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Literature summary for 3.2.1.55 extracted from

  • Hövel, K.; Shallom, D.; Niefind, K.; Belakhov, V.; Shoham, G.; Baasov, T.; Shoham, Y.; Schomburg, D.
    Crystal structure and snapshots alaong the reaction pathway of a family 51 alpha-L-arabinofuranosidase (2003), EMBO J., 22, 4922-4932.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
native and selenomethionine-labeled wild-type enzyme, and mutant E175A in complex with substrates arabinofuranose, Ara-alpha(1-3)-Xyl and 4-nitrophenyl-Ara, from 23% w/v PEG 3350, 0.2 M NH4F, 5% v/v 2-propanol, 0.1 M Tris-HCl, pH 8.0, complex formation by soaking of crystals at 4°C in a cryo-solution containing additionally 12% glycerol and 20 mM of the substrate compounds, X-ray diffraction structure determination and analysis at 1.2-2.1 A resolution, modeling Geobacillus stearothermophilus

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus Q9XBQ3
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Geobacillus stearothermophilus T-6 Q9XBQ3
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Reaction

Reaction Comment Organism Reaction ID
1,5-alpha-L-arabinofuranohexaose + 5 H2O = 6 alpha-L-arabinofuranose 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 Geobacillus stearothermophilus

Subunits

Subunits Comment Organism
hexamer
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Geobacillus stearothermophilus
More each subunit is composed of 2 domains: a (beta/alpha)8-barrel and a 12-stranded beta sandwich with jelly-roll topology Geobacillus stearothermophilus

Synonyms

Synonyms Comment Organism
alpha-L-arabinofuranosidase
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Geobacillus stearothermophilus
More enzyme belongs to glycosidase family 51 Geobacillus stearothermophilus