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.
The taxonomic range for the selected organisms is: Acetivibrio thermocellus The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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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.
the enzyme recognizes both the L-Araf motif and its D-Galf analogue. The arabinofuranosidase is also able to hydrolyze galactosyl derivatives and is efficient in catalyzing oligomerisations using 4-nitrophenyl furanosides as donors. Molecular dynamics and active site structure determination and analysis by NMR, substrate specificity, and product structures by mass spectrometry and NMR.overview
good substrates are rye and wheat arabinoxylan and oat spelt xylan with release of L-arabinose. Lower activity with xylan from beechwood and birchwood, arabinogalactan, arabinan from sugar beet, carboxy methyl cellulose and carboxy ethylcellulose
good substrates are rye and wheat arabinoxylan and oat spelt xylan with release of L-arabinose. Lower activity with xylan from beechwood and birchwood, arabinogalactan, arabinan from sugar beet, carboxy methyl cellulose and carboxy ethylcellulose
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
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
the enzyme displays an N-terminal catalytic module CtGH43 followed by two carbohydrate binding modules CtCBM6A and CtCBM6B towards the C-terminus. Circular dichroism analysis of catalytic domain CtGH43 shows 48% beta-sheets, 49% random coils but only 3% alpha-helices
the enzyme displays an N-terminal catalytic module CtGH43 followed by two carbohydrate binding modules CtCBM6A and CtCBM6B towards the C-terminus. Circular dichroism analysis of catalytic domain CtGH43 shows 48% beta-sheets, 49% random coils but only 3% alpha-helices
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His6-tagged truncated enzyme, sitting drop vapour diffusion method, mixing of 120 mg/ml protein in 50 mM HEPES, pH 7.5, 200 mM NaCl, and 5 mM CaCl2 with precipitant solution containing 0.1 M sodium acetate pH 4.5, 2 M ammonium sulfate and (b) 0.1 M Tris, pH 8.5, 20% PEG 2000 monomethyl ether, 0.2 M trimethyl N-oxide for brick shaped crystals or containing 0.1 M Tris, pH 8.5, 20% PEG 2000 monomethyl ether, 0.2 M trimethyl N-oxide for monoclinic crystals, X-ray diffraction structure determination and analysis at resolution of 1.65 A for the cubic form and 1.1 A for the monoclinic form, molecular replacement method
vapor diffusion method, using either 0.1 M sodium acetate pH 4.5, 2 M ammonium sulfate or 0.1 M Tris pH 8.5, 20% (w/v) PEG 2000 monomethyl ether, 0.2 M trimethylamine N-oxide
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
truncated 903 bp gene encoding the N-terminus of CtGH43 is part of a full-length family 43 glycoside hydrolase Ct43Araf which also contains two tandem family 6 carbohydrate-binding modules, CtCBM6A (405 bp) and CtCBM6B (402 bp), at the C-terminus, recombinant expression of the His6-tagged truncated enzyme in Escherichia coli strain BL21(DE3) pLysS
hydrolysis of insoluble wheat arabinoxylan using different endoxylanases in combination with arabinofuranosidase Araf51A. The optimized combination is endoxylanases XynZ/Xyn11A/Araf51A with a loading ratio of 2:2:1, and the value of degree of synergy increases with the increase of Araf51A proportion in the enzyme mixture. Both free and enzymes immobilized on commercial magnetic nanoparticles show a similar conversion to reducing sugars after hydrolysis for 48 h. After 10 cycles, approximately 20% of the initial enzymatic activity of both the individual or mixture of immobilized enzymes is retained, with 5.5fold increase in the production of sugars. A sustainable synergism between immobilized arabinofuranosidase and immobilized endoxylanases in the hydrolysis of arabinoxylan is observed
Crystallization and preliminary X-ray crystallographic analysis of a novel alpha-L-arabinofuranosidase (CtGH43) from Clostridium thermocellum ATCC 27405
Ahmed, S.; Luis, A.; Bras, J.; Fontes, C.; Goyal, A.
The family 6 carbohydrate-binding module (CtCBM6B) of Clostridium thermocellum alpha-L-arabinofuranosidase binds xylans and thermally stabilized by Ca2+ ions
Molecular determinants of substrate specificity revealed by the structure of Clostridium thermocellum arabinofuranosidase 43A from glycosyl hydrolase family 43 subfamily 16