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Information on EC 3.2.1.55 - non-reducing end alpha-L-arabinofuranosidase and Organism(s) Thermobacillus xylanilyticus and UniProt Accession O69262
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3.2.1.55 non-reducing end alpha-L-arabinofuranosidaseIUBMB Comments
The enzyme acts on alpha-L-arabinofuranosides, alpha-L-arabinans containing (1,3)- and/or (1,5)-linkages, arabinoxylans and arabinogalactans. Some beta-galactosidases (EC 3.2.1.23) and beta-D-fucosidases (EC 3.2.1.38) also hydrolyse alpha-L-arabinosides. cf. EC 3.2.1.185, non-reducing end beta-L-arabinofuranosidase.
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Word Map
- 3.2.1.55
- xylans
- arabinoxylans
- arabinose
- xylose
- arabinans
- arabinogalactans
-
hemicellulases
- endoxylanase
-
arabinosylated
- xylobiose
- spelt
- xylanases
- xylooligosaccharides
-
debranched
- biotechnology
- p-nitrophenyl-alpha-l-arabinofuranoside
- rhamnogalacturonans
- nutrition
-
pectic
-
xylanolytic
-
arabinose-containing
- l-arabitol
- food industry
- paper production
-
feruloylated
- p-nitrophenyl-beta-d-xylopyranoside
- kawachii
- arabinofuranose
- arabino-oligosaccharides
-
anti-complementary
-
oat-spelts
- degradation
-
xylan-degrading
-
beechwood
- agriculture
-
five-bladed
-
xylopyranosyls
-
exo-acting
-
hemicellulolytic
- arabinobiose
- cellulosa
- analysis
- industry
- synthesis
- biofuel production
- drug development
- medicine
The taxonomic range for the selected organisms is: Thermobacillus xylanilyticus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
arabinofuranosidase, arabinosidase, alpha-l-araf, alpha-arabinosidase, alpha-l-arabinosidase, afase, alpha-l-arabinofuranosidase b, arabinoxylan arabinofuranohydrolase, alpha-araf, alpha-arabinofuranosidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ABF
alpha-arabinofuranosidase
-
-
-
-
alpha-arabinosidase
-
-
-
-
Alpha-L-AF
-
-
-
-
alpha-L-arabinanase
-
-
-
-
alpha-L-arabinofuranosidase
alpha-L-arabinofuranoside hydrolase
-
-
-
-
alpha-L-arabinosidase
-
-
-
-
arabinosidase
-
-
-
-
L-arabinosidase
-
-
-
-
polysaccharide alpha-L-arabinofuranosidase
-
-
-
-
additional information
enzyme belongs to family 51 of the glycosyl hydrolase classification as part of the 4/7 glycosyl hydrolase superfamily
ABF
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides
reaction mechanism, active site structure, Glu28, the catalytic nucleophil, Glu176, the acid-base residue, and Glu298, responsible for modulation of the ionization state of the acid-base and for substrate fixation, are important for catalytic activity
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
SYSTEMATIC NAME
IUBMB Comments
alpha-L-arabinofuranoside non-reducing end alpha-L-arabinofuranosidase
The enzyme acts on alpha-L-arabinofuranosides, alpha-L-arabinans containing (1,3)- and/or (1,5)-linkages, arabinoxylans and arabinogalactans. Some beta-galactosidases (EC 3.2.1.23) and beta-D-fucosidases (EC 3.2.1.38) also hydrolyse alpha-L-arabinosides. cf. EC 3.2.1.185, non-reducing end beta-L-arabinofuranosidase.
CAS REGISTRY NUMBER
COMMENTARY
9067-74-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + L-arabinose
-
-
-
?
2 p-nitrophenyl-alpha-L-arabinofuranoside
p-nitrophenol + p-nitrophenyl-alpha-L-arabinofuranosyl-(1,2)-alpha-L-arabinofuranoside
-
-
-
-
?
2 p-nitrophenyl-beta-D-xylopyranoside
p-nitrophenol + p-nitrophenyl-beta-D-xylopyranosyl-(1,2)-beta-D-xylopyranoside
-
-
-
-
?
2 p-nitrophenyl-beta-D-xylopyranoside
p-nitrophenol + p-nitrophenyl-beta-D-xylopyranosyl-(1,3)-beta-D-xylopyranoside
-
-
-
-
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
-
-
-
-
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + L-arabinofuranose
-
the substrate binding process is driven by favourable entropy, which is linked to the movement of the beta2alpha2 loop. Loop closure relocates the solvent-exposed W99 into a buried location, allowing its involvement in substrate binding and in the formation of a functional active site. Residue H98 has a role in the dynamic formation as catalytically operational active site, which may be a specific feature of a subset of GH51 arabinofuranosidases
-
-
?
p-nitrophenyl alpha-L-arabinofuranoside + benzyl-alpha-D-xylopyranoside
?
-
-
-
-
?
p-nitrophenyl-alpha-L-arabinofuranoside + H2O
p-nitrophenol + L-arabinofuranose
-
-
-
-
?
p-nitrophenyl-alpha-L-arabinofuranoside + H2O
p-nitrophenol + L-arabinose
-
-
-
-
?
p-nitrophenyl-alpha-L-arabinopyranoside + H2O
p-nitrophenol + alpha-L-arabinopyranose
-
-
-
-
?
p-nitrophenyl-beta-D-galactofuranoside
beta-D-galactofuranosyl-(1,2)-beta-D-galactofuranoside + p-nitrophenol
-
-
-
-
?
p-nitrophenyl-beta-D-xylofuranoside + H2O
p-nitrophenol + beta-D-xylofuranose
-
-
-
-
?
phenyl alpha-L-arabinofuranoside + H2O
L-arabinose + phenol
-
-
-
-
ir
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
-
-
-
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
hydrolysis of the substrate with retention of the anomeric configuration
-
-
?
additional information
?
-
-
does not hydrolyze p-nitrophenyl-alpha-L-arabinopyranoside or gum arabic
-
-
?
additional information
?
-
-
AbfD3-catalyzed transglycosylation reactions
-
-
?
additional information
?
-
-
alpha-L-arabinofuranosidases are exo-acting glycoside hydrolases that catalyse the hydrolysis of terminal non-reducing alpha-L-arabinofuranosyl moieties in oligosaccharides and polysaccharides through the cleavage of 1->2 and/or 1->3 glycosidic bonds
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
alpha-L-arabinofuranosidases are exo-acting glycoside hydrolases that catalyse the hydrolysis of terminal non-reducing alpha-L-arabinofuranosyl moieties in oligosaccharides and polysaccharides through the cleavage of 1->2 and/or 1->3 glycosidic bonds
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Sodium azide
activates mutant enzymes: E28A 6fold, E176A 7fold, and E298A 67fold, at up to 0.5 M, no activation of the wild-type enzyme
Sodium formate
activates mutant enzymes: E28A 60fold at 4 M, E176A 4fold at 4 M, and E298A 36fold at 0.5-1.0 M, no activation of the wild-type enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.09
4-nitrophenyl alpha-L-arabinofuranoside
mutant R69H, pH 7.0, 45°C
0.25
4-nitrophenyl alpha-L-arabinofuranoside
wild-type, pH 7.0, 45°C
0.48
4-nitrophenyl alpha-L-arabinofuranoside
mutant R69H/N216W/L352M, pH 7.0, 45°C
0.69
4-nitrophenyl alpha-L-arabinofuranoside
mutant R69H/G179F/L352M, pH 7.0, 45°C
1.23
4-nitrophenyl alpha-L-arabinofuranoside
mutant R69H/L352M, pH 7.0, 45°C
8.98
4-nitrophenyl alpha-L-arabinofuranoside
mutant L352M, pH 7.0, 45°C
0.3
4-nitrophenyl-alpha-L-arabinofuranoside
pH 5.8, 60°C, mutant E176D
0.41
4-nitrophenyl-alpha-L-arabinofuranoside
pH 5.8, 60°C, mutant E176Q
0.43
4-nitrophenyl-alpha-L-arabinofuranoside
pH 5.8, 60°C, mutant E176A
0.51
4-nitrophenyl-alpha-L-arabinofuranoside
pH 5.8, 60°C, mutant E28D
0.7
4-nitrophenyl-alpha-L-arabinofuranoside
pH 5.8, 60°C, wild-type enzyme
0.91
4-nitrophenyl-alpha-L-arabinofuranoside
pH 5.8, 60°C, mutant E298Q
1.04
4-nitrophenyl-alpha-L-arabinofuranoside
pH 5.8, 60°C, mutant E28A
1.11
4-nitrophenyl-alpha-L-arabinofuranoside
pH 5.8, 60°C, mutant E298D
34
4-nitrophenyl-alpha-L-arabinofuranoside
pH 5.8, 60°C, mutant E28Q
3.2
p-nitrophenyl-alpha-L-arabinofuranose
Tx-Abf-C180A mutant
10
p-nitrophenyl-alpha-L-arabinofuranose
Tx-Abf-M94_I103delinsGG mutant
45
p-nitrophenyl-alpha-L-arabinofuranose
Tx-Abf-W99A mutant
0.72
4-nitrophenyl-alpha-L-arabinofuranoside
-
wild-type enzyme, pH 5.8, 60°C
0.87
4-nitrophenyl-alpha-L-arabinofuranoside
-
mutant H98F, pH 5.8, 60°C
1.5 - 2
4-nitrophenyl-alpha-L-arabinofuranoside
-
mutant H98A, pH 5.8, 60°C
3.4
4-nitrophenyl-alpha-L-arabinofuranoside
-
mutant H98F/W99F, pH 5.8, 60°C
4.2
4-nitrophenyl-alpha-L-arabinofuranoside
-
mutant W99F, pH 5.8, 60°C
9.1
4-nitrophenyl-alpha-L-arabinofuranoside
-
mutant W99A, pH 5.8, 60°C
15
4-nitrophenyl-alpha-L-arabinofuranoside
-
mutant H98A/W99A, pH 5.8, 60°C
additional information
additional information
kinetics, wild-type and mutant enzymes, influence of sodium formate and sodium azide, overview
-
additional information
additional information
-
kinetics, wild-type and mutant enzymes, influence of sodium formate and sodium azide, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.54
4-nitrophenyl alpha-L-arabinofuranoside
mutant R69H/G179F/L352M, pH 7.0, 45°C
0.58
4-nitrophenyl alpha-L-arabinofuranoside
mutant R69H/N216W/L352M, pH 7.0, 45°C
0.97
4-nitrophenyl alpha-L-arabinofuranoside
mutant R69H/L352M, pH 7.0, 45°C
2.29
4-nitrophenyl alpha-L-arabinofuranoside
mutant R69H, pH 7.0, 45°C
139
4-nitrophenyl alpha-L-arabinofuranoside
wild-type, pH 7.0, 45°C
233
4-nitrophenyl alpha-L-arabinofuranoside
mutant L352M, pH 7.0, 45°C
0.39
4-nitrophenyl-alpha-L-arabinofuranoside
pH 5.8, 60°C, mutant E176A
0.53
4-nitrophenyl-alpha-L-arabinofuranoside
pH 5.8, 60°C, mutant E298D
0.63
4-nitrophenyl-alpha-L-arabinofuranoside
pH 5.8, 60°C, mutant E28A
0.65
4-nitrophenyl-alpha-L-arabinofuranoside
pH 5.8, 60°C, mutant E176D
1.04
4-nitrophenyl-alpha-L-arabinofuranoside
pH 5.8, 60°C, mutant E298Q
1.08
4-nitrophenyl-alpha-L-arabinofuranoside
pH 5.8, 60°C, mutant E28D
5.95
4-nitrophenyl-alpha-L-arabinofuranoside
pH 5.8, 60°C, mutant E28Q
36.7
4-nitrophenyl-alpha-L-arabinofuranoside
pH 5.8, 60°C, mutant E176Q
4100
4-nitrophenyl-alpha-L-arabinofuranoside
pH 5.8, 60°C, wild-type enzyme
24
p-nitrophenyl-alpha-L-arabinofuranose
Tx-Abf-C180A mutant, 60°C
35
p-nitrophenyl-alpha-L-arabinofuranose
Tx-Abf-M94_I103delinsGG mutant, 60°C
165
p-nitrophenyl-alpha-L-arabinofuranose
Tx-Abf-W99A mutant, 60°C
77
4-nitrophenyl-alpha-L-arabinofuranoside
-
mutant W99F, pH 5.8, 60°C
97
4-nitrophenyl-alpha-L-arabinofuranoside
-
mutant H98F/W99F, pH 5.8, 60°C
137
4-nitrophenyl-alpha-L-arabinofuranoside
-
mutant W99A, pH 5.8, 60°C
154
4-nitrophenyl-alpha-L-arabinofuranoside
-
mutant H98A/W99A, pH 5.8, 60°C
192
4-nitrophenyl-alpha-L-arabinofuranoside
-
mutant H98A, pH 5.8, 60°C
199
4-nitrophenyl-alpha-L-arabinofuranoside
-
mutant H98F, pH 5.8, 60°C
575
4-nitrophenyl-alpha-L-arabinofuranoside
-
wild-type enzyme, pH 5.8, 60°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.8
4-nitrophenyl alpha-L-arabinofuranoside
mutant R69H/G179F/L352M, pH 7.0, 45°C
0.8
4-nitrophenyl alpha-L-arabinofuranoside
mutant R69H/L352M, pH 7.0, 45°C
1.2
4-nitrophenyl alpha-L-arabinofuranoside
mutant R69H/N216W/L352M, pH 7.0, 45°C
25.4
4-nitrophenyl alpha-L-arabinofuranoside
mutant R69H, pH 7.0, 45°C
25.9
4-nitrophenyl alpha-L-arabinofuranoside
mutant L352M, pH 7.0, 45°C
556
4-nitrophenyl alpha-L-arabinofuranoside
wild-type, pH 7.0, 45°C
9.8
4-nitrophenyl-alpha-L-arabinofuranoside
-
mutant H98A/W99A, pH 5.8, 60°C
15.1
4-nitrophenyl-alpha-L-arabinofuranoside
-
mutant W99A, pH 5.8, 60°C
18
4-nitrophenyl-alpha-L-arabinofuranoside
-
mutant W99F, pH 5.8, 60°C
28.2
4-nitrophenyl-alpha-L-arabinofuranoside
-
mutant H98F/W99F, pH 5.8, 60°C
126
4-nitrophenyl-alpha-L-arabinofuranoside
-
mutant H98A, pH 5.8, 60°C
228
4-nitrophenyl-alpha-L-arabinofuranoside
-
mutant H98F, pH 5.8, 60°C
795
4-nitrophenyl-alpha-L-arabinofuranoside
-
wild-type enzyme, pH 5.8, 60°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10.5
Tx-Abf-W99A mutant, 60°C, p-nitrophenyl-alpha-L-arabinofuranose
27
Tx-Abf-C180A mutant, 60°C, p-nitrophenyl-alpha-L-arabinofuranose
0.292
465
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.8
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
the enzyme belongs to the family 51 glycoside hydrolase, GH51
additional information
-
functional role of the mobile beta2alpha2 loop, especially of loop residues H98 and W99, analysis by site-directed mutagenesis, isothermal titration calorimetry, saturation transfer difference NMR spectroscopy, and molecular dynamics simulation, three-dimensional structure of the enzyme and its active site, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
56070
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
three-dimensional structure of the enzyme, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor-diffusion method, inactive mutant in complex with a pentasaccharide, X-ray diffraction structure determination and analysis at 2.0 A resolution, space group P 65 2 2, seleno-methionyl derivative of wild-type arabinofuranosidase, X-ray diffraction structure determination and analysis at 2.2 A resolution, space group P 65 2 2, sequence identities and homologies, phylogentic analyses
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D55A
site-directed mutagenesis, activity is similar to wild-type enzyme activity
E112A
site-directed mutagenesis, activity is similar to wild-type enzyme activity
E143A
site-directed mutagenesis, activity is similar to wild-type enzyme activity
E176A
site-directed mutagenesis, exchange of the acid-base residue, nearly inactive mutant, 8925fold reduced activity compared to the wild-type enzyme
E176D
site-directed mutagenesis, exchange of the acid-base residue, mutant enzyme shows altered kinetic properties compared to the wild-type enzyme
E176Q
E28A
site-directed mutagenesis, nearly inactive mutant, 5950fold reduced activity compared to the wild-type enzyme
E28A/E176A
site-directed mutagenesis, completely inactive mutant
E28D
site-directed mutagenesis, mutant enzyme shows altered kinetic properties compared to the wild-type enzyme
E28Q
E298A
site-directed mutagenesis, nearly inactive mutant, 178500fold reduced activity compared to the wild-type enzyme
E298D
site-directed mutagenesis, mutant enzyme shows altered kinetic properties compared to the wild-type enzyme
E298Q
site-directed mutagenesis, mutant enzyme shows increased sensitivity to pH and a lower pH optimum compared to the wild-type enzyme
G179F
mutant displays stronger xylotriose-mediated inhibition than wild-type
L352M
37fold increase of the KM value, mutant displays increased transglycosylation activity (about 18%)
M94_I103delinsGG
site-directed mutagenesis, 70fold less active than the wild-type enzyme
R69H
mutant displays severely reduced specific activity and biphasic reaction profile. Transglycosylation activitiy is increased
R69H/G179F/L352M
mutant displays severely reduced specific activity and biphasic reaction profile and is activated in the presence of xylotriose. Transglycosylation activitiy is increased
R69H/L352M
activity increases up to 260% in the presence of xylotriose, whereas wild-type is inhibited
R69H/N216W/L352M
mutant displays severely reduced specific activity and biphasic reaction profile and is activated in the presence of xylotriose. Transglycosylation activitiy is increased
W99A
site-directed mutagenesis, the arabinosyl moiety is not correctly bound in the active site when Trp99 is replaced by Ala
H98A
-
site-directed mutagenesis, the mutant shows affected kinetics and reduced activity compared to the wild-type enzyme
H98A/W99A
-
site-directed mutagenesis, the mutant shows affected kinetics and reduced activity compared to the wild-type enzyme
H98F
-
site-directed mutagenesis, the mutant shows affected kinetics and reduced activity compared to the wild-type enzyme
H98F/W99F
-
site-directed mutagenesis, the mutant shows affected kinetics and reduced activity compared to the wild-type enzyme
W99A
-
site-directed mutagenesis, the mutation causes the loss of a hydrogen bond and leads to an alternative binding mode that is detrimental for catalysis, altered binding of the aglycon motif in the active site, the mutant shows affected kinetics and reduced activity compared to the wild-type enzyme
W99F
-
site-directed mutagenesis, the mutant shows affected kinetics, reduced activity, and altered binding of the aglycon motif in the active site compared to the wild-type enzyme
E176Q
site-directed mutagenesis, exchange of the acid-base residue, mutant enzyme is insensitive to pH
E28Q
site-directed mutagenesis, mutant enzyme shows altered kinetic properties compared to the wild-type enzyme
E28Q
site-directed mutagenesis, mutant enzyme shows increased sensitivity to pH and a lower pH optimum compared to the wild-type enzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes from Escherichia coli
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant enzymes in Escherichia coli BL21(DE3)
gene AbfD3 isolated, inserted into pET24 vector and expressed in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
degradation of lignocellulose, hemicellulose and pectin
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Debeche, T.; Cummings, N.; Connerton, I.; Debeire, P.; O'Donohue, M.J.
Genetic and biochemical characterization of a highly thermostable alpha-L-arabinofuranosidase from Thermobacillus xylanilyticus
Appl. Environ. Microbiol.
66
1734-1736
2000
Aspergillus awamori, Aspergillus awamori IFO 4033, Aspergillus niger, Aspergillus terreus, Aureobasidium pullulans, Bacillus subtilis, Bacillus subtilis 03. Jun, Bifidobacterium adolescentis, Breznakibacter xylanolyticus, Geobacillus stearothermophilus, Raphanus sativus, Streptomyces lividans, Streptomyces lividans 66 1326, Streptomyces purpurascens, Thermobacillus xylanilyticus, Thermobacillus xylanilyticus D3, Thermoclostridium stercorarium
Debeche, T.; Bliard, C.; Debeire, P.; O'Donohue, M.J.
Probing the catalytically essential residues of the alpha-L-arabinofuranosidase from Thermobacillus xylanilyticus
Protein Eng.
15
21-28
2002
Thermobacillus xylanilyticus (O69262), Thermobacillus xylanilyticus
Remond, C.; Plantier-Royon, R.; Aubry, N.; Maes, E.; Bliard, C.; ODonohue, M.J.
Synthesis of pentose-containing disaccharides using a thermostable alpha-L-arabinofuranosidase
Carbohydr. Res.
339
2019-2025
2004
Thermobacillus xylanilyticus
Remond, C.; Plantier-Royon, R.; Aubry, N.; ODonohue, M.J.
An original chemoenzymatic route for the synthesis of beta-D-galactofuranosides using an alpha-L-arabinofuranosidase
Carbohydr. Res.
340
637-644
2005
Thermobacillus xylanilyticus
Numan, M.T.; Bhosle, N.B.
alpha-L-Arabinofuranosidases: the potential applications in biotechnology
J. Ind. Microbiol. Biotechnol.
33
247-260
2006
Aspergillus luchuensis, Aspergillus oryzae, Aspergillus oryzae HL15, Bacillus pumilus, Bacillus pumilus PS213, Bifidobacterium longum, Bifidobacterium longum B667, Brevibacillus brevis, Brevibacillus brevis K-110, Cellvibrio japonicus, Clostridium cellulovorans, Fusarium oxysporum f. sp. dianthi, Penicillium chrysogenum, Rhizomucor pusillus, Rhizomucor pusillus HHT1, Streptomyces chartreusis, Streptomyces chartreusis GS901, Streptomyces thermoviolaceus, Streptomyces thermoviolaceus OP-520, Talaromyces purpureogenus, Thermoanaerobacter ethanolicus, Thermoanaerobacter ethanolicus JW 200, Thermobacillus xylanilyticus, Thermobacillus xylanilyticus D3, Thermobifida fusca, Thermomicrobia bacterium PRI-1686, Thermotoga maritima, Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
Lopez, G.; Daniellou, R.; ODonohue, M.; Ferrieres, V.; Nugier-Chauvin, C.
Thioimidoyl furanosides as first inhibitors of the alpha-L-arabinofuranosidase AbfD3
Bioorg. Med. Chem. Lett.
17
434-438
2007
Thermobacillus xylanilyticus
Lopez, G.; Nugier-Chauvin, C.; Remond, C.; ODonohue, M.
Investigation of the specificity of an alpha-L-arabinofuranosidase using C-2 and C-5 modified alpha-L-arabinofuranosides
Carbohydr. Res.
342
2202-2211
2007
Thermobacillus xylanilyticus
Paes, G.; Skov, L.K.; ODonohue, M.J.; Remond, C.; Kastrup, J.S.; Gajhede, M.; Mirza, O.
The structure of the complex between a branched pentasaccharide and Thermobacillus xylanilyticus GH-51 arabinofuranosidase reveals xylan-binding determinants and induced fit
Biochemistry
47
7441-7451
2008
Thermobacillus xylanilyticus (O69262), Thermobacillus xylanilyticus
Arab-Jaziri, F.; Bissaro, B.; Barbe, S.; Saurel, O.; Debat, H.; Dumon, C.; Gervais, V.; Milon, A.; Andre, I.; Faure, R.; O'Donohue, M.J.
Functional roles of H98 and W99 and beta2alpha2 loop dynamics in the alpha-L-arabinofuranosidase from Thermobacillus xylanilyticus
FEBS J.
279
3598-3611
2012
Thermobacillus xylanilyticus
Bissaro, B.; Durand, J.; Biarnes, X.; Planas, A.; Monsan, P.; ODonohue, M.; Faure, R.
Molecular design of non-Leloir furanose-transferring enzymes from an alpha-L-arabinofuranosidase: a rationale for the engineering of evolved transglycosylases
ACS Catal.
5
4598-4611
2015
Thermobacillus xylanilyticus (O69262)
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