Modulation of Substrate Preference of Thermus Maltogenic Amylase by Mutation of the Residues at the Interface of a Dimer

スポンサーリンク

概要

• 論文の詳細を見る

• To elucidate the relationship between the substrate size and geometric shape of the catalytic site of Thermus maltogenic amylase, Gly50, Asp109, and Val431, located at the interface of the dimer, were replaced with bulky amino acids. The kcat⁄Km value of the mutant for amylose increased significantly, whereas that for amylopectin decreased as compared to that of the wild-type enzyme. Thus, the substituted bulky amino acid residues modified the shape of the catalytic site, such that the ability of the enzyme to distinguish between small and large molecules like amylose and amylopectin was enhanced.

• 社団法人 日本農芸化学会の論文

著者

• LEE Byong

  Department of Biomedical Engineering and Materials, School of Medicine, Soonchunhyang University

• PARK Sung-Hoon

  Department of Laboratory Animal Medicine, College of Veterinary Medicine and KRF Zoonotic Disease Pr

• PARK Kwan-Hwa

  Center for Agricultural Biomaterials, National Laboratory for Functional Food Carbohydrates, and Dep

• Oh Byung-ha

  Department Of Macromolecular Sciences Smithkline Beecham Pharmaceuticals King Of Prussia

• KANG Hee-Kwon

  Center for Agricultural Biomaterials and Department of Food Science and Biotechnology, School of Agr

• CHA Hyunju

  Center for Agricultural Biomaterials and Department of Food Science and Biotechnology, School of Agr

• KIM Jung-Wan

  Department of Biology, University of Incheon

• SHIM Jae-Hoon

  Center for Agricultural Biomaterials and Department of Food Science and Biotechnology, College of Ag

• WOO Eui-Jeon

  Systemic Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology

• HONG Jung-Sun

  Systemic Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology

関連論文

• Fabrication and characterization of t-ZrO2 supported small tubular SOFC
• Microbiological Quality Assessment of Laboratory Mice in Korea and Recommendations for Quality Improvement
• Purification and Characterization of a Novel Fibrinolytic Enzyme from Bacillus sp. KA38 Originated from Fermented Fish
• Validation of porcine corneal opacity and permeability assay as an alternative to eye irritation tests
• Maltosyl-erythritol, a Major Transglycosylation Product of Erythritol by Bacillus stearothermophilus Maltogenic Amylase(Food & Nutrition Science)
• Analysis of Policy Alternatives on the Public Acceptance of Nuclear Power Plant in Korea
• Antioxidative Effects of Glycosyl-ascorbic Acids Synthesized by Maltogenic Amylase to Reduce Lipid Oxidation and Volatiles Production in Cooked Chicken Meat
• TreX from Sulfolobus solfataricus ATCC 35092 Displays Isoamylase and 4-α-Glucanotransferase Activities
• Modulation of Substrate Preference of Thermus Maltogenic Amylase by Mutation of the Residues at the Interface of a Dimer
• Engineering Thermus Maltogenic Amylase with Improved Thermostability : Probing the Role of the Conserved Calcium Binding Site in Cyclodextrin-degrading Enzymes
• Synthesis of Branched Oligosaccharides from Starch by Two Amylases Cloned from Bacillus licheniformis
• 平成17年度日本応用糖質科学会特別学会賞受賞講演 Function and Tertiary- and Quaternary-structure of Cyclodextrin-hydrolyzing Enzymes(CDase), a Group of Multisubstrate Specific Enzymes Belonging to the α-Amylase Family
• TreX from Sulfolobus solfataricus ATCC 35092 Displays Isoamylase and 4-α-Glucanotransferase Activities
• Microbiological Quality Assessment of Laboratory Mice in Korea and Recommendations for Quality Improvement
• Modulation of Substrate Preference of Thermus Maltogenic Amylase by Mutation of the Residues at the Interface of a Dimer

もっと見る 閉じる

スポンサーリンク