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Enzyme Nomenclature
Information on EC 3.2.1.55 - non-reducing end alpha-L-arabinofuranosidase
for references in articles please use BRENDA:EC3.2.1.55
Word Map on EC 3.2.1.55
- 3.2.1.55
- xylans
-
arabinoxylans
- arabinose
- arabinans
- xylose
- arabinogalactans
-
hemicellulases
- endoxylanase
- biotechnology
- nutrition
- spelt
-
arabinosylated
- xylobiose
- xylanases
-
pectic
- p-nitrophenyl-alpha-l-arabinofuranoside
-
xylanolytic
- food industry
-
rhamnogalacturonans
- xylooligosaccharides
-
debranched
-
feruloylated
-
cellulose-binding
-
arabinose-containing
- l-arabitol
- paper production
- arabinobiose
- synthesis
- degradation
- p-nitrophenyl-beta-d-xylopyranoside
-
xylopyranosyls
- kawachii
-
anti-complementary
-
five-bladed
-
hemicellulolytic
- arabinofuranose
- cellulosa
- agriculture
-
oat-spelts
-
xylan-degrading
-
exo-acting
-
arabino-oligosaccharides
- analysis
- industry
- drug development
- medicine
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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EC NUMBER 
COMMENTARY 
3.2.1.55
-
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RECOMMENDED NAME
GeneOntology No.
non-reducing end alpha-L-arabinofuranosidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides
hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides
-
-
-
-
hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides
the enzyme also 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
-
hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides
exo-acting enzyme
hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides
endolytic mode of action
-
hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides
catalytic mechanism, 2 stable states in the double displacement mechanism with formation of a transient covalent arabinofuranosyl-enzyme intermediate, structure of enzyme-substrate complex, substrate binding and specificity
-
hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides
catalytic mechanism, Glu175 is the acid-base residue, Glu294 functions as the catalytic nucleophile
hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides
enzyme shows 2 catalytic activities: alpha-L-arabinofuranosidase and beta-D-xylosidase activity
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
-
hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides
catalytic mechanism and substrate binding structure, overview
-
hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides
mode of action of Penicillium funiculosum family 62 isozymes, overview
-
hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides
the enzyme hydrolyze the glycosidic bond via the double-displacement mechanism in the active site of a funnel-shaped pocket, catalytic residues are the acid/base Glu172 and the enzymatic nucleophile Glu281
hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides
the enzyme also 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
-
-
hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides
exo-acting enzyme
-
-
hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides
endolytic mode of action
-
-
hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides
the enzyme hydrolyze the glycosidic bond via the double-displacement mechanism in the active site of a funnel-shaped pocket, catalytic residues are the acid/base Glu172 and the enzymatic nucleophile Glu281
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
hydrolysis of O-glycosyl bond
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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.
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CAS REGISTRY NUMBER
COMMENTARY
9067-74-7
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional beta-xylosidase/alpha-L-arabinofuranosidase, EC 3.2.1.37/EC 3.2.1.55
UniProt
Rhodotorula flava
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
171754, 171764, 288807, 288808, 288809, 288810, 288811, 288812, 288813, 288814, 288815, 288816, 288818, 288820, 288822, 288823, 288824, 288826, 288828, 288829, 288830, 288831, 288832, 288833, 288834, 288835, 288837, 288838, 288840, 288841, 288842, 288843, 288849
-
-
-
171764, 288809, 288812, 288813, 288816, 288822, 288828, 288829, 288835, 288837, 288842, 288845, 288846, 288850, 677383
-
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strain 31B, 2 distinct type B enzymes encoded by different genes
-
-
Rhodotorula flava
yeast, strain IFO 0407, also called Cryptococcus flavus, Torula flava, Chromotorula flava
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-
IFO 3389
-
-
a soil deuteromycete, genes PfabfB1, PfabfB2, PfabfB3, and PfabfB4
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-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
the enzyme belongs to the glycosyl hydrolase family 43, GH43
evolution
the enzyme belongs to the alpha-L-AF C superfamily, which is associated with glycoside hydrolase family 51, but the enzyme's properties are unique
evolution
the enzyme belongs to glycosyl hydrolase family 51, GH51
evolution
the enzyme belongs to the family 51 glycoside hydrolase, GH51; the enzyme belongs to the family 54 glycoside hydrolase, GH54
evolution
-
the enzyme belongs to glycosyl hydrolase family 43, GH43
evolution
-
the isozymes belong to the family 62 glycoside hydrolase, GH62, sequence comparisons, only isozyme PfABF62c is unique in bearing at its N-terminus a canonical family 1 carbohydrate-binding module of 37 amino acids length, which helps the protein to bind to microcrystalline cellulose
evolution
isozyme AFS1 belongs to the family 54 glycoside hydrolase, GH54
evolution
isozyme AFQ1 belongs to the family 51 glycoside hydrolase, GH51
evolution
-
the enzyme belongs to the family 51 glycoside hydrolase, GH51
evolution
the enzyme belongs to the family 62 glycoside hydrolase, GH62, phylogenetic analysis. The overall three-dimensional structure of PaAbf62A reveals a five-bladed beta-propeller fold that confirms its predicted classification into clan GH-F together with GH43 alpha-L-arabinofuranosidases, structure-function relationships within the GH62 family, overview
evolution
Q4P6F4;
the enzyme belongs to the family 62 glycoside hydrolase, GH62, phylogenetic analysis. The overall three-dimensional structure of PaAbf62A reveals a five-bladed beta-propeller fold that confirms its predicted classification into clan GH-F together with GH43 alpha-L-arabinofuranosidases, structure-function relationships within the GH62 family, overview
evolution
-
the enzyme belongs to the family 62 glycoside hydrolase, GH62. The crystal structure comprises a carbohydrate-binding module family 13 domain at its N-terminus and a catalytic domain at its C-terminus
evolution
the enzyme belongs to the glycoside hydrolase 51 family, GH51
evolution
the enzyme belongs to the family 51 glycoside hydrolase, GH51
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
evolution
the enzyme belongs to the family 43 glycoside hydrolase, GH43
evolution
-
the enzyme belongs to glycosyl hydrolase family 54, GH54
-
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
-
evolution
-
isozyme AFS1 belongs to the family 54 glycoside hydrolase, GH54; the enzyme belongs to the family 51 glycoside hydrolase, GH51; the enzyme belongs to the family 54 glycoside hydrolase, GH54
-
evolution
-
the enzyme belongs to the family 43 glycoside hydrolase, GH43; the enzyme belongs to the glycosyl hydrolase family 43, GH43
-
evolution
-
the enzyme belongs to the family 62 glycoside hydrolase, GH62. The crystal structure comprises a carbohydrate-binding module family 13 domain at its N-terminus and a catalytic domain at its C-terminus
-
evolution
-
the enzyme belongs to the alpha-L-AF C superfamily, which is associated with glycoside hydrolase family 51, but the enzyme's properties are unique
-
evolution
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
the enzyme belongs to the glycoside hydrolase 51 family, GH51
-
evolution
-
the enzyme belongs to the family 62 glycoside hydrolase, GH62, phylogenetic analysis. The overall three-dimensional structure of PaAbf62A reveals a five-bladed beta-propeller fold that confirms its predicted classification into clan GH-F together with GH43 alpha-L-arabinofuranosidases, structure-function relationships within the GH62 family, overview
-
metabolism
the presence of L-arabinofuranoside side chains restricts the action of endo-acting xylanases. Therefore, the AFases are the most important accessory enzymes involved in synergy with other hemicellulases for the complete hydrolysis of hemicelluloses
metabolism
-
the presence of L-arabinofuranoside side chains restricts the action of endo-acting xylanases. Therefore, the AFases are the most important accessory enzymes involved in synergy with other hemicellulases for the complete hydrolysis of hemicelluloses
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physiological function
-
alpha-L-arabinanases are essential glycosyl hydrolases participating in the complete hydrolysis of hemicellulose
physiological function
BXL1 is a bifunctional beta-D-xylosidase/alpha-L-arabinofuranosidase required for pectic arabinan modification in Arabidopsis mucilage secretory cells, overview. BXL1 is acting as an alpha-L-arabinofuranosidase in the seed coat during vascular development
physiological function
arabinoxylan arabinofuranohydrolase AXS5 is involved in xylan degradation
physiological function
-
the enzyme participates in the hydrolysis of arabinoxylans in corn/wheat fibers used in poultry feed
physiological function
isozyme PcABF43A together with isozyme AFS1 function as debranching enzymes in this fungus
physiological function
isozyme AFQ1 plays a role of saccharification in the degradation of L-arabinan by this fungus; isozyme PcABF43A together with isozyme AFS1 function as debranching enzymes in this fungus
physiological function
A0A0F6VYJ7;
the enzyme shows synergism with xylanase Xyn11E, leading to a 2.54fold increase in the amount of sugars released. It does not show synergism with the xylanases of families GH10 or GH30
physiological function
B6T9B9;, K7UQ06;
elongation growth of cells with type II cell walls is accompanied by the up-regulation of specific and predicted alpha-L-arabinofuranosidase genes, and the corresponding activity is pronounced and is important for the modification of glucuronoarabinoxylan; elongation growth of cells with type II cell walls is accompanied by the up-regulation of specific and predicted alpha-L-arabinofuranosidase genes, and the corresponding activity is pronounced and is important for the modification of glucuronoarabinoxylan; elongation growth of cells with type II cell walls is accompanied by the up-regulation of specific and predicted alpha-L-arabinofuranosidase genes, and the corresponding activity is pronounced and is important for the modification of glucuronoarabinoxylan
physiological function
-
the enzyme shows synergism with xylanase Xyn11E, leading to a 2.54fold increase in the amount of sugars released. It does not show synergism with the xylanases of families GH10 or GH30
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physiological function
-
arabinoxylan arabinofuranohydrolase AXS5 is involved in xylan degradation; isozyme PcABF43A together with isozyme AFS1 function as debranching enzymes in this fungus
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additional information
tryptic peptide mass fingerprinting, overview
additional information
comparison of isozyme gene expression profiles
additional information
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comparison of isozyme gene expression profiles
additional information
comparison of isozyme gene expression profiles; comparison of isozyme gene expression profiles
additional information
comparison of isozyme gene expression profiles; comparison of isozyme gene expression profiles
additional information
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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
additional information
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the catalytic domain is a five-bladed beta-propeller consisting of five radially oriented anti-parallel beta-sheets, substrate binding at five subsites in the catalytic cleft and an L-arabinose-binding pocket at the bottom of the cleft. Asp202 and Glu361 are catalytic residues, and Trp270, Tyr461, and Asn462 are involved in the substrate-binding site for discriminating the substrate structures
additional information
tight domain associations found in the enzyme, such as an interdomain disulfide bond (Cys306 and Cys476) in each monomer, an extended arm (amino acids 374-385) at the dimer interface, and total 12 salt bridges in the hexamer, may account for the thermostability of the enzyme. One of the xylan binding determinants (Trp96) is identified in the active site, and a region of amino acids (374-385) protrudes out forming an obvious wall at the substrate-binding groove to generate a cavity. The altered cavity shape with a strong negative electrostatic distribution is likely related to the unique substrate preference of TmAFase towards branched polymeric substrates
additional information
the recombinant enzyme shows a synergistic effect in combination with endoxylanase on the degradation of oat spelt xylan and wheat arabinoxylan
additional information
structure-function analysis, molecular modeling and molecular dynamic simulations, overview
additional information
the enzyme displays an N-terminal catalytic module CtGH43 followed by two carbohydrate binding modules CtCBM6A and CtCBM6B towards the C-terminus, CtCBM6A and CtCBM6B do not have any effect on the enzyme activity
additional information
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structure-function analysis, molecular modeling and molecular dynamic simulations, overview
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additional information
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the recombinant enzyme shows a synergistic effect in combination with endoxylanase on the degradation of oat spelt xylan and wheat arabinoxylan
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additional information
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comparison of isozyme gene expression profiles
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additional information
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the enzyme displays an N-terminal catalytic module CtGH43 followed by two carbohydrate binding modules CtCBM6A and CtCBM6B towards the C-terminus, CtCBM6A and CtCBM6B do not have any effect on the enzyme activity
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additional information
-
the catalytic domain is a five-bladed beta-propeller consisting of five radially oriented anti-parallel beta-sheets, substrate binding at five subsites in the catalytic cleft and an L-arabinose-binding pocket at the bottom of the cleft. Asp202 and Glu361 are catalytic residues, and Trp270, Tyr461, and Asn462 are involved in the substrate-binding site for discriminating the substrate structures
-
additional information
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
tight domain associations found in the enzyme, such as an interdomain disulfide bond (Cys306 and Cys476) in each monomer, an extended arm (amino acids 374-385) at the dimer interface, and total 12 salt bridges in the hexamer, may account for the thermostability of the enzyme. One of the xylan binding determinants (Trp96) is identified in the active site, and a region of amino acids (374-385) protrudes out forming an obvious wall at the substrate-binding groove to generate a cavity. The altered cavity shape with a strong negative electrostatic distribution is likely related to the unique substrate preference of TmAFase towards branched polymeric substrates
-
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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
(1-5)-alpha-L-arabinofuranohexaose + H2O
alpha-L-arabinofuranose
-
-
-
?
1,5-methyl alpha-L-arabinofuranobioside + H2O
methyl alpha-L-arabinofuranose
-
-
-
-
?
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
-
-
-
-
?
2',4',6'-trichlorophenyl alpha-L-arabinofuranoside + H2O
2,4,6-trichlorophenol + alpha-L-arabinofuranose
2',5'-dinitrophenyl alpha-L-arabinofuranoside + H2O
2,5-dinitrophenol + alpha-L-arabinofuranose
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
-
1.7% of activity with p-nitrophenyl-alpha-L-arabinofuranoside
-
-
?
3',4'-dinitrophenyl alpha-L-arabinofuranoside + H2O
3',4'-dinitrophenol + alpha-L-arabinofuranose
-
-
-
r
3-nitrophenyl-alpha-L-arabinofuranoside + H2O
3-nitrophenol + alpha-L-arabinofuranose
-
-
-
r
3-O-alpha-L-arabinofuranosyl-alpha-L-arabinofuranoside + H2O
alpha-L-arabinofuranose
-
-
-
-
?
4-chloro-2-nitrophenyl-alpha-L-arabinofuranoside + H2O
4-chloro-2-nitrophenol + L-arabinofuranose
4-methylumbelliferyl alpha-L-arabinofuranoside + H2O
4-methylumbelliferol + alpha-L-arabinofuranose
4-methylumbelliferyl-alpha-L-arabinopyranoside + H2O
4-methylumbelliferol + alpha-L-arabinopyranose
4-nitrophenyl alpha-D-galactopyranoside + H2O
4-nitrophenol + alpha-D-galactopyranose
-
isoform AbfII exhibits very low activity with this substrate
-
-
?
4-nitrophenyl alpha-D-glucoside + H2O
4-nitrophenol + D-glucose
-
9% of the rate exhibited on p-nitrophenyl-alpha-L-arabinofuranoside
-
-
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
?
-
-
-
-
?
4-nitrophenyl alpha-L-arabinopyranoside + H2O
?
-
-
-
-
?
4-nitrophenyl beta-D-glucofuranoside + H2O
4-nitrophenol + beta-D-glucofuranose
-
very low activity
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranoside
low activity
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-mannopyranoside + H2O
4-nitrophenol + beta-D-mannopyranose
-
isoform AbfII exhibits very low activity with this substrate
-
-
?
4-nitrophenyl beta-D-mannoside + H2O
4-nitrophenol + D-mannose
-
3.4% activity compared to 4-nitrophenyl alpha-L-arabinofuranoside
-
-
?
4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + D-xylose
-
100% activity
-
-
?
4-nitrophenyl beta-L-fucopyranoside + H2O
4-nitrophenol + beta-L-fucopyranose
-
very low activity
-
-
?
4-nitrophenyl beta-L-galactofuranoside + H2O
4-nitrophenol + beta-L-galactofuranose
-
very low activity
-
-
?
4-nitrophenyl-alpha-L-arabinopyranoside + H2O
4-nitrophenyl + L-arabinopyranose
-
-
-
?
alkyl-alpha-arabinofuranoside + H2O
L-arabinose + alkyl alcohol
-
-
-
-
?
alpha-(1->5)-L-arabinofuranotriose + H2O
?
branched and unbranched, feruloylation of branched substrate strongly decreases the enzyme activity of isozyme rAFQ1
-
-
?
alpha-(1->5)-L-arabinofuranotriose + H2O
alpha-L-arabinofuranose
-
-
-
?
alpha-1,5-L-arabinohexaose + H2O
alpha-1,5-L-arabinobiose + alpha-1,5-L-arabinotetraose
-
-
-
-
?
alpha-1,5-L-arabinopentaose + H2O
alpha-1,5-L-arabinobiose + alpha-1,5-L-arabinotriose
-
-
-
-
?
alpha-1,5-L-arabinotriose + H2O
alpha-1,5-L-arabinobiose + alpha-L-arabinose
-
-
-
-
?
alpha-L-arabinan + H2O
oligo-alpha-1,5-L-arabinose + ?
-
-
the enzyme releases alpha-1,5-L-arabinobiose from the nonreducing end of the polysaccharide
-
?
alpha-L-arabinofuranoptetraose + H2O
alpha-L-arabinofuranose
-
-
-
?
alpha-L-arabinofuranosyl 1-naphthol + H2O
alpha-L-arabinofuranose + 1-naphthol
-
-
-
-
?
alpha-L-arabinofuranosyl 3,4-dinitrophenol + H2O
alpha-L-arabinofuranose + 3,4-dinitrophenol
-
-
-
-
?
alpha-L-arabinofuranosyl 3,5-dinitrophenol + H2O
alpha-L-arabinofuranose + 3,5-dinitrophenol
-
-
-
-
?
alpha-L-arabinofuranosyl 4-bromoisoquinoline + H2O
alpha-L-arabinofuranose + 4-bromoisoquinoline
-
-
-
-
?
alpha-L-arabinofuranosyl 4-methylumbelliferone + H2O
methylumbelliferone + alpha-L-arabinofuranose
alpha-L-arabinofuranosyl 4-phenylphenol + H2O
alpha-L-arabinofuranose + 4-phenylphenol
-
-
-
-
?
alpha-L-arabinofuranosyl-(1->2)-[alpha-L-arabinofuranosyl-(1->3)]-beta-D-xylopyranose + 2 H2O
2 L-arabinofuranose + D-xylopyranose
-
-
complete hydrolysis
-
?
alpha-L-arabinofuranosyl-1,4-alpha-D-xylopyranoside + H2O
L-arabinofuranose + D-xylopyranose
-
-
-
-
?
arabinan + H2O
alpha-L-arabinofuranose
-
from sugar beet, not from wheat
-
-
?
arabinoxylan + H2O
alpha-L-arabinofuranose + ?
-
soluble or insoluble
-
-
?
barley arabinoxylan + H2O
L-arabinose + ?
-
on barley arabinoxylan-0.76 the combination of isoform AbfA and AXH-d3 cleaves 35% of the total arabinose
-
-
?
ginsenoside Mc + H2O
ginsenoside K + L-arabinofuranose
-
-
-
?
ginsenoside Rd + H2O
ginsenoside K + D-glucopyranose
-
-
-
-
?
larch arabinoxylan + H2O
?
substrate of mutant F435Y/Y446F, no activity with the wild-type enzyme
-
-
?
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
o-nitrophenyl-beta-D-xylopyranoside + H2O
o-nitrophenol + beta-D-xylopyranose
-
3% of activity with p-nitrophenyl-alpha-L-arabinofuranoside
-
-
?
p-nitrophenyl alpha-L-arabinofuranoside + benzyl-alpha-D-xylopyranoside
?
-
-
-
-
?
p-nitrophenyl-alpha-D-galactopyranoside + H2O
p-nitrophenol + alpha-D-galactopyranose
6.1% of the activity of p-nitrophenyl-alpha-L-arabinofuranoside
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + alpha-D-glucopyranose
5.1% of the activity of p-nitrophenyl-alpha-L-arabinofuranoside
-
-
?
p-nitrophenyl-alpha-L-arabinopyranoside + H2O
p-nitrophenol + L-arabinopyranose
0.4% of the activity of p-nitrophenyl-alpha-L-arabinofuranoside
-
-
?
p-nitrophenyl-beta-D-fucopyranoside + H2O
p-nitrophenol + beta-D-fucopyranose
8.3% of the activity of p-nitrophenyl-alpha-L-arabinofuranoside
-
-
?
p-nitrophenyl-beta-D-galactofuranoside
beta-D-galactofuranosyl-(1,2)-beta-D-galactofuranoside + p-nitrophenol
-
-
-
-
?
p-nitrophenyl-beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactopyranose
-
0.33% of activity observed with p-nitrophenyl-alpha-L-arabinofuranoside
-
-
?
p-nitrophenyl-beta-D-galactopyranoside + H2O
p-nitrophenol + beta-D-galactopyranose
19% of the activity of p-nitrophenyl-alpha-L-arabinofuranoside
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
p-nitrophenol + ?
9.1% of the activity of p-nitrophenyl-alpha-L-arabinofuranoside
-
-
?
p-nitrophenyl-beta-D-mannopyranoside + H2O
p-nitrophenol + beta-D-mannopyranose
2.8% of the activity of p-nitrophenyl-alpha-L-arabinofuranoside
-
-
?
p-nitrophenyl-beta-D-xylofuranoside + H2O
p-nitrophenol + beta-D-xylofuranose
-
-
-
-
?
p-nitrophenyl-beta-D-xylopyranoside + H2O
p-nitrophenol + ?
0.9% of the activity of p-nitrophenyl-alpha-L-arabinofuranoside
-
-
?
phenyl-alpha-L-arabinofuranoside + H2O
phenol + L-arabinofuranose
-
-
-
-
?
polygalacturonase-soluble carbohydrates + H2O
?
-
PGSC of alfalfa cell walls
-
-
?
rye arabinoxylan + H2O
L-arabinose
-
on rye arabinoxylan-0.52 the combination of isoform AbfA and AXH-d3 cleaves 30% of the total arabinose
-
-
?
softwood Kraft pulp + H2O
L-arabinose + ?
-
arabinoglucuronoxlan I and II
-
-
?
sugar beet arabinan + H2O
arabinose + ?
-
0.82% L-arabinose liberated after 72 h incubation at 28°C
-
?
sugar beet arabinan + H2O
L-arabinofuranose + ?
-
-
release of 24.5% of L-arabinofuranose
-
?
wheat flour arabinoxylan + H2O
L-arabinofuranose + ?
-
-
release of 23% of L-arabinofuranose
-
?
wheat flour arabinoxylan + H2O
L-arabinose + ?
-
15.9% L-arabinose liberated after 72 h incubation at 28°C
-
?
(1-5)-alpha-L-arabinofuranooligosaccharides + H2O
alpha-L-arabinose + ?
-
-
-
-
?
(1-5)-alpha-L-arabinofuranooligosaccharides + H2O
alpha-L-arabinose + ?
-
-
-
-
?
1,5-alpha-L-arabinofuranohexaose + H2O
L-arabinose + L-arabinopentaose
-
-
-
-
?
1,5-alpha-L-arabinofuranohexaose + H2O
L-arabinose + L-arabinopentaose
-
-
-
-
?
1,5-alpha-L-arabinofuranohexaose + H2O
L-arabinose + L-arabinopentaose
-
-
-
-
?
1,5-alpha-L-arabinofuranohexaose + H2O
L-arabinose + L-arabinopentaose
-
-
-
-
?
1,5-alpha-L-arabinohexaose + H2O
1,5-alpha-L-arabinopentaose + L-arabinose
-
-
-
?
1,5-alpha-L-arabinohexaose + H2O
1,5-alpha-L-arabinopentaose + L-arabinose
-
-
-
-
?
1,5-alpha-L-arabinotetraose + H2O
L-arabinose
-
-
-
?
1,5-alpha-L-arabinotriose + H2O
1,5-alpha-L-arabinobiose + L-arabinose
-
-
-
?
1,5-alpha-L-arabinotriose + H2O
1,5-alpha-L-arabinobiose + L-arabinose
-
-
-
-
?
1,5-alpha-L-arabinotriose + H2O
L-arabinose
-
-
-
?
1,5-L-arabinan + H2O
L-arabinose + ?
-
-
-
-
ir
2',4',6'-trichlorophenyl alpha-L-arabinofuranoside + H2O
2,4,6-trichlorophenol + alpha-L-arabinofuranose
-
-
-
r
2',4',6'-trichlorophenyl alpha-L-arabinofuranoside + H2O
2,4,6-trichlorophenol + alpha-L-arabinofuranose
-
-
-
r
2',5'-dinitrophenyl alpha-L-arabinofuranoside + H2O
2,5-dinitrophenol + alpha-L-arabinofuranose
-
-
-
r
2',5'-dinitrophenyl alpha-L-arabinofuranoside + H2O
2,5-dinitrophenol + alpha-L-arabinofuranose
-
-
-
r
2,5-dinitrophenyl beta-D-xylopyranoside + H2O
2,5-dinitrophenol + beta-D-xylopyranose
-
-
-
-
?
2,5-dinitrophenyl beta-D-xylopyranoside + H2O
2,5-dinitrophenol + beta-D-xylopyranose
-
-
-
-
?
2,5-dinitrophenyl-alpha-L-arabinofuranoside + H2O
2,5-dinitrophenol + L-arabinofuranose
-
-
-
-
2,5-dinitrophenyl-alpha-L-arabinofuranoside + H2O
2,5-dinitrophenol + L-arabinofuranose
-
-
-
-
?
2,5-dinitrophenyl-alpha-L-arabinofuranoside + H2O
2,5-dinitrophenol + L-arabinofuranose
-
-
-
-
?
2-nitrophenyl beta-D-xylopyranoside + H2O
2-nitrophenol + beta-D-xylopyranose
-
-
-
-
?
2-nitrophenyl beta-D-xylopyranoside + H2O
2-nitrophenol + beta-D-xylopyranose
-
-
-
-
?
2-O-alpha-L-arabinofuranosyl-alpha-L-arabinofuranoside + H2O
alpha-L-arabinofuranose
-
-
-
-
?
2-O-alpha-L-arabinofuranosyl-alpha-L-arabinofuranoside + H2O