Mould 1, 2-α-Mannosidases

概要

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Three mould 1, 2-α-mannosidases have been characterized. They were all monomeric enzymes with similar molecular weights of about 60 kDa, showed maximum activity at pH 5, and shared a similar sensitivity for glycosidase inhibitors. Chemical modification of mould 1, 2-α-mannosidases by water soluble carbodiimide resulted in a loss of their activity, suggesting that acidic amino acids were responsible for the catalytic action. Using 1-deoxymannojirimycin (dMM), a competitive inhibitor of Penicillium 1, 2-α-mannosidase as a protecting reagent in the modification, we identified an aspartic acid residue which was involved in the interaction of the enzyme with its substrate . An α-carboxyl structure was formed via an imide intermediate in the reaction with 1-ethyl-3- (3-dimethylaminopropyl) carbodiimide (EDC).
日本応用糖質科学会の論文