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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- 吾郷 日出夫 AGO Hideo
- 日本たばこ産業株式会社医薬総合研究所
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- 宮野 雅司 MIYANO Masashi
- 日本たばこ産業株式会社医薬総合研究所
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著者
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- 吾郷 日出夫 AGO Hideo
- 日本たばこ産業株式会社医薬総合研究所
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- 宮野 雅司 MIYANO Masashi
- 日本たばこ産業株式会社医薬総合研究所
抄録
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
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- 日本結晶学会誌
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日本結晶学会誌 40(6), 389-397, 1998-12-31
The Crystallographic Society of Japan
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牛首 文隆 , 平田 雅一 , 平田 多佳子 , 中村 健一 , 村田 隆彦 , 小林 拓也 , 成宮 周
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