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  • Title: Enzymatic synthesis of a new inhibitor of alpha-amylases: acarviosinyl-isomaltosyl-spiro-thiohydantoin.
    Author: Kandra L, Remenyik J, Batta G, Somsák L, Gyémánt G, Park KH.
    Journal: Carbohydr Res; 2005 May 23; 340(7):1311-7. PubMed ID: 15854600.
    Abstract:
    Synthesis of acarviosinyl-isomaltosyl-spiro-thiohydantoin in yields up to 20%, has been achieved by Bacillus stearothermophilus maltogenic amylase (BSMA). BSMA is capable of transferring the acarviosine-glucose residue from an acarbose donor onto glucopyranosylidene-spiro-thiohydantoin. Reactions were followed using HPLC and MALDI-TOF MS. 1H and 13C NMR studies revealed that the enzyme reserved its stereoselectivity. Glycosylation took place mainly at C-6 resulting in alpha-acarviosinyl-(1-->4)-alpha-D-glucopyranosyl-(1-->6)-D-glucopyranosylidene-spiro-thiohydantoin. This compound was found to be a much more efficient salivary amylase inhibitor than glucopyranosylidene-spiro-thiohydantoin with kinetic constants of K(EI)=0.19 microM and K(ESI)=0.24 microM.
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