Crystallization (Comment) | Organism |
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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 | UniProt | Comment | Textmining |
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Aspergillus luchuensis | Q8NK89 | - |
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Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
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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 | Comment | Organism |
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AkAbf54 | - |
Aspergillus luchuensis |
family 54 alpha-L-arabinofuranosidase | - |
Aspergillus luchuensis |