The Multisubstrate Specificity and the Quaternary Structure of Cyclodextrin-/Pullulan-degrading Enzymes

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著者

    • Park Kwan Hwa PARK Kwan Hwa
    • Research Center for New Bio-Materials in Agriculture and Department of Food Science and Technology, School of Agricultural Biotechnology, Seoul National University

抄録

Multiple amino acid sequence alignment and crystal structures of cyclodextrin (CD)-/pullulandegrading enzymes revealed the presence of an N-terminal extension of approximately 130 residuesnot found in ordinary α-amylases. Based on the results obtained from size exclusion chromatogra-phy and sedimentation equilibrium ultracentrifugation experiments, most of these enzymes aremainly in monomer-dimer-tetramer or monomer-dimer-dodecamer equilibrium and the unique Nterminal domain contributes to the formation of oligomeric state in this group of enzymes. Thestudies on the oligomerization and activity of the CD-/pullulan-degrading enzymes indicated thatthere was a significant correlation between the presence of monomer-dimer equilibrium and enzymatic activity. They also suggested that both the monomer and dimer were enzymatically active, but with different substrate preference for fl-CD and starch. The substrate preference of a dimerfor fl-CD was interpreted from the geometry of the active site in the homodimer, that is, small andcompact substrate molecules such as fl-CD might effectively access to the deep and narrow activesite of the dimeric enzyme. Therefore, it was suggested that the monomer-dimer equilibrium present in the reaction mixture reflected different multisubstrate specificity of CD-/pullulan-degrading Multiple amino acid sequence alignment and crystal structures of cyclodextrin (CD)-/pullulan degrading enzymes revealed the presence of an N-terminal extension of approximately 130 residues not found in ordinary α-amylases. Based on the results obtained from size exclusion chromatography and sedimentation equilibrium ultracentrifugation experiments, most of these enzymes are mainly in monomer-dimer-tetramer or monomer-dimer-dodecamer equilibrium and the unique Nterminal domain contributes to the formation of oligomeric state in this group of enzymes. The studies on the oligomerization and activity of the CD-/pullulan-degrading enzymes indicated that there was a significant correlation between the presence of monomer-dimer equilibrium and enzymatic activity. They also suggested that both the monomer and dimer were enzymatically active, but with different substrate preference for β-CD and starch. The substrate preference of a dimer for β-CD was interpreted from the geometry of the active site in the homodimer, that is, small and compact substrate molecules such as fl-CD might effectively access to the deep and narrow activesite of the dimeric enzyme. Therefore, it was suggested that the monomer-dimer equilibrium present in the reaction mixture reflected different multisubstrate specificity of CD-/pullulan-degrading enzymes.

収録刊行物

  • 応用糖質科学 : oyo toshitsu kagaku = Journal of applied glycoscience

    応用糖質科学 : oyo toshitsu kagaku = Journal of applied glycoscience 48(3), 293-299, 2001-07-01

    The Japanese Society of Applied Glycoscience

参考文献:  36件中 1-36件 を表示

被引用文献:  2件中 1-2件 を表示

各種コード

  • NII論文ID(NAID)
    10008252941
  • NII書誌ID(NCID)
    AN10453916
  • 本文言語コード
    ENG
  • 資料種別
    REV
  • ISSN
    13403494
  • NDL 記事登録ID
    5831569
  • NDL 雑誌分類
    ZP24(科学技術--化学・化学工業--糖・澱粉)
  • NDL 請求記号
    Z17-15
  • データ提供元
    CJP書誌  CJP引用  NDL  J-STAGE 
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