Abstract:
ATP (adenosine triphosphate) is a vital energy source for living organisms, and its biosynthesis and precise concentration regulation often depend on macromolecular machinery composed of protein complexes or complicated multidomain proteins. We have identified a single-domain protein HK853CA derived from bacterial histidine kinases (HK) that can catalyze ATP synthesis efficiently. Here, we explored the reaction mechanism and multiple factors that influence this catalysis through a combination of experimental techniques and molecular simulations. Moreover, we optimized its enzymatic activity and applied it as an ATP replenishment machinery to other ATP-dependent systems. Our results broaden the understanding of ATP biosynthesis and show that the single CA domain can be applied as a new biomolecular catalyst used for ATP supply.
摘要:
ATP(三磷酸腺苷)是生物体的重要能源,其生物合成和精确的浓度调节通常取决于由蛋白质复合物或复杂的多结构域蛋白质组成的大分子机制。我们已经鉴定了源自细菌组氨酸激酶(HK)的单结构域蛋白HK853CA,可以有效催化ATP合成。这里,我们通过实验技术和分子模拟相结合,探索了影响这种催化作用的反应机理和多种因素。此外,我们优化了其酶活性,并将其作为ATP补充机制应用于其他ATP依赖性系统。我们的结果拓宽了对ATP生物合成的理解,并表明单个CA结构域可用作用于ATP供应的新型生物分子催化剂。