Subsite Affinities of α-Glucosidases from Spinach Seeds

Satoshi Furui, Manabu Sugimoto, Yukio Suzuki

    Research output: Contribution to journalArticlepeer-review

    1 Citation (Scopus)

    Abstract

    The rate parameters for maltooligosaccharides of two α-glucosidases from spinach seeds were examined and subsite affinities were evaluated. The subsite affinities for subsites 1, 2, 3, 4, 5, 6, and 7 in the active site of α-glucosidase A and B were 1.73, 2.91, 1.10, 0.25, 0.94, 0.03, and −0.01 kcal/mol, and 0.33, 4.94, 0.26, 0.14, −0.24, −0.52, and 0.14 kcal/mol, respectively. The six and four subsites exist in α-glucosidase A and B, respectively, which maltooligosaccharides or soluble starch could be bound.

    Original languageEnglish
    Pages (from-to)1382-1383
    Number of pages2
    JournalBioscience, Biotechnology and Biochemistry
    Volume61
    Issue number8
    DOIs
    Publication statusPublished - Jan 1997

    Keywords

    • Multiple molecular forms
    • Spinach seeds
    • Subsite affinity
    • α-glucosidase

    ASJC Scopus subject areas

    • Biotechnology
    • Analytical Chemistry
    • Biochemistry
    • Applied Microbiology and Biotechnology
    • Molecular Biology
    • Organic Chemistry

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