Kanaoka Y, Ago H, Inagaki E, Nanayama T, Miyano M, Kikuno R, Fujii Y, Eguchi N, Toh H, Urade Y, Hayaishi O
Department of Molecular Behavioral Biology, Osaka Bioscience Institute, Japan.
Cell. 1997 Sep 19;90(6):1085-95. doi: 10.1016/s0092-8674(00)80374-8.
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 isolated a cDNA for the rat enzyme, crystallized the recombinant enzyme, and determined the three-dimensional structure of the enzyme complexed with glutathione at 2.3 A 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 cleft leads to the putative substrate binding mode and its catalytic mechanism, responsible for the specific isomerization from PGH2 to PGD2.
造血前列腺素（PG）D合成酶是免疫系统和肥大细胞中前列腺素D和J系列生成的关键酶。我们分离出了大鼠该酶的cDNA，使重组酶结晶，并以2.3埃的分辨率确定了与谷胱甘肽复合的该酶的三维结构。该酶是脊椎动物中sigma类谷胱甘肽S-转移酶（GST）的首个成员，拥有一个作为活性位点的突出裂隙，这在GST家族的其他成员中从未见过。该裂隙独特的三维结构导致了假定的底物结合模式及其催化机制，负责从PGH2到PGD2的特异性异构化。
