Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) mediates the fixation of atmospheric CO2 in photosynthesis by catalyzing the carboxylation of the 5-carbon sugar ribulose-1,5-bisphosphate (RuBP). Rubisco is a remarkably inefficient enzyme, fixing only 2-10 CO2 molecules per second. Efforts to increase crop yields by bioengineering Rubisco remain unsuccessful, owing in part to the complex cellular machinery required for Rubisco biogenesis and metabolic maintenance. The large subunit of Rubisco requires the chaperonin system for folding, and recent studies have shown that assembly of hexadecameric Rubisco is mediated by specific assembly chaperones. Moreover, Rubisco function can be inhibited by a range of sugar-phosphate ligands, including RuBP. Metabolic repair depends on remodeling of Rubisco by the ATP-dependent Rubisco activase and hydrolysis of inhibitory sugar phosphates by specific phosphatases. Here, we review our present understanding of the structure and function of these auxiliary factors and their utilization in efforts to engineer more catalytically efficient Rubisco enzymes.

中文翻译：

---

Rubisco 的生物发生和代谢维持

核酮糖-1,5-二磷酸羧化酶/加氧酶 (Rubisco) 通过催化 5-碳糖核酮糖-1,5-二磷酸 (RuBP) 的羧化，介导光合作用中大气 CO2 的固定。Rubisco 是一种非常低效的酶，每秒只能固定 2-10 个 CO2 分子。通过生物工程 Rubisco 提高作物产量的努力仍未成功，部分原因是 Rubisco 生物发生和代谢维持所需的复杂细胞机制。Rubisco 的大亚基需要伴侣蛋白系统进行折叠，最近的研究表明，十六聚体 Rubisco 的组装是由特定的装配伴侣蛋白介导的。此外，Rubisco 功能可以被一系列的糖磷酸配体抑制，包括 RuBP。代谢修复取决于 ATP 依赖性 Rubisco 激活酶对 Rubisco 的重塑和特定磷酸酶对抑制性糖磷酸盐的水解。在这里，我们回顾了我们目前对这些辅助因子的结构和功能的理解，以及它们在努力设计催化效率更高的 Rubisco 酶中的应用。