Signal discrimination analyses based on the domain structure of soluble guanylate cyclase

基于可溶性鸟苷酸环化酶结构域结构的信号判别分析

• 批准号: 19510224
• 负责人: MAKINO Ryu
• 金额: $ 2.66万
• 依托单位: Rikkyo University
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for Scientific Research (C)
• 财政年份: 2007
• 资助国家: 日本
• 起止时间: 2007 至 2009
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-19510224/
• 关键词: 活性発現の分子機構; 可溶性グアニル酸シクラーゼ; ヌクレオチド; 低分子シグナル分子; ヘム鉄; アジド; 5配位高スピン型; YC-1; 一酸化窒素(NO); EXAFS; alky1 isocyanide; 酸素化型ヘム; ガス状シグナル分子

We have revealed that there were two kinds of nucleotide binding sites, a catalytic and a pseudo-nucleotide sites in soluble guanylate cyclase. When carbon monoxide combined to the enzymic heme, the binding of YC-1 to the pseudo-nucleotide binding site increased the affinity of a nucleotide for the pseudo nucleotide binding site, through interaction between two binding sites. Furthermore, we have first confirmed the formation of the oxygenated form of the enzyme, which was stable under frozen conditions. The formation of the oxygenated form was noted to be regulated by YC-1 binding, and also was suggested to be governed by the deformation of the heme iron from the heme plane, based on the EXAFS analyses.

我们发现在可溶性鸟苷环化酶中存在两种核苷酸结合部位，一种是催化部位，一种是假核苷酸部位。当一氧化碳与酶促血红素结合时，YC-1与假核苷酸结合部位的结合通过两个结合部位之间的相互作用增加了核苷酸对假核苷酸结合部位的亲和力。此外，我们首次证实了该酶的氧化形式的形成，该形式在冷冻条件下是稳定的。EXAFS分析表明，含氧形式的形成受YC-1结合的调节，也可能是由血红素平面上的血红素铁的变形所控制。

项目成果

可溶性グアニル酸シクラーゼにおけるヌクレオチド結合部位の役割

可溶性鸟苷酸环化酶中核苷酸结合位点的作用

• 发表时间: 2007
• 作者: 牧野龍;矢澤真介;堀洋
• 通讯作者: 堀洋