Subsite Affinities of α-Glucosidases from Spinach Seeds

Satoshi Furui, Manabu Sugimoto, Yukio Suzuki

Research output: Contribution to journalArticle

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 - 1997

Keywords

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

ASJC Scopus subject areas

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

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