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Information on EC 3.2.1.55 - non-reducing end alpha-L-arabinofuranosidase
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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 expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
arabinofuranosidase, arabinosidase, alpha-l-araf, alpha-l-arabinosidase, alpha-arabinosidase, afase, alpha-l-arabinofuranosidase b, arabinoxylan arabinofuranohydrolase, alpha-araf, alpha-arabinofuranosidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ABF
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-
-
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alpha-arabinofuranosidase
-
-
-
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alpha-arabinosidase
-
-
-
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Alpha-L-AF
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-
-
-
alpha-L-arabinanase
-
-
-
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alpha-L-arabinofuranoside hydrolase
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-
-
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alpha-L-arabinosidase
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-
-
-
arabinosidase
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-
-
-
L-arabinosidase
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-
-
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polysaccharide 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
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
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-
-
-
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
additional information
?
-
a highly thermostable exo-acting hemicellulase that exhibits a relatively higher activity towards arabinan and arabinoxylan, compared with other glycoside hydrolase 51 family enzymes
-
-
?
additional information
?
-
-
a highly thermostable exo-acting hemicellulase that exhibits a relatively higher activity towards arabinan and arabinoxylan, compared with other glycoside hydrolase 51 family enzymes
-
-
?
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
?
-
a highly thermostable exo-acting hemicellulase that exhibits a relatively higher activity towards arabinan and arabinoxylan, compared with other glycoside hydrolase 51 family enzymes
-
-
?
additional information
?
-
-
a highly thermostable exo-acting hemicellulase that exhibits a relatively higher activity towards arabinan and arabinoxylan, compared with other glycoside hydrolase 51 family enzymes
-
-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to the glycoside hydrolase 51 family, GH51
additional information
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
-
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
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). Q9WYB7_THEMA
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
484
0
55268
TrEMBL
-
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the enzyme is organized by two domains: a catalytic N-terminal (beta/alpha)8-barrel domain and a C-terminal beta-strand sandwich domain, three-dimensional structure, interaction at the dimer interface, overview
additional information
-
the enzyme is organized by two domains: a catalytic N-terminal (beta/alpha)8-barrel domain and a C-terminal beta-strand sandwich domain, three-dimensional structure, interaction at the dimer interface, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged enzyme in complex with a branched tetrasaccharide O-beta-D-xylopyranosyl-(1->4)-O-alpha-L-arabinofuranosyl-(1->3)-O-beta-D-xylopyranosyl-(1->4)-O-beta-D-xylopyranoside, sitting drop vapor-diffusion method, mixing 0.0015 ml of protein solution containing 14 mg/ml protein, 50 mM Tris-HCl, pH 7.5, 50 mM NaCl, and 5.0% 2-mercaptoethanol, with an equal volume of the reservoir solution, 16.1°C, X-ray diffraction structure determination and analysis
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain MC1061 by nickel affinity chromatography, dialysis, and gel filtration, to homogeneity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
constitutive recombinant expression of His-tagged enzyme in Escherichia coli strain MC1061
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dumbrepatil, A.; Park, J.M.; Jung, T.Y.; Song, H.N.; Jang, M.U.; Han, N.S.; Kim, T.J.; Woo, E.J.
Structural analysis of alpha-L-arabinofuranosidase from Thermotoga maritima reveals characteristics for thermostability and substrate specificity
J. Microbiol. Biotechnol.
22
1724-1730
2012
Thermotoga maritima (Q9WYB7), Thermotoga maritima, Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 (Q9WYB7)
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