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Information on EC 3.2.1.55 - non-reducing end alpha-L-arabinofuranosidase and Organism(s) Bacillus subtilis and UniProt Accession Q45071
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EC Tree
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.
Specify your search results
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: Bacillus subtilis
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
-
-
-
-
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
p-nitrophenyl-alpha-L-arabinofuranoside + H2O
p-nitrophenol + L-arabinofuranose
-
-
-
?
O-alpha-L-arabinofuranosyl-(1-3-)-O-beta-D-xylopyranosyl-(1-4)-D-xylopyranose + H2O
L-arabinose + O-beta-D-xylopyranosyl-(1-4)-D-xylopyranose
-
-
-
-
?
O-beta-D-xylopyranosyl-(1-4)-[O-alpha-L-arabinofuranosyl-(1-3)]-O-beta-D-xylopyranosyl-(1-4)-D-xylopyranose + H2O
L-arabinose + O-beta-D-xylopyranosyl-(1-4)-O-beta-D-xylopyranosyl-(1-4)-D-xylopyranose
-
-
-
-
?
p-nitrophenyl-alpha-L-arabinofuranoside + H2O
p-nitrophenol + L-arabinofuranose
-
-
-
?
phenyl alpha-L-arabinofuranoside + H2O
L-arabinose + phenol
-
-
171764, 288809, 288813, 288815, 288816, 288822, 288823, 288828, 288829, 288831, 288835, 288837, 288840, 288842, 288845, 288846, 288850
-
-
ir
beet arabinan + H2O
L-arabinose + ?
-
-
-
-
ir
L-arabinan + H2O
(1,5-alpha-L-arabinose)25 + ?
-
-
-
-
?
p-nitrophenyl-alpha-L-arabinofuranoside + H2O
p-nitrophenol + L-arabinose
-
-
288812, 288813, 288816, 288822, 288823, 288828, 288829, 288835, 288840, 288842, 288845, 288846, 288850
-
-
?
p-nitrophenyl-alpha-L-arabinofuranoside + H2O
p-nitrophenol + L-arabinose
-
arabinofuranosidase I
-
-
?
additional information
?
-
XynD specifically releases arabinofuranosyl groups from mono-substituted C-(O)-2 and C-(O)-3 xylopyranosyl residues on the xylan backbone. XynD does not display endoxylanase, xylosidase or arabinanase activity and is inactive on arabinan
-
-
?
additional information
?
-
-
XynD specifically releases arabinofuranosyl groups from mono-substituted C-(O)-2 and C-(O)-3 xylopyranosyl residues on the xylan backbone. XynD does not display endoxylanase, xylosidase or arabinanase activity and is inactive on arabinan
-
-
?
additional information
?
-
BsAXH-m2,3 cleaves arabinose units from O-2- or O-3-mono-substituted xylose residues
-
-
?
additional information
?
-
-
BsAXH-m2,3 cleaves arabinose units from O-2- or O-3-mono-substituted xylose residues
-
-
?
additional information
?
-
-
arabinofuranosidase I does not hydrolyze L-arabinan, arabinofuranosidase II has no activity on polygalacturonic acid, carboxymethylcellulose, larch galactan, citrus pectic galactan or the synthetic substrates p-nitrophenyl derivatives of alpha- and beta-D-xylopyranosides, alpha- and beta-D-glucopyranosides, beta-D-fucopyranoside and beta-D-galactopyranoside
-
-
?
additional information
?
-
-
O-beta-D-xylopyranosyl-(1-2)-O-alpha-L-arabinofuranosyl-(1-3)-O-beta-D-xylopyranosyl-(1-4)-O-beta-D-xylopyranosyl-(1-4)-D-xylopyranose, arabinoxylan, gum arabic and arabinogalactan are no substrates
-
-
?
additional information
?
-
Abf2 is most active on (1-2) and (1-3) linkages of branched arabinan and arabinoxylan
-
-
?
additional information
?
-
Abf2 is most active on (1-2) and (1-3) linkages of branched arabinan and arabinoxylan
-
-
?
additional information
?
-
-
Abf2 is most active on (1-2) and (1-3) linkages of branched arabinan and arabinoxylan
-
-
?
additional information
?
-
AbfA acts preferentially on (1-5) linkages of linear alpha-1,5-L-arabinan and alpha-1,5-linked arabino-oligomers, and is much less effective on branched sugar beet arabinan and arabinoxylan and arabinogalactan
-
-
?
additional information
?
-
AbfA acts preferentially on (1-5) linkages of linear alpha-1,5-L-arabinan and alpha-1,5-linked arabino-oligomers, and is much less effective on branched sugar beet arabinan and arabinoxylan and arabinogalactan
-
-
?
additional information
?
-
-
AbfA acts preferentially on (1-5) linkages of linear alpha-1,5-L-arabinan and alpha-1,5-linked arabino-oligomers, and is much less effective on branched sugar beet arabinan and arabinoxylan and arabinogalactan
-
-
?
additional information
?
-
the enzyme preferentially cleaves debranched or linear arabinan and is an exo-acting enzyme producing arabinose from arabinoheptaose
-
-
?
additional information
?
-
-
the enzyme preferentially cleaves debranched or linear arabinan and is an exo-acting enzyme producing arabinose from arabinoheptaose
-
-
?
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the addition of the chelating agent EDTA does not affect the activity of AbfA, suggesting that no metals are needed for the enzymic reaction
additional information
the addition of the chelating agent EDTA does not affect the activity of AbfA, suggesting that no metals are needed for the enzymic reaction
additional information
-
the addition of the chelating agent EDTA does not affect the activity of AbfA, suggesting that no metals are needed for the enzymic reaction
additional information
the addition of the chelating agent EDTA does not affect the activity of either Abf2, suggesting that no metals are needed for the enzymic reaction
additional information
the addition of the chelating agent EDTA does not affect the activity of either Abf2, suggesting that no metals are needed for the enzymic reaction
additional information
-
the addition of the chelating agent EDTA does not affect the activity of either Abf2, suggesting that no metals are needed for the enzymic reaction
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 6
pH 5.0: about 20% of maximal activity, pH 6.0: about 80% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 50
30°C: about 60% of maximal activity, 50°C: about 60% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
isoelectric focusing revealed a pI to be at least 9.3
additional information
-
isoelectric focusing revealed a pI to be at least 9.3
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 glycoside hydrolase 51 family, GH51. Important contribution of the quaternary arrangement in the stabilization of the beta-sandwich accessory domain and other regions involved in the formation of the catalytic interface of hexameric Abfases belonging to GH51 family
additional information
additional information
structure-function analysis, molecular modeling and molecular dynamic simulations, overview
additional information
-
structure-function analysis, molecular modeling and molecular dynamic simulations, overview
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
112000
Abf2 is present in two oligomeric states, a predominant form with an estimated molecular mass of 112 kDa that could correspond to the dimer and an additional oligomeric form of about 276 kDa
116000
gradient native PAGE, two oligomeric forms are observed, the dimer (116 kDa) and an oligomer with a higher-order structure than the tetramer
276000
Abf2 is present in two oligomeric states, a predominant form with an estimated molecular mass of 112 kDa that could correspond to the dimer and an additional oligomeric form of about 276 kDa
296000
gradient native PAGE, two oligomeric forms are observed, the dimer (116 kDa) and an oligomer with a higher-order structure than the tetramer
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
oligomer
additional information
oligomer
two oligomeric forms are observed, the dimer (116 kDa) and an oligomer with a higher-order structure than the tetramer, subunit mass 58000
additional information
the enzyme has a canonical circular dichroism spectrum of alpha/beta proteins and exhibits a hexameric quaternary structure in solution, mechanisms associated with the unfolding process by molecular dynamics simulations, important contribution of the quaternary arrangement in the stabilization of the beta-sandwich accessory domain and other regions involved in the formation of the catalytic interface of hexameric Abfases belonging to GH51 family
additional information
-
the enzyme has a canonical circular dichroism spectrum of alpha/beta proteins and exhibits a hexameric quaternary structure in solution, mechanisms associated with the unfolding process by molecular dynamics simulations, important contribution of the quaternary arrangement in the stabilization of the beta-sandwich accessory domain and other regions involved in the formation of the catalytic interface of hexameric Abfases belonging to GH51 family
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
AXH, 4.0 M Na formate, 30% sucrose, pH 5.0, X-ray diffraction structure determination and analysis at 2.0 A resolution, AXH xylotriose, 4.0 M Na formate, 1.0 M lithium chloride, pH 5.0, X-ray diffraction structure determination and analysis at 1.55 A resolution, AXH xylotetraose, X-ray diffraction structure determination and analysis at 2.05 A resolution, AXH AXOS-4-0.5, X-ray diffraction structure determination and analysis at 1.8 A resolution, AXH cellotetraose, X-ray diffraction structure determination and analysis at 1.8 A resolution, vapor diffusion, hanging drop, temperature 277K, space group P 21 21 21
hanging-drop vapour-diffusion method. Purified recombinant AXH crystallizes in the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 68.7, b = 73.7, c = 106.5 A. X-ray diffraction data are collected to a resolution of 1.55 A
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
xynD is isolated from genomic DNA of Bacillus subtilis subsp. subtilis ATCC 6051 and cloned for cytoplasmatic expression in Escherichia coli
gene BSU28720, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli strain BL21(DE3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nutrition
paper production
paper production
-
enzyme becomes very important in the effective use of hemicellulose
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Van der Veen, P.; Flipphi, M.J.A.; Voragen, A.G.J.; Visser, J.
Induction, purification and characterisation of arabinases produced by Aspergillus niger
Arch. Microbiol.
157
23-28
1991
Aspergillus niger, Bacillus subtilis, Streptomyces purpurascens, Aspergillus niger N400(CBS 120-49)
Uesaka, E.; Sato, M.; Raiju, M.; Kaji, A.
alpha-L-Arabinofuranosidase from Rhodotorula flava
J. Bacteriol.
133
1073-1077
1978
Aspergillus niger, Bacillus subtilis, Botrytis allii, Botrytis cinerea, Clostridium felsineum, Coniella diplodiella, Fusarium oxysporum, Gloeosporium kaki, Rhodotorula flava, Sclerotinia libertiana, Sclerotinia sclerotiorum
Komae, K.; Kaji, A.; Sato, M.
An alpha-L-arabinofuranosidase from Streptomyces purpurascens IFO 3389
Agric. Biol. Chem.
46
1899-1905
1982
Streptomyces lavendulae, Aspergillus niger, Bacillus subtilis, Botrytis cinerea, Botrytis fabae, Clostridium felsineum, Athelia rolfsii, Pectobacterium carotovorum, Albifimbria verrucaria, Rhodotorula flava, Sclerotinia fructigena, Sclerotinia libertiana, Streptomyces olivochromogenes, Kitasatospora aureofaciens, Streptomyces flaveolus, Streptomyces massasporeus, Streptomyces purpurascens, Streptomyces lavendulae KA140, Streptomyces olivochromogenes IFO3178, Kitasatospora aureofaciens KA 204, Streptomyces flaveolus KA1143
-
Greve, L.C.; Labavitch, J.M.; Hungate, R.E.
alpha-L-Arabinofuranosidase from Ruminococcus albus 8: purification and possible role in hydrolysis of alfalfa cell wall
Appl. Environ. Microbiol.
47
1135-1140
1984
Aspergillus niger, Bacillus subtilis, Ruminococcus albus, Ruminococcus albus 8, Sclerotinia fructigena, Scopolia japonica, Streptomyces sp., Streptomyces sp. 17-1, Streptomyces sp. 65
Whitaker, J.R.
Pectic substances, pectic enzymes and haze formation in fruit juices
Enzyme Microb. Technol.
6
341-349
1984
Aspergillus niger, Bacillus subtilis, Athelia rolfsii, Bacillus subtilis F-11, Aspergillus niger 5195
-
Lee, S.F.; Forsberg, C.W.
Purification and characterization of an alpha-L-arabinofuranosidase from Clostridium acetobutylicum ATCC 824
Can. J. Microbiol.
33
1011-1016
1987
Aspergillus niger, Bacillus subtilis, Streptomyces sp., Clostridium acetobutylicum, Ruminococcus albus, Streptomyces purpurascens, Streptomyces sp. 17-1
-
Hespell, R.B.; O'Bryan, P.
Purification and characterization of an alpha-L-arabinofuranosidase from Butyrivibrio fibrisolvens GS113
Appl. Environ. Microbiol.
58
1082-1088
1992
Aspergillus niger, Bacillus sp. (in: Bacteria), Bacillus subtilis, Bacteroides ovatus, Butyrivibrio fibrisolvens, Butyrivibrio fibrisolvens GS113, Clostridium acetobutylicum, Fibrobacter succinogenes, Monilinia fructigena, Prevotella ruminicola, Pseudomonas sp., Ruminococcus albus, Ruminococcus flavefaciens, Streptomyces purpurascens, Streptomyces sp.
Tajana, E.; Fiechter, A.; Zimmermann, W.
Purification and characterization of two alpha-L-arabinofuranosidases from Streptomyces diastaticus
Appl. Environ. Microbiol.
58
1447-1450
1992
Aspergillus niger, Bacillus sp. (in: Bacteria), Bacillus subtilis, Bacillus subtilis F-11, Ruminococcus albus, Ruminococcus albus 8, Scopolia japonica, Streptomyces diastaticus, Streptomyces diastaticus ET/BW200, Streptomyces diastatochromogenes, Streptomyces purpurascens, Streptomyces sp., Streptomyces sp. 17-1, Trichoderma reesei
Manin, C.; Shareek, F.; Morosoli, R.; Klueppel, D.
Purification and characterization of an alpha-L-arabinofuranosidase from Streptomyces lividans 66 and DNA sequence of the gene (abfA)
Biochem. J.
302
443-449
1994
Aspergillus niger, Bacillus subtilis, Butyrivibrio fibrisolvens, Streptomyces sp., Clostridium acetobutylicum, Thermoclostridium stercorarium, Athelia rolfsii, Dichomitus squalens, Pseudomonas fluorescens, Streptomyces lividans, Streptomyces purpurascens, Trichoderma reesei, Streptomyces sp. 17-1, Streptomyces lividans 66 1326
-
Schyns, P.J.Y.M.J.; de Frankrijker, J.; Zehnder, A.J.B.; Stams, A.J.M.
Production, purification and characterization of an alpha-L-arabinofuranosidase from Bacteroides xylanolyticus X5-1
Appl. Microbiol. Biotechnol.
42
548-554
1994
Aspergillus niger, Bacillus subtilis, Butyrivibrio fibrisolvens, Butyrivibrio fibrisolvens GS113, Butyrivibrio fibrisolvens NCFB 2249, Clostridium acetobutylicum, Hungatella xylanolytica, Ruminococcus albus, Ruminococcus albus 8, Streptomyces purpurascens, Streptomyces sp., Streptomyces sp. 17-1
-
Kaneko, S.; Sano, M.; Kusakabe, I.
Purification and some properties of alpha-L-arabinofuranosidase from Bacillus subtilis 3-6
Appl. Environ. Microbiol.
60
3425-3428
1994
Aspergillus aculeatus, Aspergillus niger, Aspergillus niger 5-16, Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) 430, Bacillus subtilis, Bacillus subtilis 03. Jun, Bacillus subtilis F-11, Butyrivibrio fibrisolvens, Butyrivibrio fibrisolvens GS113, Clostridium acetobutylicum, Dichomitus squalens, Glycine max, Rhodotorula flava, Ruminococcus albus, Ruminococcus albus 8, Scopolia japonica, Streptomyces diastaticus, Streptomyces diastatochromogenes, Streptomyces diastatochromogenes 65, Streptomyces massasporeus, Streptomyces purpurascens, Streptomyces sp., Streptomyces sp. 17-1, Trichoderma reesei
Luonteri, E.; Siika-aho, M.; Tenkanen, M.; Viikari, L.
Purification and characterization of three alpha-arabinosidases from Aspergillus terreus
J. Biotechnol.
38
279-291
1995
Aspergillus awamori, Aspergillus niger, Aspergillus terreus, Bacillus subtilis, Streptomyces sp., Athelia rolfsii, Ruminococcus albus, Rasamsonia emersonii, Trichoderma reesei, Ruminococcus albus 8, Aspergillus awamori CMI 142717, Aspergillus niger N400(CBS 120-49)
-
Le Clinche, F.; Pinaga, F.; Ramon, D.; Valles, S.
alpha-L-arabinofuranosidases from Aspergillus terreus with potential application in enology: Induction, purification, and characterization
J. Agric. Food Chem.
45
2379-2383
1997
Aspergillus nidulans, Aspergillus niger, Aspergillus terreus, Bacillus subtilis, Pectobacterium carotovorum, Sclerotinia fructigena, Sclerotinia sclerotiorum, Streptomyces purpurascens, Trichoderma reesei, Aspergillus terreus CECT 2663, Aspergillus terreus VTT-D-82209
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
Christakopoulos, P.; Katapodis, P.; Hatzinikolaou, D.G.; Kekos, D.; Macris, B.J.
Purification and characterization of an extracellular alpha-L-arabinofuranosidase from Fusarium oxysporum
Appl. Biochem. Biotechnol.
87
127-133
2000
Aspergillus awamori, Aspergillus niger, Bacillus subtilis, Dichomitus squalens, Fusarium oxysporum, Ruminococcus albus, Streptomyces purpurascens, Trichoderma reesei, Fusarium oxysporum F3
Matsuo, N.; Kaneko, S.; Kuno, A.; Kobayashi, H.; Kusakabe, I.
Purification, characterization and gene cloning of two alpha-L-arabinofuranosidases from Streptomyces chartreusis GS901
Biochem. J.
346
9-15
2000
Arabidopsis thaliana, Aspergillus awamori, Aspergillus awamori IFO 4033, Aspergillus niger (P42254), Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) D3, Bacillus subtilis, Bacteroides ovatus (Q59218), Breznakibacter xylanolyticus, Pseudomonas fluorescens, Streptomyces chartreusis, Streptomyces chartreusis GS901, Streptomyces coelicolor, Streptomyces diastatochromogenes, Streptomyces lividans (P53627), Streptomyces lividans 66 1326 (P53627), Thermoclostridium stercorarium (O08457), Thermotoga maritima
Lee, R.C.; Burton, R.A.; Hrmova, M.; Fincher, G.B.
Barley arabinoxylan arabinofuranohydrolases: Purification, characterization and determination of primary structures from cDNA clones
Biochem. J.
356
181-189
2001
Arabidopsis thaliana, Geobacillus stearothermophilus, Bacillus subtilis, Bacillus sp. (in: Bacteria), Breznakibacter xylanolyticus, Hordeum vulgare, Streptomyces coelicolor, Thermotoga maritima, Thermoclostridium stercorarium (O08457), Aspergillus niger (P42254), Streptomyces chartreusis (P82593), Bacteroides ovatus (Q59218)
Shallom, D.; Belakhov, V.; Solomon, D.; Gilead-Gropper, S.; Baasov, T.; Shoham, G.; Shoham, Y.
The identification of the acid-base catalyst of alpha-arabinofuranosidase from Geobacillus stearothermophilus T-6, a family 51 glycoside hydrolase
FEBS Lett.
514
163-167
2002
Agrobacterium tumefaciens, Bacillus subtilis, Geobacillus stearothermophilus, Geobacillus stearothermophilus T-6, Halalkalibacterium halodurans, Mesorhizobium loti, Sinorhizobium meliloti, Streptomyces coelicolor, Streptomyces lividans, Streptomyces lividans 66 1326
Vandermarliere, E.; Bourgois, T.M.; Van Campenhout, S.; Strelkov, S.V.; Volckaert, G.; Delcour, J.A.; Courtin, C.M.; Rabijns, A.
Crystallization and preliminary X-ray analysis of an arabinoxylan arabinofuranohydrolase from Bacillus subtilis
Acta Crystallogr. Sect. F
63
692-694
2007
Bacillus subtilis
Bourgois, T.M.; Van Craeyveld, V.; Van Campenhout, S.; Courtin, C.M.; Delcour, J.A.; Robben, J.; Volckaert, G.
Recombinant expression and characterization of XynD from Bacillus subtilis subsp. subtilis ATCC 6051: a GH 43 arabinoxylan arabinofuranohydrolase
Appl. Microbiol. Biotechnol.
75
1309-1317
2007
Bacillus subtilis (Q45071), Bacillus subtilis
Vandermarliere, E.; Bourgois, T.M.; Winn, M.D.; van Campenhout, S.; Volckaert, G.; Delcour, J.A.; Strelkov, S.V.; Rabijns, A.; Courtin, C.M.
Structural analysis of a glycoside hydrolase family 43 arabinoxylan arabinofuranohydrolase in complex with xylotetraose reveals a different binding mechanism compared with other members of the same family
Biochem. J.
418
39-47
2009
Bacillus subtilis (Q45071), Bacillus subtilis
Inacio, J.M.; Correia, I.L.; de Sa-Nogueira, I.
Two distinct arabinofuranosidases contribute to arabino-oligosaccharide degradation in Bacillus subtilis
Microbiology
154
2719-2729
2008
Bacillus subtilis (P94531), Bacillus subtilis (P94552), Bacillus subtilis, Bacillus subtilis 168T+ (P94531)
Hoffmam, Z.B.; Oliveira, L.C.; Cota, J.; Alvarez, T.M.; Diogo, J.A.; Neto, M.; Citadini, A.P.; Leite, V.B.; Squina, F.M.; Murakami, M.T.; Ruller, R.
Characterization of a hexameric exo-acting GH51 alpha-L-arabinofuranosidase from the mesophilic Bacillus subtilis
Mol. Biotechnol.
55
260-267
2013
Bacillus subtilis (P94531), Bacillus subtilis, Bacillus subtilis 168 (P94531)
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