Structural Basis of Specific and Efficient Catalysis in Hematopoietic Prostaglandin D Synthase as an Glutathione S-Transferase.

• AGO Hideo

  日本たばこ産業株式会社医薬総合研究所

• MIYANO Masashi

  日本たばこ産業株式会社医薬総合研究所

Bibliographic Information

Other Title

• プロスタグランジンＤ２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
• プロスタグランジン D2 ゴウセイ コウソ タカイ ハンノウ トクイセイ ト コウリツ オ ソナエタ シンキ ナ グルタチオン テンイ コウソ
• 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

Abstract

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 PGH₂ to PGD₂.

Journal

• Nihon Kessho Gakkaishi

  Nihon Kessho Gakkaishi 40 (6), 389-396, 1998

  The Crystallographic Society of Japan

Details

• CRID: 1390282679064708864
• NII Article ID: 10002591188
• NII Book ID: AN00188364
• DOI: 10.5940/jcrsj.40.389
• ISSN: 18845576
• ISSN: 03694585
• NDL BIB ID: 4641370
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I4641370
• Text Lang: ja
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
• Abstract License Flag: Disallowed