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The structure and function of PGF synthase

PGF合酶的结构和功能

基本信息

批准号：
01570145
负责人：
WATANABE Kikuko
金额：
$ 1.41万
依托单位：
Osaka Bioscience Instutute
依托单位国家：
日本
项目类别：
Grant-in-Aid for General Scientific Research (C)
财政年份：
1989
资助国家：
日本
起止时间：
1989 至 1991
项目状态：
已结题

项目摘要

1. prostaglandin(PG)F synthase from bovine lung is a monomeric protein with a Mr of 36, 666 consisting of 323 amino acid residues. The enzyme is a dual function enzyme catalyzing the reduction of PGH_2 to PGF_<>a and PGD_2 to 9a, 11b-PGF_2 at different active sites on the swne molecule. The enzyme is constructed from at least two domains, and ^<195>Pro is related to the function of the binding site of PGD_2.2. About 50th, 200th, and 280th amino acid residues from N-terminus of PGF synthase are modified with the derivative of PGD_2, and so these amino acids may construct the active site for PGD_2.3. We reported that new type of PGF synthase was discovered in bovine liver which shows cross-reactivity with anti-PGF synthase antibody, but that the enzymatic property of liver PGF synthase was different from that of lung PGF synthase.We isolated cDNA clone which has 3 amino acids exchanged in the primary structure of lung PGF synthase. The property of the expressed protein of this clone was almost the same as that of lung PGF synthase, and the enzyme was the different type of liver PGF synthase. PGF synthase has at least two types of isozyme, and has the different biological role of each isozyme.Another structure-function study to be carried out involves prostaglandin(PG)F synthase. The enzyme is a dual function enzyme. The problem of structure-function relationship in this enzyme will be studied by variety of methods, including biochemical, molecular biological and protein chemical methods using X-ray analysis and NMR. Fourthermore, PGF synthase has at least two types of isozyme. The relationships of these isozymes will also be clarified by genomic study of PGF synthase.

1.牛肺前列腺素(PG)F合成酶是一种由323个氨基酸残基组成的蛋白质，分子量为36,666。该酶是一种双功能酶，在SWNE分子上不同的活性部位催化PGH_2还原为PGF_2和PGD_2为9a，11b-PGF_2。该酶至少由两个结构域组成，并且^&lt；195&gt；Pro与PGD_2.2结合部位的功能有关。PGF合成酶N端约50、200和280位氨基酸残基被PGD_2的衍生物修饰，这些氨基酸可能构成了PGD_2.3的活性部位。我们报道了在牛肝脏中发现了一种新型的PGF合成酶，该酶与抗PGF合成酶抗体有交叉反应，但其酶性质与肺PGF合成酶不同，我们克隆了在肺PGF合成酶一级结构中有3个氨基酸交换的基因克隆。该克隆表达的蛋白性质与肺PGF合酶基本相同，为不同类型的肝PGF合酶。前列腺素F合成酶至少有两种同工酶，每种同工酶具有不同的生物学作用。另一项结构-功能研究涉及前列腺素F合成酶。该酶是一种双功能酶。这种酶的结构-功能关系问题将通过多种方法进行研究，包括生化、分子生物学和蛋白质化学方法，包括X射线分析和核磁共振。此外，PGF合成酶至少有两种同工酶。这些同工酶之间的关系也将通过对PGF合成酶的基因组研究而得到澄清。