Two Additional Carbohydrate-Binding Sites of β-Amylase from Bacillus cereus var. mycoides Are Involved in Hydrolysis and Raw Starch-Binding
作者： Z. Ye
DOI: 10.1093/JB/MVH043
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摘要: In the previous X-ray crystallographic study, it was found that beta-amylase from Bacillus cereus var. mycoides has three carbohydrate-binding sites aside active site: two (Site2 and Site3) in domain B one (Site1) C. To investigate roles of these catalytic reaction raw starch-binding, Site1 Site2 were mutated. From analyses starch-binding wild-type mutant enzymes, contributes to binding affinity raw-starch more than Site2, capacity is maintained when either or exists. The starch-digesting ability this enzyme poor. inhibition studies by maltitol, GGX alpha-CD for hydrolyses maltopentaose (G5) amylose ( (n) = 16) catalyzed a competitive inhibitor, while, maltitol behaves as mixed-type inhibitor depending on chain length substrate enzyme. analysis mechanism, we conclude bindings form an abortive ESI complex used substrate.
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