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
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>.
日本結晶学会誌 40(6), 389-397, 1998-12-31
The Crystallographic Society of Japan