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Literature summary for 3.2.1.55 extracted from

  • Miyanaga, A.; Koseki, T.; Miwa, Y.; Mese, Y.; Nakamura, S.; Kuno, A.; Hirabayashi, J.; Matsuzawa, H.; Wakagi, T.; Shoun, H.; Fushinobu, S.
    The family 42 carbohydrate-binding module of family 54 alpha-L-arabinofuranosidase specifically binds the arabinofuranose side chain of hemicellulose (2006), Biochem. J., 399, 503-511.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
to determine the structure of the complex between AkAbf54 and arabinofuranosyl-alpha-1,2-xylobiose derived from natural xylan, the E221A mutant is used to prevent hydrolysis of the ligand. Measurement of the crystallographic data of the E221A mutant soaked with arabinotriose at a 2.8 A resolution Aspergillus luchuensis

Organism

Organism UniProt Comment Textmining
Aspergillus luchuensis Q8NK89
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
arabinoxylan + H2O the arabinose-binding domain of AkAbf54 is named AkCBM42. In the complex between AkAbf54 and arabinofuranosyl-alpha-1,2-xylobiose, the arabinose moiety occupies the binding pocket of AkCBM42, whereas the xylobiose moiety is exposed to the solvent. AkCBM42 facilitates the hydrolysis of insoluble arabinoxylan, because mutants at the arabinose binding site exhibit markedly decreased activity. AkCBM42 interacts with arabinose-substituted, but not with unsubstituted, hemicelluloses Aspergillus luchuensis ?
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Synonyms

Synonyms Comment Organism
AkAbf54
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Aspergillus luchuensis
family 54 alpha-L-arabinofuranosidase
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Aspergillus luchuensis