acid esterase Xyn10D-Fae1A, Xyl3A improves the release of xylose monomers from a hemicellulosic xylan substrate, suggesting that these two enzymes function synergistically to depolymerize xylan
physiological function
RuBG3A or RuBG3B alone do not release any reducing sugars from xylan. The addition of each enzyme into the reaction mixture of xylanase XynR8 improves the liberation of reducing sugars. The addition of RuBG3A with an activity ratio of 10:1 (xylosidase/xylanase) increases the liberation to 218% of that in the presence of XynR8 alone
physiological function
RuBG3A or RuBG3B alone do not release any reducing sugars from xylan. The addition of each enzyme into the reaction mixture of xylanase XynR8 improves the liberation of reducing sugars. The addition of RuBG3B with an activity ratio of 5:1 (xylosidase/xylanase) increases the liberation to 169% of that in the presence of XynR8 alone. RuBG3B shows no synergism with xylanase XynR8 at the optimal pH 7.5, but at pH 5.5, indicating that RuBG3B may have different pH preferences between aryl xylosidic substrate 4-nitrophenyl-beta-D-xylopyranoside and xylooligisaccharide xylan
physiological function
-
screening of thermophilic and thermotolerant filamentous fungi for the production of beta-xylosidase and arabinanase at different temperatures. beta-Xylosidase and arabinanase activities from mycelial extract (intracellular form) are higher in cultures grown at high temperatures (35-40°C), while the correspondent extracellular activities are favorably secreted from cultures at 30°C. Aspergillus niger and Aspergillus thermomutatus are the filamentous fungi with the most expressive production of beta-xylosidase and arabinanase, respectively
physiological function
-
strain grows well on locust bean galactomannan, Solka floc, wheat bran and pectin and at 45°C
physiological function
-
strain grows well on locust bean galactomannan, Solka floc, wheat bran and pectin and at 45°C
physiological function
-
growth on corncobs (coarse) induces the highest titres of xylosidase and acetyl esterase
physiological function
endo-xylanase and beta-xylosidase are the major enzymes for hemicellulose hydrolysis, which play a significant role in biomass conversion
physiological function
-
the enzyme catalyzes the degradation of an anthocyanin component of Brunfelsia calycina, and the release of xylose and galactose due to hydrolysis of glycosidic bonds by BcXyl is detected. The enzyme is activated at the stage at which the rapid anthocyanin degradation occurrs
physiological function
enzyme BfdXYL2 can cleave mainly beta-1,4-D-xylopyranosidic linkages of xylo-oligosaccharides (XOS) substrates. BfdXYL2 is a typical exo-hydrolase exhibiting much higher activity against xylobiose, the shortest substrate, than the longer oligomeric and polymeric substrates. Even though the activity of BfdXYL2 against AOS is much lower than that against XOS, this enzyme can very slowly and partly remove the L-arabinose residues from the non-reducing end of arabino-oligosaccharides
physiological function
the enzyme is a thermostable bacterial GH5 family beta-D-xylosidase. It is active against beechwood xylan and rye arabinoxylan. It yields only xylose molecules as products of beechwood xylan hydrolysis
physiological function
beta-D-xylosidase is a vital exoglycosidase with the ability to hydrolyze xylooligosaccharides to xylose and to biotransform some saponins by cleaving outer beta-xylose. beta-Xylosidase Xln-DT has a high selectivity for cleaving the outer xylose moieties of natural saponins, such as notoginsenoside R1 and astragaloside IV, which produces the ginsenoside Rg1 with stronger anti-fatigue activity and produces cycloastragenol with stronger anti-aging activity, respectively
physiological function
the enzyme can convert flavonoids of epimedium, it converts epimedin B and epimedin C into icariin. Only icariin is currently included in the Chinese Pharmacopoeia as a quality marker (Q-marker) for epimedium flavonoids. Icariin has the functions of anti-aging, anti-inflammation, antioxidation, anti-osteoporosis, and ameliorating fibrosis
physiological function
Dt-Xyl3 demonstrates multifunctional activities on 4-nitrophenyl beta-D-xyloside, 4-nitrophenyl alpha-L-arabinofuranoside, and 4-nitrophenyl beta-D-glucopyranoside and has a high selectivity for cleaving the outer xylose moieties of 10-deacetyl-7-xylosyltaxol, which produces 10-deacetyl-taxol to semi-synthesize paclitaxel, a potential cancer treament drug
physiological function
-
the enzyme can convert flavonoids of epimedium, it converts epimedin B and epimedin C into icariin. Only icariin is currently included in the Chinese Pharmacopoeia as a quality marker (Q-marker) for epimedium flavonoids. Icariin has the functions of anti-aging, anti-inflammation, antioxidation, anti-osteoporosis, and ameliorating fibrosis
-
physiological function
-
growth on corncobs (coarse) induces the highest titres of xylosidase and acetyl esterase
-
physiological function
-
Dt-Xyl3 demonstrates multifunctional activities on 4-nitrophenyl beta-D-xyloside, 4-nitrophenyl alpha-L-arabinofuranoside, and 4-nitrophenyl beta-D-glucopyranoside and has a high selectivity for cleaving the outer xylose moieties of 10-deacetyl-7-xylosyltaxol, which produces 10-deacetyl-taxol to semi-synthesize paclitaxel, a potential cancer treament drug
-
physiological function
-
strain grows well on locust bean galactomannan, Solka floc, wheat bran and pectin and at 45°C
-
physiological function
-
strain grows well on locust bean galactomannan, Solka floc, wheat bran and pectin and at 45°C
-
physiological function
Irpex lacteus CD2
-
endo-xylanase and beta-xylosidase are the major enzymes for hemicellulose hydrolysis, which play a significant role in biomass conversion
-
physiological function
-
beta-D-xylosidase is a vital exoglycosidase with the ability to hydrolyze xylooligosaccharides to xylose and to biotransform some saponins by cleaving outer beta-xylose. beta-Xylosidase Xln-DT has a high selectivity for cleaving the outer xylose moieties of natural saponins, such as notoginsenoside R1 and astragaloside IV, which produces the ginsenoside Rg1 with stronger anti-fatigue activity and produces cycloastragenol with stronger anti-aging activity, respectively
-
physiological function
-
beta-D-xylosidase is a vital exoglycosidase with the ability to hydrolyze xylooligosaccharides to xylose and to biotransform some saponins by cleaving outer beta-xylose. beta-Xylosidase Xln-DT has a high selectivity for cleaving the outer xylose moieties of natural saponins, such as notoginsenoside R1 and astragaloside IV, which produces the ginsenoside Rg1 with stronger anti-fatigue activity and produces cycloastragenol with stronger anti-aging activity, respectively
-
physiological function
-
enzyme BfdXYL2 can cleave mainly beta-1,4-D-xylopyranosidic linkages of xylo-oligosaccharides (XOS) substrates. BfdXYL2 is a typical exo-hydrolase exhibiting much higher activity against xylobiose, the shortest substrate, than the longer oligomeric and polymeric substrates. Even though the activity of BfdXYL2 against AOS is much lower than that against XOS, this enzyme can very slowly and partly remove the L-arabinose residues from the non-reducing end of arabino-oligosaccharides
-
physiological function
-
the enzyme is a thermostable bacterial GH5 family beta-D-xylosidase. It is active against beechwood xylan and rye arabinoxylan. It yields only xylose molecules as products of beechwood xylan hydrolysis
-
physiological function
-
beta-D-xylosidase is a vital exoglycosidase with the ability to hydrolyze xylooligosaccharides to xylose and to biotransform some saponins by cleaving outer beta-xylose. beta-Xylosidase Xln-DT has a high selectivity for cleaving the outer xylose moieties of natural saponins, such as notoginsenoside R1 and astragaloside IV, which produces the ginsenoside Rg1 with stronger anti-fatigue activity and produces cycloastragenol with stronger anti-aging activity, respectively
-
additional information
A0A1L3GYC8
enzyme structural modeling, structure comparisons of GH39o family enzymes, overview. E160 is the general acid/base residue and E278 is the catalytic nucleophile, and 11 substrate recognition residues, i.e. H54, F115, N159, F166, H228, Y230, Y283, W316, F322, E324, F336, are also identified. The excellent tolerance of the enzyme against salt and reaction prduct inhibition may be attributed to its high structural flexibility caused by the high proportion of random coils. Interaction analysis of XYL21 and xylanase Xyn11-1, which show synergistic behaviour
additional information
-
the recombinant arbohydrate-binding module of PxXyl43A, named as CBM91, is specific for xylan-containing polysaccharides. It binds to insoluble xylans like birchwood xylan and oat spelt xylan, whereas it does not bind to cellulosic substrates such as ball-milled cellulose, carboxymethyl cellulose, or lichenan
additional information
modelling of notoginsenoside R1 in DtXyl active site identifies several hydrophobic residues interacting in close contact to the substrate hydrophobic core. Unlike other residues involved in substrate binding, these residues are not conserved among GH39 xylosidase family, and their physico-chemical properties can be correlated to the efficient binding and subsequent hydrolysis of Notoginsenoside R1
additional information
DtXyl enzyme is modelled as a monomer, as the substrate entrance channel is located opposite to oligomeric interfaces. Substrate docking and binding analysis. As for xylose ligand, Noto-R1 xyloside moiety interacts with the similar residues. Structure comparisons of beta-D-xylosidases
additional information
identification of amino acid residues for catalysis and binding of GH3 AnBX beta-xylosidase. Complete conservation of the residues that make up their active site pockets. These residues are Trp86, Glu88, Arg164, Lys203, His204, Met251, Asp288 (nucleophile), Cys289 and Glu500 (acid/base catalyst) in the former, and Trp105, Glu107, Arg183, Lys222, His223, Met270, Asp307 (nucleophile), Cys308 and Glu509 (acid/base catalyst), respectively, in the latter. Residues Glu88, Asp288 and Glu500 in AnBX constitute the conserved carboxylic acid triad in the active sites of GH3 beta-xylosidases, each of which could significantly contribute to the catalysis. Trp86 is responsible for the xyloside specificity of enzyme AnBX
additional information
-
molecular dynamics simulation indicating that XYLO shows a notable overall structural stability and an enlargement of substrate binding pocket under alkaline condition, resulting in the formation of a new hydrogen bond between substrate and Arg286 of XYLO, and the tight binding plays a key role in improving the XYLO activity with the increasing pH. Structure homology modelling, the tertiary structure model of XYLO is built using the structure of Bacillus pumilus beta-xylosidase (PDB ID 5ZQJ) as template (over 70% homology), substrate molecular docking, structure-function analysis, detailed overview
additional information
molecular docking of D-xylose and p-nitrophenyl-beta-D-xylopyranoside (pNPX) with beta-xylosidase Xln-DT, overview. Besides binding to the active sites at the bottom of the substrate channel, xylose can also bind to sites in the middle or entrance of the channel with different affinities, which may determine the xylose inhibition of beta-xylosidase, mutational analysis
additional information
enzyme HJ14GH43 has no signal peptide, and the protein is comprised of two domains, including a GH 43 domain (from K2 to A315) linked to a DUF1349 domain with unknown function (from V330 to E535, PF07081) via a linker (from P316 to T329, PKIEEKVFAPTYHT). Residues D14 and E186 residues of HJ14GH43 are the general base and acid, respectively. D127 is predicted to assist in correct function of the general acid, and S29, F31, W73, A74, F126, W145, H152, T206, H248, R287, and F504 are predicted to bind the substrate
additional information
-
molecular docking analysis shows the involvement of Glu525, Val237, Lys238, Val761, and Asn76 in XynB-ligand interaction. Molecular docking with substrate xylan, overview
additional information
-
molecular docking analysis shows the involvement of Glu525, Val237, Lys238, Val761, and Asn76 in XynB-ligand interaction. Molecular docking with substrate xylan, overview
-
additional information
-
modelling of notoginsenoside R1 in DtXyl active site identifies several hydrophobic residues interacting in close contact to the substrate hydrophobic core. Unlike other residues involved in substrate binding, these residues are not conserved among GH39 xylosidase family, and their physico-chemical properties can be correlated to the efficient binding and subsequent hydrolysis of Notoginsenoside R1
-
additional information
-
DtXyl enzyme is modelled as a monomer, as the substrate entrance channel is located opposite to oligomeric interfaces. Substrate docking and binding analysis. As for xylose ligand, Noto-R1 xyloside moiety interacts with the similar residues. Structure comparisons of beta-D-xylosidases
-
additional information
-
modelling of notoginsenoside R1 in DtXyl active site identifies several hydrophobic residues interacting in close contact to the substrate hydrophobic core. Unlike other residues involved in substrate binding, these residues are not conserved among GH39 xylosidase family, and their physico-chemical properties can be correlated to the efficient binding and subsequent hydrolysis of Notoginsenoside R1
-
additional information
-
DtXyl enzyme is modelled as a monomer, as the substrate entrance channel is located opposite to oligomeric interfaces. Substrate docking and binding analysis. As for xylose ligand, Noto-R1 xyloside moiety interacts with the similar residues. Structure comparisons of beta-D-xylosidases
-
additional information
-
molecular docking of D-xylose and p-nitrophenyl-beta-D-xylopyranoside (pNPX) with beta-xylosidase Xln-DT, overview. Besides binding to the active sites at the bottom of the substrate channel, xylose can also bind to sites in the middle or entrance of the channel with different affinities, which may determine the xylose inhibition of beta-xylosidase, mutational analysis
-
additional information
-
modelling of notoginsenoside R1 in DtXyl active site identifies several hydrophobic residues interacting in close contact to the substrate hydrophobic core. Unlike other residues involved in substrate binding, these residues are not conserved among GH39 xylosidase family, and their physico-chemical properties can be correlated to the efficient binding and subsequent hydrolysis of Notoginsenoside R1
-
additional information
-
DtXyl enzyme is modelled as a monomer, as the substrate entrance channel is located opposite to oligomeric interfaces. Substrate docking and binding analysis. As for xylose ligand, Noto-R1 xyloside moiety interacts with the similar residues. Structure comparisons of beta-D-xylosidases
-
additional information
-
the recombinant arbohydrate-binding module of PxXyl43A, named as CBM91, is specific for xylan-containing polysaccharides. It binds to insoluble xylans like birchwood xylan and oat spelt xylan, whereas it does not bind to cellulosic substrates such as ball-milled cellulose, carboxymethyl cellulose, or lichenan
-
additional information
Shouchella clausii TCCC 11004
-
molecular dynamics simulation indicating that XYLO shows a notable overall structural stability and an enlargement of substrate binding pocket under alkaline condition, resulting in the formation of a new hydrogen bond between substrate and Arg286 of XYLO, and the tight binding plays a key role in improving the XYLO activity with the increasing pH. Structure homology modelling, the tertiary structure model of XYLO is built using the structure of Bacillus pumilus beta-xylosidase (PDB ID 5ZQJ) as template (over 70% homology), substrate molecular docking, structure-function analysis, detailed overview
-
Show AA Sequence and Transmembrane Helices (1685 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
110000
120000
122000
150000
165000
17000
-
1 * 68000, catalytic subunit, 1 * 17000, carbohydrate binding subunit, SDS-PAGE
180000
200000
210000
245000
-
recombinant His-tagged enzyme, gel filtration
37000
39000
47305
50000
50700
55000
58000
4 * 58000, deduced from gene sequence, crystallization data
59700
-
x * 59700, protein with C-terminal His-tag, mass spectrometry
60000
61500
68000
75000
79894
2 * 79894, sequence calculation and crystal structure
80000
82000
83000
87000
90000
100000
Penicillium wortmanni
-
gel filtration, sucrose density gradient centrifugation, SDS-PAGE
47305
1 * 47305, mature protein, calculated from amino acid sequence
68000
-
1 * 68000, catalytic subunit, 1 * 17000, carbohydrate binding subunit, SDS-PAGE
75000
-
extra- and intracellular activity of beta-xylosidase-1, gel filtration, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterodimer
crystal structure analysis, overview. The N-terminal domain of AnBX (Pro25-Gly358) adopts a TIM-barrel fold, but lacks the equivalent of first two beta-strands and two alpha-helices present in the structure of HvExoI. The second domain (Ile387-Gly573) is an (alpha/beta)6 sandwich fold with six beta-strands and three helices on either side, which is similar to the second domain of HvExoI. The C-terminal domain (Thr630-Lys776) is the 7-stranded FnIII domain. In comparison to the FnIII domain of beta-glucosidase 3B from Thermotoga neapolitana, strand A of AnBX is shorter, and linked to strand B by a long loop containing a small beta-strand and short helices. The three domains are linked by long coils containing short helices. The electron densities of Ala1-Pro24 are not observed. Each molecule contains 3 disulfide bonds between Cys31-Cys42, Cys252-Cys263 and Cys289-Cys321 in the N-terminal domain. The entrance to the active site pocket of the E88A mutant is approximately 7.0 A high and 11.6 A, which is approximately the same size as those of other GH3 beta-xylosidases. Structure comparisons, overview
homodimer
monomer
oligomer
-
tetramer or trimer of 3-4 identical subunits of 56000-62000, SDS-PAGE
tetramer
trimer
additional information
?
x * 95100, recombinant enzyme as N-terminal fusion protein with the alpha-mating factor signal sequence and a poly-histidine tag, calculated from amino acid sequence
?
x * 130000, glycosylated recombinant enzyme, calculated from amino acid sequence
?
x * 85000-90000, deglycosylated recombinant enzyme, calculated from amino acid sequence
?
-
x * 95100, recombinant enzyme as N-terminal fusion protein with the alpha-mating factor signal sequence and a poly-histidine tag, calculated from amino acid sequence
-
?
-
x * 130000, glycosylated recombinant enzyme, calculated from amino acid sequence
-
?
-
x * 85000-90000, deglycosylated recombinant enzyme, calculated from amino acid sequence
-
?
x * 59011, sequence calculation, x * 59000, recombinant His6-tagged enzyme, SDS-PAGE
?
-
x * 59011, sequence calculation, x * 59000, recombinant His6-tagged enzyme, SDS-PAGE
-
?
x * 37400, about, sequence calculation, x * 39300, recombinant His-tagged enzyme, SDS-PAGE
?
x * 39423, His6-tagged enzyme, Q-TOF mass spectrometry
?
x * 54000, SDS-PAGE of recombinant protein carrying an alpha secretion signal peptide
?
-
x * 59700, protein with C-terminal His-tag, mass spectrometry
dimer
2 * 79894, sequence calculation and crystal structure
dimer
-
1 * 68000, catalytic subunit, 1 * 17000, carbohydrate binding subunit, SDS-PAGE
dimer
2 * 54000, recombinant His-tagged enzyme, SDS-PAGE
monomer
-
1 * 60000-75000, beta-xylosidase-1, SDS-PAGE, gel filtration
monomer
DtXyl enzyme is modelled as a monomer, as the substrate entrance channel is located opposite to oligomeric interfaces
monomer
-
DtXyl enzyme is modelled as a monomer, as the substrate entrance channel is located opposite to oligomeric interfaces
-
monomer
-
DtXyl enzyme is modelled as a monomer, as the substrate entrance channel is located opposite to oligomeric interfaces
-
monomer
-
DtXyl enzyme is modelled as a monomer, as the substrate entrance channel is located opposite to oligomeric interfaces
-
monomer
1 * 47305, mature protein, calculated from amino acid sequence
monomer
-
1 * 47305, mature protein, calculated from amino acid sequence
-
monomer
-
small-angle X-ray scattering and circular dichroism spectroscopy, structure analysis, overview
tetramer
4 * 58000, deduced from gene sequence, crystallization data
tetramer
-
4 * 58000, deduced from gene sequence, crystallization data
-
additional information
enzyme HJ14GH43 has no signal peptide, and the protein is comprised of two domains, including a GH 43 domain (from K2 to A315) linked to a DUF1349 domain with unknown function (from V330 to E535, PF07081) via a linker (from P316 to T329, PKIEEKVFAPTYHT)
additional information
-
enzye PxXyl43A is composed of a glycoside hydrolase (GH) family 43, subfamily 12, catalytic module and a carbohydrate-binding module, named as CBM91, specific for xylan-containing polysaccharides, domain structure, overview
additional information
-
enzye PxXyl43A is composed of a glycoside hydrolase (GH) family 43, subfamily 12, catalytic module and a carbohydrate-binding module, named as CBM91, specific for xylan-containing polysaccharides, domain structure, overview
-
additional information
-
coordinate interaction of enzyme with alpha-L-arabinofuranosidase and xylanase
additional information
-
coordinate interaction of enzyme with alpha-L-arabinofuranosidase and xylanase
-
additional information
small-angle X-ray scattering (SAXS) data enables reconstruction of the enzyme's low-resolution molecular envelope and reveals that it forms dimers in solution
additional information
-
small-angle X-ray scattering (SAXS) data enables reconstruction of the enzyme's low-resolution molecular envelope and reveals that it forms dimers in solution
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
additional information
glycoprotein
-
treatment with PNGase F results in a decrease in molecular weight to approximately 85000 Da confirming that the purified enzyme is glycosylated
glycoprotein
Aspergillus niger DSM 22593
-
treatment with PNGase F results in a decrease in molecular weight to approximately 85000 Da confirming that the purified enzyme is glycosylated
-
glycoprotein
sequence contains a potential N-glycosylation site at N243
glycoprotein
protein is N-glycosylated, 6% carbohydrate contnet. Presence of 16 putative N-glycosylation sites
glycoprotein
Aureobasidium melanogenum ATCC 20524
-
protein is N-glycosylated, 6% carbohydrate contnet. Presence of 16 putative N-glycosylation sites
-
glycoprotein
-
active enzyme after deglycosylation by endoglycosidase H
glycoprotein
molecular mass of deglycosylated protein is 66000 Da
glycoprotein
-
13.5% carbohydrate moiety, arabinose, galactose residues
additional information
sequence contains no potential secretion signal peptides
additional information
-
sequence contains no potential secretion signal peptides
additional information
there is no predicted N-glycosylation site for RrXyl43A
additional information
-
there is no predicted N-glycosylation site for RrXyl43A
additional information
Rhizophlyctis rosea NBRC 105426
-
there is no predicted N-glycosylation site for RrXyl43A
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant E88A mutant of AnBX, sitting drop vapor diffusion method, mixing of 18 mg/ml protein with 16% v/v ethylene glycol, 0.1 M citric acid, pH 3.5, and 10% w/v PEG 6000, 20°C, X-ray diffraction structure determination and analysis at 2.50 A resolution, molecular replacement method using the structure of AnidXlnD (PDB ID 6Q7I) as a search model
purified recombinant enzyme, hanging drop vapour diffusion method, mixing of equal volumes of 7-10 mg/ml protein in 50 mM Tris-HCl, 0.2 M NaCl, and 10% w/v glycerol, pH 7.3, with commercial crystallization solution, X-ray diffraction structure determination and analysis, molecular replacement method using GH 43 beta-xylosidase from Bacillus subtilis (PDB ID 1YIF) as a template
purified recombinant His-tagged enzyme free or bound to xylose, sitting drop vapor diffusion method, mixing of 1 mg/ml enzyme protein in HEPES 0.1 M, pH 7.5, and 1 mM DTT with crystallization solution containing 10% w/v PEG 4000, 100 mM tri-sodium citrate, pH 5.6, and 200 mM ammonium sulfate, ligand-free crystals are obtained from 22% w/v PEG 4000, 100 mM tri-sodium citrate, pH 5.6, and 200 mM ammonium sulfate, method optimization, X-ray diffraction structure determination and analysis at 2.67-2.72 A resolution, molecular replacement using the structure with PDB ID 1PX8 as template, modelling
in complex with substrate xylobiose. The xylose moiety at the K1 subsite is held by a large number of hydrogen bonds, whereas only one hydroxyl of the xylose unit at the C1 subsite can create hydrogen bonds with the enzyme. The general base, Asp15, is located on the alpha-side of the K1 xylose sugar ring, 5.2 A from the anomeric carbon. This location enables it to activate a water molecule for a single displacement attack on the anomeric carbon, resulting in inversion of the anomeric configuration. Glu187, the general acid, is 2.4 A from the glycosidic oxygen atom and can protonate the leaving aglycon. The third catalytic carboxylic acid, Asp128, is 4 A from the general acid, modulating its pKa and keeping it in the correct orientation relative to the substrate
-
purified recombinant enzyme, hanging drop vapour diffusion method, 0.002 ml protein solution containing 5 mg/ml protein in 50 mM Tris-HCl, pH 7.0, 100 mM NaCl, and 0.02% NaN3, is mixed with 0.002 ml well solution containing 2.3-2.4 M ammonium sulfate, and 40-60 mM sodium citrate at pH 5.5, a few weeks, X-ray diffraction structure determination and analysis at 2.0 A resolution
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
hanging-drop vapor-diffusion method at 10°C, crystal structures of the enzyme in the unliganded form and with bound products, at 1.7 A resolution. The structures are very similar to those of other enzymes belonging to glycoside hydrolase family 43. The monosaccharides are bound in very different ways. Arabinose preferentially binds in subsite -1, while xylose exclusively interacts with subsite +1
two crystal forms. Bipyramid shaped crystals of space group P432121, diffraction to 1.55 A, and rectangular crystals of space group P21, diffracting to 1.8 A resolution
vapour-diffusion method at 289 K, resolution to 2.5 A. Crystals belong to the monoclinic space group C2, with unit-cell parameters a 142.2 A, b 129.5 A, c 01.4 A , beta 119.8°
both D-xylose-bound enzyme and a covalent 2-deoxy-2-fluoro-alpha-D-xylosyl-enzyme intermediate complex
-
molecular docking studies for the enzyme with the substrates xylobiose and 4-nitrophenyl-beta-D-xylopyranoside. The essential catalytic residues of RuBG3A are D297 and E499. Besides D113, K218, H219, and R185 also form hydrogen bonds with substrates and are condervative. The active center for beta-glucosidic and beta-xylosidic substrates are the same and the bifunctional activity should come from one functional domain. RuBG3A and RuBG3B exhibit higher scores in the docking analysis against 4-nitrophenyl-beta-D-glucopyranoside than against 4-nitrophenyl-beta-D-xylopyranoside, indicating a larger affinity between the enzymes and 4-nitrophenyl-beta-D-glucopyranoside, which is consistent with the kinetic parameters
molecular docking studies for the enzyme with the substrates xylobiose and 4-nitrophenyl-beta-D-xylopyranoside. The essential catalytic residues of RuBG3B are D272 and E481. Besides D88, K193, H194, and R160 also form hydrogen bonds with substrates and are condervative. The active center for beta-glucosidic and beta-xylosidic substrates are the same and the bifunctional activity should come from one functional domain. RuBG3A and RuBG3B exhibit higher scores in the docking analysis against 4-nitrophenyl-beta-D-glucopyranoside than against 4-nitrophenyl-beta-D-xylopyranoside, indicating a larger affinity between the enzymes and 4-nitrophenyl-beta-D-glucopyranoside, which is consistent with the kinetic parameters
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C289W
site-directed mutagenesis, the mutation reduces catalytic efficiency toward all four substrates tested, reduced catalytic activity compared to wild-type
E88A
site-directed mutagenesis, mutant structure analysis, overview
E88D
site-directed mutagenesis, the mutation reduces catalytic efficiency toward all four substrates tested, reduced catalytic activity compared to wild-type
W86A
site-directed mutagenesis, the mutation in AnBX increases the preference for glucoside substrates relative to xyloside substrates, reduced catalytic activity compared to wild-type
W86D
site-directed mutagenesis, the mutation in AnBX increases the preference for glucoside substrates relative to xyloside substrates, reduced catalytic activity compared to wild-type
W86S
site-directed mutagenesis, the mutation in AnBX increases the preference for glucoside substrates relative to xyloside substrates, reduced catalytic activity compared to wild-type
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
E335G
nucleophile-deficient mutant enzyme can function as an efficient glycosynthase, using alpha-D-xylopyranosyl fluoride as a donor and various aryl sugars as acceptors. The mutant enzyme can also catalyze the self-condensation reaction of alpha-D-xylopyranosyl fluoride, providing mainly alpha-D-xylobiosyl fluoride
E335G
-
nucleophile-deficient mutant enzyme can function as an efficient glycosynthase, using alpha-D-xylopyranosyl fluoride as a donor and various aryl sugars as acceptors. The mutant enzyme can also catalyze the self-condensation reaction of alpha-D-xylopyranosyl fluoride, providing mainly alpha-D-xylobiosyl fluoride
-
biofuel production
E186A
-
The E186A mutation abolishes the pKa assigned to the catalytic acid E186, mutant enzyme binds only the neutral aminoalcohol triethanolamine, whereas wild-type enzyme binds only the cationic aminoalcohol. At pH 7.0 and 25°C, the ratio of kcat values for substrates 4-nitrophenyl-beta-D-xylopyranoside and 4-nitrophenyl-alpha-L-arabinofuranoside of E186A is 100fold that of wild-type enzyme
additional information
biofuel production
potential application in the field of biomass pretreatment and biofuel production
biofuel production
Irpex lacteus CD2
-
potential application in the field of biomass pretreatment and biofuel production
-
additional information
generation of a bifunctional enzyme consisting of a GH11 endo-1,4-beta-xylanase fused to a GH43 beta-xylosidase, both from Bacillus subtilis. The substrate cleavage rate is altered by the molecular fusion improving at least 3fold the xylose production using specific substrates as beechwood xylan and hemicelluloses from pretreated biomass. The chimeric enzyme shows higher thermotolerance with a positive shift of the optimum temperature from 35°C to 50°C for xylosidase activity
additional information
-
generation of a bifunctional enzyme consisting of a GH11 endo-1,4-beta-xylanase fused to a GH43 beta-xylosidase, both from Bacillus subtilis. The substrate cleavage rate is altered by the molecular fusion improving at least 3fold the xylose production using specific substrates as beechwood xylan and hemicelluloses from pretreated biomass. The chimeric enzyme shows higher thermotolerance with a positive shift of the optimum temperature from 35°C to 50°C for xylosidase activity
additional information
-
generation of a bifunctional enzyme consisting of a GH11 endo-1,4-beta-xylanase fused to a GH43 beta-xylosidase, both from Bacillus subtilis. The substrate cleavage rate is altered by the molecular fusion improving at least 3fold the xylose production using specific substrates as beechwood xylan and hemicelluloses from pretreated biomass. The chimeric enzyme shows higher thermotolerance with a positive shift of the optimum temperature from 35°C to 50°C for xylosidase activity
-
additional information
recombinant alpha-L-rhamnosidase BtRha (EC 3.2.1.40) from Bacteroides thetaiotaomicron strain VPI-5482 can convert epoetin C to produce icariin. From a combination of BbXyl and BtRha, the conversion of epimedium total flavonoids in vitro and in vivo to obtain product icariin is catalyzed. Under optimal conditions, in vitro hydrolysis of 5 g/l of total flavonoids of epimedium eventually yield a concentration of icariin of 678.1 micromol/l. To explore the conversion of total flavonoids of epimedium in vivo. Under the optimal conditions, the yield of icariin reached 97.27 micromol/l when the total flavonoid concentration of epimedium is 1 g/l
additional information
-
recombinant alpha-L-rhamnosidase BtRha (EC 3.2.1.40) from Bacteroides thetaiotaomicron strain VPI-5482 can convert epoetin C to produce icariin. From a combination of BbXyl and BtRha, the conversion of epimedium total flavonoids in vitro and in vivo to obtain product icariin is catalyzed. Under optimal conditions, in vitro hydrolysis of 5 g/l of total flavonoids of epimedium eventually yield a concentration of icariin of 678.1 micromol/l. To explore the conversion of total flavonoids of epimedium in vivo. Under the optimal conditions, the yield of icariin reached 97.27 micromol/l when the total flavonoid concentration of epimedium is 1 g/l
-
additional information
construction of Xln-DT mutants Xln-DT-284ASP and Xln-DT-284ALA, the mutants show high xylose tolerance, with the Ki values of 4602 mM and 3708 mM, respectively, an increase of 9-35% compared to wild-type Xln-DT. The thermostability of mutant Xln-DT-284ASP is significantly improved at 75-85°C. While the activity of the wild-type enzyme Xln-DT decreases to 40-20% at that temperature, the activity of the mutant enzyme still remains at 100%. The mutant Xln-DT-284ALA shows excellent stability at pH 4.0-7.0, mutant Xln-DT-284ASP shows slightly decreased activity compared to wild-type. Temperature and pH profiles of wild-type and mutant enzymes, overview
additional information
-
construction of Xln-DT mutants Xln-DT-284ASP and Xln-DT-284ALA, the mutants show high xylose tolerance, with the Ki values of 4602 mM and 3708 mM, respectively, an increase of 9-35% compared to wild-type Xln-DT. The thermostability of mutant Xln-DT-284ASP is significantly improved at 75-85°C. While the activity of the wild-type enzyme Xln-DT decreases to 40-20% at that temperature, the activity of the mutant enzyme still remains at 100%. The mutant Xln-DT-284ALA shows excellent stability at pH 4.0-7.0, mutant Xln-DT-284ASP shows slightly decreased activity compared to wild-type. Temperature and pH profiles of wild-type and mutant enzymes, overview
-
additional information
-
the recombinant xylanase Xyn (EC 3.2.1.8) and beta-xylosidase XynB exhibit synergistic hydrolysis of beechwood xylan and pretreated lignocellulose, where Xyn and XynB pre-hydrolysis achieve an improvement of pretreated lignocellulose hydrolysis by commercial cellulase
additional information
-
the recombinant xylanase Xyn (EC 3.2.1.8) and beta-xylosidase XynB exhibit synergistic hydrolysis of beechwood xylan and pretreated lignocellulose, where Xyn and XynB pre-hydrolysis achieve an improvement of pretreated lignocellulose hydrolysis by commercial cellulase
-
additional information
-
combinantion of recombinant enzyme XYLO with an endo-xylanase (EC 3.2.1.8) results in high xylose yields by hydrolyzing alkali-extracted xylan from agricultural wastes
additional information
Shouchella clausii TCCC 11004
-
combinantion of recombinant enzyme XYLO with an endo-xylanase (EC 3.2.1.8) results in high xylose yields by hydrolyzing alkali-extracted xylan from agricultural wastes
-
additional information
-
formation of magnetic CLEAs of the beta-xylosidase rBxTW1 and the mutant multi-glycoligase rBxTW1-E495A derived from it. Magnetic cross-linked enzyme aggregates (mCLEAs) of rBxTW1 keep the excellent hydrolytic and O-transxylosylating activities of the free enzyme and have improved thermal and pH stability. Multi-glycoligases are able not only to synthesize O-xylosides, but also N- and S-xylosides. The mCLEAs of the mutant enzyme also maintains or improves the catalytic properties of the soluble enzyme, synthetizing the O-xylosides of vanillin and (-)-epigallocatechin gallate, and the N- and S-xyloside of 3,5-dibromo-1,2,4-triazole and thiophenol, respectively. The mCLEAs are recyclable across 4 cycles of synthesis of the O-xylosides through a green and highly selective process. The magnetic properties of the scaffold used for immobilization may allow the easy recovery and reuse of the biocatalyst even from reactions containing insoluble lignocellulosic biomass. Functionalization of nude magnetic nanoparticles, nanoparticles activated with glutaraldehyde, method, overview. Conducting four consecutive reaction cycles of O-transglycosylation, with hydroxytyrosol and vanillyl alcohol as acceptors for rBxTW1 mCLEAs and vanillin and EGCG for mCLEAs of multi-glycoligase. The thermostability of the mCLEAs of rBxTW1 widely surpasses that of the free enzyme, that is nearly inactive after 72 h at 50°C. The mCLEAs maintain 81% of their initial activity at this temperature, and even around 10% at 60°C, and show much higher activity at 30°C and 40°C. Similarly, the CLEAS show enhanced pH stability at over pH 5.0, and especially at pH 8.0 and pH 9.0
additional information
-
with use of vector pHsh, expression of XylC increases approximately 4fold when a loop within the translational initiation region in the mRNA is removed by site-directed mutagenesis. The increased expression of xylCm is due to removal of a stem-loop structure without a change of the amino acid sequence of the heterologously expressed enzyme
additional information
with use of vector pHsh, expression of XylC increases approximately 4fold when a loop within the translational initiation region in the mRNA is removed by site-directed mutagenesis. The increased expression of xylCm is due to removal of a stem-loop structure without a change of the amino acid sequence of the heterologously expressed enzyme
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 6.5
the recombinant enzyme is stable up to pH 6.5, when incubated at 4°C for 4 h
2.2 - 9
the enzyme retains more than 80% activity after 72 h at pH 2.2-9.0
2.9
-
pH 5.0, room temperature, 12 h, the enzyme maintains 73.1% of its maximal activity
2.9 - 8
-
the enzyme maintains significant activity when pre-incubated at pH from 2.9 to 8.0 for 12 h, with 73.1% and 51.5% of its maximum activity, respectively
3 - 8
3 - 9
-
the enzyme is stable at pH range 4.0-9.0 for 4 h and retains 75 and 100% activity at pH 3.0 and 9.0, respectively, after incubation for 24 h
4 - 12
the enzyme retains more than 80% residual activity after incubation at pH range of 4.0 to 12.0 for 24 h
4 - 5.5
purified recombinant His-tagged enzyme, over 80% activity remaining after 24 h
4 - 7.5
4 - 9
A0A1L3GYC8
purified recombinant enzyme, over 60% activity remaining at pH 5.0-7.5, 30% at pH 8.0, inactivation at pH 4.0 and pH 9.0
4.5 - 8
purified recombinant enzyme, stable for about 4 h in this pH range at 45°C in the absence of substrate
5 - 10
stable, over 80% activity remaining, purified recombinant enzyme
6 - 8
6 - 9
6.5 - 9.5
-
the enzyme retains more than 60% activity between pH 6.5 and 9.5 for 24 h
7.5
-
activity decreases above, involvement of an essential acid-base group, which is protonated for catalysis
additional information
pH profiles of wild-type and mutant enzymes, overview
4
-
soluble beat-xylosidase I, highly stable up to, immobilized beta-xylosidase II 10 times more stable
4 - 7.5
-
stable within a pH range of 4.0-7.5. The residual beta-xylosidase activity is more than 50% of the original purified enzyme activity after 1 h of incubation at 75 °C in the pH range from 4.5 to 7.5 at the absence of the substrate
6 - 8
purified recombinant His-tagged enzyme, completely stable for 24 h
6 - 9
purified recombinant HJ14GH43 is most active and stable at pH 7.0, below 40% activity at pH 6.0 and pH 9.0
6 - 9
the enzyme is relatively stable in the range of pH 6.0 to 9.0, retaining more than 61% residual activity after 30 min of incubation
8
-
pH 5.0, room temperature, 12 h, the enzyme maintains 51.1% of its maximal activity
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 30
the recombinant enzyme is stable at 20°C, but shows poor stability at temperatures over 20 °C, half-lives of less than 20 min are observed at 25°C and 30°C. The purified recombinant enzyme shows loss of 80% activity after 10 min
30
30 - 50
30 - 60
the recombinant enzyme shows thermostability up to 60°C with more than 60% activity remaining after incubation at this temperature for 30 min
35
35 - 50
the enzyme loses 40% of its activity at 35°C and 90% at 50°C after 30 min of incubation
40
40 - 52
-
the activity of purified recombinant PxXyl43A is stably maintained at 40-52°C, but decreases drastically at temperatures higher than 52°C, profile overview
45
45 - 50
purified recombinant enzyme, over 80% activity remaining
50
55
55 - 60
-
the enzyme retains 94.4% activity after incubation at 55°C for 1 h and 75.4% activity at 60°C for 1 h
60
65
65 - 85
purified recombinant enzyme, pH 6.0, above 60% activity remaining after 2 h
70
75
75 - 85
purified recombinant His-tagged enzyme, pH 5.0, the thermostability of enzyme Dt-xyl3 significantly decreases over 75°C within 30 min and is completely lost at 85°C after 30 min
80
85
24 h, soluble enzyme and enzyme immobilized by entrapment into alginate are completely stable
90
95
additional information
30
purified recombinant His-tagged enzyme, 1 h, loss of 24% activity
30 - 50
the enzyme remains stable up to 50°C after 30 min of incubation but the activity rapidly decreases when the temperature above 50°C
30 - 50
the enzyme retains more than 70% activity and more than 50% activity after 72 h at 30-40 or 50°C, respectively
35
purified recombinant His-tagged enzyme, 1 h, loss of 48% activity
40
purified recombinant His-tagged enzyme, 1 h, loss of 80% activity
40
the enzyme retains more than 80% activity after incubation for 66 h
45
A0A1L3GYC8
purified recombinant enzyme, pH 5.5, 60 min, loss of 10 % activity
50
the enzyme keeps almost 100% of its initial activity when incubating below 50°C for 2 h at pH 6.0
50
t1/2: 0.14 h, without Ca2+, the addition of Ca2+ improves enzyme stability at 50 °C
50
purified recombinant enzyme, pH 5.0, fully stable during 4 h
50
the enzyme retains more than 80% activity after incubation for 66 h
55
-
half-life of the xylan-inducible enzyme is 9 min, of the xylose-inducible enzyme 18 min
55
purified recombinant enzyme, loss of 80% activity after 10 min, inactivated after 60 min
55
t1/2: 29.7 h. The enzyme retains 47% of its activity after 30 h incubation at 55°C, the enzyme retains 90% of its activity after 24 h incubation at 55°C
55
-
the enzyme is more thermostable at 55°C and pH 7 retaining 80% activity for 90 min
55
A0A1L3GYC8
purified recombinant enzyme, pH 5.5, about 5% activity after 5 min and complete loss of activity after 10 min
60
-
12 h, enzyme retains 80% of its initial activity. Half-life: 38 h
60
-
the enzyme maintains 70% of its maximum activity after 24 h of incubation at 60°C
60
purified recombinant enzyme, pH 5.0, 3 h, inactivation
60
purified recombinant enzyme, inactivation within about 3 min
65
-
highly stable at pH 4.0, immobilized beta-xylosidase II 10 times more stable
65
purified recombinant His-tagged enzyme, pH 5.0, 88% activity remaining after 1 h
65
-
half-life is 11 min in absence of Ca2+, half-life is 30 min in presence of Ca2+
70
purified recombinant enzyme, pH 5.0, 10 min, inactivation
70
-
residual activity is more than 85% of its original activity after being incubated at 70°C for 2 h
75
-
51.13% activity is retained after 1 h. 15% activity is retained up to 3 h
90
half life of enzyme immobilized by entrapment into alginate: 21 h. Half-life of soluble enzyme: 10 h
90
-
residual activity is more than 50% of its original activity after being incubated at 90°C for 2 h
95
purified recombinant enzyme, pH 6.0, half-life is approximately 1 h
additional information
temperature profiles of wild-type and mutant enzymes, overview
additional information
temperature profile and thermal stability
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
coating the enzyme with aldehyde-dextran or polyethylenimine, fully stabilizes the quaternary structure of the enzyme rendering much more stabilization to the biocatalyst. The enzyme coated with polyethylenimine of molecular weight 1300 is the most stable one exhibiting an half-life of more than 10 days at pH 5.0 and 50°C, being 240fold more stable than the free enzyme
-
immobilized enzyme shows good operational stability retaining 84% of its initial activity and yielding 63% xylose after four cycles of reusing
improved pH- and temperature-stability as native sucrase-cellobiase-xylosidase aggregate
-
recombinant enzyme HJ14GH43 shows moderate or high activity, but poor stability in NaCl, KCl, NaNO3, KNO3, Na2SO4, and (NH4)2SO4 at concentrations from 3.0 to 30.0% w/v. Approximately one-third of the surface of rHJ14GH43 is positively charged, which may be the primary factor responsible for poor stability in high neutral salt environments
the recombinant enzyme displays high tolerance to salts with 60.8% activity in 20% w/v NaCl
xylose protects against thermal inactivation
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DMSO
Ethanol
Methanol
additional information
Ethanol
5% (v/v), 112.7% activity compared to activity without addition of ethanol, 1.25 mM 4-nitrophenyl-beta-D-xylopyranoside as substrate, pH 4.6, 40°C
Ethanol
5% (v/v), 316.9% activity compared to activity without addition of ethanol, 1.25 mM 4-nitrophenyl-beta-D-xylopyranoside as substrate, pH 4.6, 42°C
Methanol
5% (v/v), 94.3% activity compared to activity without addition of methanol, 1.25 mM 4-nitrophenyl-beta-D-xylopyranoside as substrate, pH 4.6, 40°C
Methanol
5% (v/v), 167% activity compared to activity without addition of methanol, 1.25 mM 4-nitrophenyl-beta-D-xylopyranoside as substrate, pH 4.6, 42°C
additional information
ethanol and methanol at 5-15% show little effect on the enzymatic activity
additional information
-
ethanol and methanol at 5-15% show little effect on the enzymatic activity
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, soluble enzyme, retains 50% of the activity after 2 months
4°C, the enzyme immobilized by entrapment into alginate retains 38% activity after 1 year
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE-Sephadex gel filtration, SP Sepharose column chromatography and BioGel P-300 gel filtration
ammonium sulfate precipitation, QAE cellulose column chromatography, butyl Toyopearl column chromatography, hydroxyapatite column chromatography, and Q Sepharose column chromatography
ammonium sulfate precipitation, QAE-Sephadex A50 ion exchange column chromatography, and Superdex 200 gel filtration
-
DEAE-Sepharose column chromatography and Sephacryl S-300 gel filtration
-
further purification from commercially available enzyme by 2step chromatogarphy
-
HisTrap column chromatography
HiTrap column chromatography, Mono S column chromatography, and Superose 12 gel filtration
native enzyme 125fold from mycelium by heat treatment at 50°C, ammonium sulfate fractionation, gel filtration, and ion exchange chromatography
-
native enzyme 53fold by ion exchange chromatography and gel filtration to homogeneity
-
native enzyme 9.3fold from mycelium, by ammonium sulfate fractionation, 2 steps of ion exchange chromatography, and gel filtration
native enzyme by acetone precipitation, freeze-drying, gel filtration, anion exchange chromatography, and a second step of gel filtration
native enzyme from stem, 29.1fold by concanavalin A affinity chromatography, cation exchange chromatography, and gel filtration to homogeneity
native enzyme from stem, 40.3fold by concanavalin A affinity chromatography, cation exchange chromatography, and gel filtration to homogeneity
partial
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant enzyme from Escherichia coli strain BL21(DE3) to near homogeneity
recombinant extracellular His-tagged enzyme from Bacillus subtilis culture medium by heat treatment at 60°C for 30 min, followed by nickel affinity chromatography
-
recombinant full-length His6-tagged enzyme from Escherichia coli by nickel affinity chromatography
recombinant His-tagged enzyme 2.59fold from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to homogeneity
recombinant His-tagged enzyme 2.91fold from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged enzyme 2.94fold from Escherichia coli strain BL21(DE3) by heat treatment at 75°C for 30 min, followed by nickel affinity chromatography
recombinant His-tagged enzyme 3.07fold from Escherichia coli strain BL21(DE3) by heat treatment and nickel affinity chromatography
recombinant His-tagged enzyme 5.78fold from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged enzyme 7fold from Escherichia coli by heat treatment and nickel affinity chromatography to homogeneity
-
recombinant His-tagged enzyme from Escherichia coli strain BL21 pLysS (DE3) by nickel affinity chromatography, ultrafiltration, and gel filtration
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain Rosetta (DE3) pLysS by nickel affinity chromatography, tag cleavage by TEV protease
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant N-terminally His6-tagged enzyme BoGH43A from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain Rosetta(DE3) by heat treatment for 15 min at 70°C, followed by nickel affinity chromatography and gel filtration, to homogeneity
recombinant protein
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
to homogeneity
to homogeneity by 2step chromatography
to homogeneity by 3step chromatography techniques
to homogeneity by 4step chromatography
to homogeneity by 4step chromatography techniques
to homogeneity by chromatography and electrophoretic steps
Malbranchea pulchella var. sulfurea
-
to homogeneity by chromatography steps, separation of beta-xylosidase 1 and beta-xylosidase 2
-
to homogeneity by heat treatment and 2step chromatography techniques
-
to homogeneity, 4step chromatography techniques
two forms of native enzyme from mycelium by ion exchange chromatography, xylose-inducible enzyme form 11.3fold, xylan.inducible enzyme form 12.3fold, ammonium sulfate, and gel filtration
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
A0A1L3GYC8
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
BfdXYL2, cloning and recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
expressed in Escherichia coli BL21(DE3) cells
expressed in Pichia pastoris strains Y11430 and KM71H as an N-terminal fusion protein with the alpha-mating factor signal sequence and a poly-histidine tag
expression in Aspergillus oryzae
expression in Escherichia coli
expression in Escherichia coli BL21
expression in Pichia pastoris
full-length protein is expressed in Escherichia coli as an N-terminal or C-terminal His-tagged fusions protein
W0BU85
gene BbXyl, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene bxl2, ORF2, DNA and amino acid sequence determination and analysis
gene bxtw1, recombinant expression of wild-type and mutant enzymes in Pichia pistorius strain GS115
-
gene DICTH_1792, recombinant expression of N-terminallyHis6-tagged enzyme in Escherichia coli strain Rosetta(DE3), subcloning in Escherichia coli strain DH5alpha
gene xln-DT, DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene xyl1, cDNA library construction, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene xyl1, DNA and amino acid sequence determination and analysis, expression and phylogenetic analysis
gene xyl21, cloning from soil environment DNA, subcloning in Escherichia coli strain DH5alpha, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
A0A1L3GYC8
gene xyl4, DNA and amino acid sequence determination and analysis, expression and phylogenetic analysis
gene xynB, recombinant expression of His-tagged enzyme in Bacillus subtilis from vector pWB980, the enzyme is secreted
-
gene xynB2, overexpression of the soluble enzyme in Escherichia coli strain BL21(DE3)
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)
Gt-Xyl, sequence comparisons and phylogenetic tree, recombinant expression of soluble His6-tagged enzyme in Escherichia coli strain BL21(DE3)
locus ORY16049, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 pLysS (DE3)
overexpression in Escherichia coli
PxXyl43A, cloning and DNA and amino acid sequence determination, phylogenetic analysis and phylogenetic tree of GH43 enzymes, recombinant expression of full-length enzyme in Escherichia coli strains JM109 and BL21(DE3), subcloning in Escherichia coli strains alphaINV and ME9806
-
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta (DE3) pLysS, subcloning in Escherichia coli strain DH10B
recombinant expression of N-terminally His6-tagged enzyme BoGH43A in Escherichia coli strain BL21(DE3)
-
recombinant expression of wild-type and mutant enzymes
XylRBM26, cloning and DNA and amino acid sequence determination, sequence comparisons and phylogenetic analysis and phylogenetic tree of GH43 enzymes, recombinant expression of full-length, N-terminally His6-tagged enzyme in Escherichia coli
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
maximum activity is detected in cultures grown in Vogel's medium containing oat-spelt xylan
-
optimized medium composition for production of xylanase/beta-xylosidase is 3.24% wheat straw (steam pretreated, particle size approx. 0.25 mm), 1.32% pharmamedia and 0.49% KH2PO4, leading to 5347.4 nkat/ml of xylanase, 3.0 nkat/ml of beta-xylosidase, 1.0 nkat/ml of acetyl esterase, 89.7 nkat/ml of acetyl xylan esterase and 3.5 nkat/ml of alpha-arabinosidase activities
the expression of the enzyme can be induced by 1% (w/v) Avicel, 1% (w/v) D-xylose, or 1-3% (w/v) beechwood xylan
transcript levels in fruit are relatively high at the end of S1, i.e. fruit set, and at S3-E, i.e. beginning of the cell expansion. Transcripts reach a maximum when fruit firmness is 22-26 N, with a slight decline during the melting stage
optimized medium composition for production of xylanase/beta-xylosidase is 3.24% wheat straw (steam pretreated, particle size approx. 0.25 mm), 1.32% pharmamedia and 0.49% KH2PO4, leading to 5347.4 nkat/ml of xylanase, 3.0 nkat/ml of beta-xylosidase, 1.0 nkat/ml of acetyl esterase, 89.7 nkat/ml of acetyl xylan esterase and 3.5 nkat/ml of alpha-arabinosidase activities
-
optimized medium composition for production of xylanase/beta-xylosidase is 3.24% wheat straw (steam pretreated, particle size approx. 0.25 mm), 1.32% pharmamedia and 0.49% KH2PO4, leading to 5347.4 nkat/ml of xylanase, 3.0 nkat/ml of beta-xylosidase, 1.0 nkat/ml of acetyl esterase, 89.7 nkat/ml of acetyl xylan esterase and 3.5 nkat/ml of alpha-arabinosidase activities
-
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
analysis
-
comparison of glycolytic and chitinolytic enzyme activities between desert and oasis flies of Phlebotomus papatasi to evaluate potential differences in susceptibility to infection with Leishmania major
biofuel production
biotechnology
degradation
food industry
industry
nutrition
pharmacology
synthesis
additional information
agriculture
-
the pretreatment of rice straw with ammonia followed by beta-xylosidase hydrolysis by Weisella cibaria FB069 seems to be a promising method for xylooligosaccharide (prebiotic) production from rice straw
agriculture
Weissella cibaria FB069
-
the pretreatment of rice straw with ammonia followed by beta-xylosidase hydrolysis by Weisella cibaria FB069 seems to be a promising method for xylooligosaccharide (prebiotic) production from rice straw
-
biofuel production
-
the relatively broad pH profile is favourable for industrial application as it offers potential flexibility in terms of process pH and is in line with the current pH range of lignocellulose enzymatic hydrolysis processes for bioethanol production
biofuel production
-
the beta-xylosidase when combined with xylanase shows positive effect on xylan hydrolysis. The higher amount of glucose and xylose generated from sugarcane bagasse hydrolysis using the commercial cocktail Multifect CL supplemented with beta-xylosidase demonstrates that this enzyme has potential to be used as a supplement for commercial cocktails to improve the yield of xylose and glucose release, and this is of great importance for the production of second generation ethanol
biofuel production
-
the enzyme has great potential for applications in the bioconversion of lignocellulose to sugars, fuel ethanol and chemicals
biofuel production
application of this recombinant beta-xylosidase together with xylanase improves xylan hydrolysis efficiency, thus leading to increased biofuels productivity
biofuel production
a tailored enzymatic cocktail of alpha-glucuronidase (Agu115) from Schizophyllum commune with alpha-L-arabinofuranosidase (AbfA), xylanase (Xyn10C) and beta-xylosidase (XynB) achieves efficient hydrolysis of softwood xylans, which is instrumental for material- and cost-efficient processes for the generation of biofuels from lignocellulose-based streams. Cooperative enzymatic activities have important significance for enhancing the release of fermentable sugars and therefore generate an attractive sugar platform from lignocellulosic biomass to produce products such as bioethanol by fermentation, and for the production of hemicellulosic polymers and oligosaccharides with tailored molecular structures for material applications
biofuel production
-
the beta-xylosidase when combined with xylanase shows positive effect on xylan hydrolysis. The higher amount of glucose and xylose generated from sugarcane bagasse hydrolysis using the commercial cocktail Multifect CL supplemented with beta-xylosidase demonstrates that this enzyme has potential to be used as a supplement for commercial cocktails to improve the yield of xylose and glucose release, and this is of great importance for the production of second generation ethanol
-
biofuel production
-
the enzyme has great potential for applications in the bioconversion of lignocellulose to sugars, fuel ethanol and chemicals
-
biofuel production
Aspergillus niger DSM 22593
-
the relatively broad pH profile is favourable for industrial application as it offers potential flexibility in terms of process pH and is in line with the current pH range of lignocellulose enzymatic hydrolysis processes for bioethanol production
-
biofuel production
Ceratocystis fimbriata RM 35
-
the beta-xylosidase when combined with xylanase shows positive effect on xylan hydrolysis. The higher amount of glucose and xylose generated from sugarcane bagasse hydrolysis using the commercial cocktail Multifect CL supplemented with beta-xylosidase demonstrates that this enzyme has potential to be used as a supplement for commercial cocktails to improve the yield of xylose and glucose release, and this is of great importance for the production of second generation ethanol
-
biotechnology
coexpression of enzyme with Trichoderma reesei xylanase II in Saccharomyces cerevisiae allows for degradation of birchwood xylan to D-xylose
biotechnology
-
use of strain for bioconversion of xylan-rich plant wastes to value-added products
biotechnology
-
use of stable transgenic Medicago truncatula plants as an expression system for purification and characterization of proteins
biotechnology
the bifunctional beta-glucosidase/xylosidase can be used in simultaneous saccharification of cellulose ans xylan into fermenantable glucose and xylose
biotechnology
-
a method for bioconversion of 3-O-beta-D-xylopyranosyl-6-O-beta-D-glucopyranosyl-cycloastragenol into cycloastragenol is optimized. A green and efficient biotransformation method is established for 3-O-beta-D-xylopyranosyl-6-O-beta-D-glucopyranosyl-cycloastragenol using beta-glucosidase Dth3 and beta-xylosidase Xln-DT
biotechnology
-
the beta-xylosidase when combined with xylanase shows positive effect on xylan hydrolysis. The higher amount of glucose and xylose generated from sugarcane bagasse hydrolysis using the commercial cocktail Multifect CL supplemented with beta-xylosidase demonstrates that this enzyme has potential to be used as a supplement for commercial cocktails to improve the yield of xylose and glucose release, and this is of great importance for the production of second generation ethanol
biotechnology
-
use of strain for bioconversion of xylan-rich plant wastes to value-added products
-
biotechnology
-
the beta-xylosidase when combined with xylanase shows positive effect on xylan hydrolysis. The higher amount of glucose and xylose generated from sugarcane bagasse hydrolysis using the commercial cocktail Multifect CL supplemented with beta-xylosidase demonstrates that this enzyme has potential to be used as a supplement for commercial cocktails to improve the yield of xylose and glucose release, and this is of great importance for the production of second generation ethanol
-
biotechnology
-
a method for bioconversion of 3-O-beta-D-xylopyranosyl-6-O-beta-D-glucopyranosyl-cycloastragenol into cycloastragenol is optimized. A green and efficient biotransformation method is established for 3-O-beta-D-xylopyranosyl-6-O-beta-D-glucopyranosyl-cycloastragenol using beta-glucosidase Dth3 and beta-xylosidase Xln-DT
-
biotechnology
Ceratocystis fimbriata RM 35
-
the beta-xylosidase when combined with xylanase shows positive effect on xylan hydrolysis. The higher amount of glucose and xylose generated from sugarcane bagasse hydrolysis using the commercial cocktail Multifect CL supplemented with beta-xylosidase demonstrates that this enzyme has potential to be used as a supplement for commercial cocktails to improve the yield of xylose and glucose release, and this is of great importance for the production of second generation ethanol
-
degradation
hydrolysis of water-soluble and water-insoluble arabinoxylan and whole vinasse by an enzyme cocktail containing a 20%:20%:20%:40% mixture and a 25%:25%:25%:25% mixture, respectively, of the GH43 alpha-L-arabinofuranosidase from Humicola insolens, the GH51 alpha-L-arabinofuranosidase from M. giganteus, a GH10 endo-1,4-beta-xylanase from H. insolens, and a GH3 beta-xylosidase from Trichoderma reesei. The optimal dosages of the minimal enzyme cocktails are 0.4, 0.3, and 0.2 g enzyme protein per kilogram of substrate dry matter for the water-soluble wheat arabinoxylan, the water-insoluble wheat arabinoxylan, and the vinasse, respectively
degradation
-
hydrolysis of xylan by co-action of enzyme and xylanase from Anoxybacillus flavithermus BC gives 63.6% conversion after 4 h. Beechwood xylan is the best substrate, main product is xylose
degradation
-
in hydrolysis of corn stover hemicellulose, the xylose production increases by 94.9% and 140% when Trichoderma reesei hemicellulase is supplemented with purified beta-xylosidase and crude cell wall proteins of corn stover, respectively
degradation
-
co-immobilization of xylanase, beta-xylosidase and alpha-L-arabinofuranosidase from Penicillium janczewskii on a single support leads to a functional multi-enzymatic biocatalyst acting in the complete hydrolysis of different and complex substrates such as oat spelt and wheat arabinoxylans, with xylose yield higher than 40%. The xylanase and the alpha-L-arabinofuranosidase present high stability retaining 86.6 and 88.0% of activity after 10 reuse cycles
degradation
-
treatment of Eucalyptus kraft pulp with culture supernatant at 10 IU per gram pulp to enhance bleaching of kraft pulp results in a 10.5% reduction in Kappa number (indicating the amount of chemicals needed for bleaching pulps) and has a positive effect on the brightness of the resulting handsheets
degradation
enzyme increases reducing sugar release of birchwood xylan, beechwood xylan, and arabinoxylan by 6.4%, 13%, 15.8%, respectively, in synergistic action with endoxylanase. The late addition of the enzyme into reaction with endoxylanase results in a larger increase of reducing sugar release from pretreated barley straw that addition at the start or by treatment with endoxylanases alone. The increases observed are 6.3% and 13.8%, respectively
degradation
the enzyme has potential for promoting hemicellulose degradation and other industrial applications
degradation
the enzyme is useful for degradation of lignocellulosic biomass in bioethanol production, pulp bleaching process and beverage industry
degradation
enzyme Xln-DT shows excellent xylose/glucose/arabinose tolerance, and is applied as a candidate for degradation of hemicellulose
degradation
Saccharolobus solfataricus Oalpha
-
hydrolysis of xylan by co-action of enzyme and xylanase from Anoxybacillus flavithermus BC gives 63.6% conversion after 4 h. Beechwood xylan is the best substrate, main product is xylose
-
degradation
-
the enzyme is useful for degradation of lignocellulosic biomass in bioethanol production, pulp bleaching process and beverage industry
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degradation
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co-immobilization of xylanase, beta-xylosidase and alpha-L-arabinofuranosidase from Penicillium janczewskii on a single support leads to a functional multi-enzymatic biocatalyst acting in the complete hydrolysis of different and complex substrates such as oat spelt and wheat arabinoxylans, with xylose yield higher than 40%. The xylanase and the alpha-L-arabinofuranosidase present high stability retaining 86.6 and 88.0% of activity after 10 reuse cycles
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degradation
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enzyme Xln-DT shows excellent xylose/glucose/arabinose tolerance, and is applied as a candidate for degradation of hemicellulose
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food industry
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the pretreatment of rice straw with ammonia followed by beta-xylosidase hydrolysis by Weisella cibaria FB069 seems to be a promising method for xylooligosaccharide (prebiotic) production from rice straw
food industry
Weissella cibaria FB069
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the pretreatment of rice straw with ammonia followed by beta-xylosidase hydrolysis by Weisella cibaria FB069 seems to be a promising method for xylooligosaccharide (prebiotic) production from rice straw
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industry
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the relatively broad pH profile is favourable for industrial application as it offers potential flexibility in terms of process pH and is in line with the current pH range of lignocellulose enzymatic hydrolysis processes for bioethanol production
industry
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the recombinant xylanase Xyn (EC 3.2.1.8) and beta-xylosidase XynB exhibit synergistic hydrolysis of beechwood xylan and pretreated lignocellulose, where Xyn and XynB pre-hydrolysis achieve an improvement of pretreated lignocellulose hydrolysis by commercial cellulase. The observed stability of the enzymes at high temperature and the synergistic effect on lignocellulosic substrates suggested possible application of these enzymes in the field of saccharification process. The synergistic activity of xylanase and beta-xylosidase makes applications in biofuel production and other industrial fields possible
industry
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the recombinant xylanase Xyn (EC 3.2.1.8) and beta-xylosidase XynB exhibit synergistic hydrolysis of beechwood xylan and pretreated lignocellulose, where Xyn and XynB pre-hydrolysis achieve an improvement of pretreated lignocellulose hydrolysis by commercial cellulase. The observed stability of the enzymes at high temperature and the synergistic effect on lignocellulosic substrates suggested possible application of these enzymes in the field of saccharification process. The synergistic activity of xylanase and beta-xylosidase makes applications in biofuel production and other industrial fields possible
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industry
Aspergillus niger DSM 22593
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the relatively broad pH profile is favourable for industrial application as it offers potential flexibility in terms of process pH and is in line with the current pH range of lignocellulose enzymatic hydrolysis processes for bioethanol production
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nutrition
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enzyme efficiently releases monoterpenols from an aroma precursor extracted from muscat grape juice
nutrition
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the pretreatment of rice straw with ammonia followed by beta-xylosidase hydrolysis by Weisella cibaria FB069 seems to be a promising method for xylooligosaccharide (prebiotic) production from rice straw
nutrition
Weissella cibaria FB069
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the pretreatment of rice straw with ammonia followed by beta-xylosidase hydrolysis by Weisella cibaria FB069 seems to be a promising method for xylooligosaccharide (prebiotic) production from rice straw
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pharmacology
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cooperated transformation of ginsenoside extract to the pharmacologically active ginsenoside 20(S)-Rg3 with a beta-glucosidase. After transforming under optimal condition, the 20 g/l of ginsenoside extract is transformed into 6.28 g/l of Rg3 within 90 min, with a corresponding molar conversion of 95.0% and Rg3 productivity of 1793.49 mg/l/h, respectively
pharmacology
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cooperated transformation of ginsenoside extract to the pharmacologically active ginsenoside 20(S)-Rg3 with a beta-glucosidase. After transforming under optimal condition, the 20 g/l of ginsenoside extract is transformed into 6.28 g/l of Rg3 within 90 min, with a corresponding molar conversion of 95.0% and Rg3 productivity of 1793.49 mg/l/h, respectively
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synthesis
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synthesis of a group of uncommon xylosides via the transxylosylation activity
synthesis
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immobilization of enzyme on chitosan as best support material gives immobilization and activity yields of 94% and 87%, respectively, of initial activity, and also provides the highest stability, retaining 94% of its initial activity even after being recycled 25times. Maximal activity of immobilized enzyme is achieved at pH 8.0 and 53°C, whereas that for the free enzyme is obtained at pH 7.0 and 50°C. The immobilized enzyme is more thermostable than the free beta-xylosidase. Km values of the free enzyme increases from 2.37 mM to 3.42 mM at the immobilized state. Immobilized enzyme catalyzes the reverse hydrolysis reaction, forming xylooligosaccharides in the presence of a high concentration of xylose. Co-immobilized of beta-xylosidase and xylanase on chitosan leads to a continuous hydrolysis of 3% oat spelt xylan at 50°C and better hydrolysis yields and higher amount of xylose are obtained
synthesis
the enzyme immobilized by entrapment into alginate can be used for a continuous production of xylose from xylooligosaccharides at high temperature
synthesis
formation of xylooligosaccharides from alpha-D-xylopyranosyl fluoride in a conjugated reaction between beta-xylosidase E335G mutant enzyme and endo-1,4-beta-xylanase E265G mutant enzyme
synthesis
co-production of xylooligosaccharides and xylose from poplar sawdust by recombinant endo-1,4-beta-xylanase (MxynB-8) and beta-xylosidase mixture hydrolysis
synthesis
Dictyoglomus thermophilum beta-D-xylosidase DtXyl is attractive as a potential thermostable biocatalyst able to produce biologically active ginsenosides intermediates from beta-(1,2)-D-xylosylated compounds, including Notoginsenoside-R1
synthesis
extracellular GH3 beta-xylosidase Dt-Xyl3 with highly specific activity for 10-deacetyl-7-xylosltaxol biotransformation can be applicated as a biocatalyst in biopharmaceutics for synthesis of 10-deacetyl-taxol in paclitaxel production
synthesis
-
formation of xylooligosaccharides from alpha-D-xylopyranosyl fluoride in a conjugated reaction between beta-xylosidase E335G mutant enzyme and endo-1,4-beta-xylanase E265G mutant enzyme
-
synthesis
-
the enzyme immobilized by entrapment into alginate can be used for a continuous production of xylose from xylooligosaccharides at high temperature
-
synthesis
-
extracellular GH3 beta-xylosidase Dt-Xyl3 with highly specific activity for 10-deacetyl-7-xylosltaxol biotransformation can be applicated as a biocatalyst in biopharmaceutics for synthesis of 10-deacetyl-taxol in paclitaxel production
-
synthesis
-
Dictyoglomus thermophilum beta-D-xylosidase DtXyl is attractive as a potential thermostable biocatalyst able to produce biologically active ginsenosides intermediates from beta-(1,2)-D-xylosylated compounds, including Notoginsenoside-R1
-
synthesis
-
co-production of xylooligosaccharides and xylose from poplar sawdust by recombinant endo-1,4-beta-xylanase (MxynB-8) and beta-xylosidase mixture hydrolysis
-
synthesis
-
Dictyoglomus thermophilum beta-D-xylosidase DtXyl is attractive as a potential thermostable biocatalyst able to produce biologically active ginsenosides intermediates from beta-(1,2)-D-xylosylated compounds, including Notoginsenoside-R1
-
synthesis
-
Dictyoglomus thermophilum beta-D-xylosidase DtXyl is attractive as a potential thermostable biocatalyst able to produce biologically active ginsenosides intermediates from beta-(1,2)-D-xylosylated compounds, including Notoginsenoside-R1
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additional information
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the beta-xylosidase from Aureobasidium pullulans CBS 135684 is a prospective enzyme for a wide range of applications, especially for the bioconversion of hemicellulose
additional information
the enzyme can be a suitable additive for hemicellulases in long-term hydrolysis reactions. Because of its moderate inhibition by monomeric sugars but its high inhibition by ethanol, the enzyme can be particularly more useful in separate hydrolysis and fermentation than in simultaneous saccharification and co-fermentation or consolidated bioprocessing
additional information
Aureobasidium pullulans CBS 135684
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the beta-xylosidase from Aureobasidium pullulans CBS 135684 is a prospective enzyme for a wide range of applications, especially for the bioconversion of hemicellulose
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Release 2026.1 (March 2026)
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