Crystal Structure of a Maltogenic Amylase: Insights into a Catalytic Versatility

  • Oh, Sang-Taek (Department of Life Science, Pohang University of Science and Technology) ;
  • Cha, Sun-Shin (Department of Life Science, Pohang University of Science and Technolog) ;
  • Kim, Hyun-Ju (Department of Life Science, Pohang University of Science and Technolog) ;
  • Kim, Tae-Jip (Department of Food Science and Technology & Research Center for New Bio-materials in Agriculture, Seoul National University) ;
  • Cho, Hyun-Soo (Department of Life Science, Pohang University of Science and Technolog) ;
  • Park, Kwan-Hwa (Department of Food Science and Technology & Research Center for New Bio-materials in Agriculture, Seoul National University) ;
  • Oh, Byung-Ha (Department of Life Science, Pohang University of Science and Technology)
  • 발행 : 1999.06.01

초록

Amylases catalyze the hydrolysis of starch material and play central roles in carbohydrate metabolism. The structure and a size exclusion column chromatography proved that the enzyme is a dimer in solution. The N -terminal segment of the enzyme folds into a distinct domain and comprises the enzyme active site together with the central (${\alpha}$/ ${\beta}$)$\sub$8/ barrel of the adjacent subunit.(omitted)

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