プロスタグランジンD_2合成酵素 高い反応特異性と効率を備えた新奇なグルタチオン転移酵素 Structural Basis of Specific and Efficient Catalysis in Hematopoietic Prostaglandin D Synthase as an Glutathione S-Transferase

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Hematopoietic prostaglandin (PG) D synthase is the key enzyme for production of the D and J series of prostanoids in the immune system and mast cells. We crystallized the recombinant enzyme, and determined the three-dimensional structure of the enzyme complexed 0 with glutathione at 2.3 Å resolution. The enzyme is the first member of the sigma class glutathione S-transferase (GST) from vertebrates and possesses a prominent cleft as the active site which is never seen among other members of the GST family. The unique 3-D architecture of the catalytic cleft leads to the putative substrate binding mode and its catalytic mechanism, responsible for the specific conversion of PGH<SUB>2</SUB> to PGD<SUB>2</SUB>.

収録刊行物

  • 日本結晶学会誌  

    日本結晶学会誌 40(6), 389-397, 1998-12-31 

    The Crystallographic Society of Japan

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各種コード

  • NII論文ID(NAID)
    10002591188
  • NII書誌ID(NCID)
    AN00188364
  • 本文言語コード
    JPN
  • 資料種別
    ART
  • ISSN
    03694585
  • NDL 記事登録ID
    4641370
  • NDL 雑誌分類
    ZM46(科学技術--地球科学--岩石・鉱物・鉱床)
  • NDL 請求記号
    Z15-138
  • データ提供元
    CJP書誌  NDL  J-STAGE 
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