Kobayashi Yuichiro, Takashima Yoshinori, Hashidzume Akihito, Yamaguchi Hiroyasu, Harada Akira
Department of Macromolecular Science, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Japan.
Project Research Center for Fundamental Sciences, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Japan.
Sci Rep. 2015 Nov 5;5:16254. doi: 10.1038/srep16254.
Enzymes play a vital role in catalysing almost all chemical reactions that occur in biological systems. Some enzymes must form complexes with non-protein molecules called cofactors to express catalytic activities. Although the control of catalytic reactions via apoenzyme-cofactor complexes has attracted significant attention, the reports have been limited to the microscale. Here, we report a system to express catalytic activity by adhesion of an apoenzyme gel and a cofactor gel. The apoenzyme and cofactor gels act as catalysts when they form a gel assembly, but they lose catalytic ability upon manual dissociation. We successfully construct a system with switchable catalytic activity via adhesion and separation of the apoenzyme gel with the cofactor gel. We expect that this methodology can be applied to regulate the functional activities of enzymes that bear cofactors in their active sites, such as the oxygen transport of haemoglobin or myoglobin and the electron transport of cytochromes.
酶在催化生物系统中几乎所有的化学反应中起着至关重要的作用。一些酶必须与称为辅因子的非蛋白质分子形成复合物才能表达催化活性。尽管通过脱辅酶 - 辅因子复合物对催化反应的控制已引起广泛关注,但相关报道仅限于微观尺度。在此,我们报道了一种通过脱辅酶凝胶和辅因子凝胶的粘附来表达催化活性的系统。脱辅酶凝胶和辅因子凝胶在形成凝胶组装体时充当催化剂,但人工解离后它们会失去催化能力。我们通过脱辅酶凝胶与辅因子凝胶的粘附和分离成功构建了一个具有可切换催化活性的系统。我们期望这种方法能够应用于调节在其活性位点带有辅因子的酶的功能活性,例如血红蛋白或肌红蛋白的氧运输以及细胞色素的电子运输。