Proceedings of the Korean Biophysical Society Conference (한국생물물리학회:학술대회논문집)
- 1999.06a
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- Pages.35-35
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- 1999
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)
- Published : 1999.06.01
Abstract
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 (
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