The mechanism of Rubisco activase: Insights from studies of the properties and structure of the enzyme

被引:205
作者
Salvucci, ME [1 ]
Ogren, WL [1 ]
机构
[1] PHOTOSYNTH RES UNIT, URBANA, IL 61801 USA
关键词
chaperone chloroplast; enzyme regulation; photosynthesis; protein-protein interaction; ribulose-1,5-bisphosphate carboxylase/oxygenase;
D O I
10.1007/BF00017748
中图分类号
Q94 [植物学];
学科分类号
071001 [植物学];
摘要
Rubisco, the primary carboxylating enzyme in photosynthesis, must be activated to catalyze CO2 fixation. The concept of an 'activase', a specific protein for activating Rubisco, was first introduced in 1985 based largely on biochemical and genetic studies of a high CO2-requiring mutant of Arabidopsis (Salvucci et al. (1985) Photosynth Res 7: 193-201). Over the past ten years, details about the occurrence, structure, and properties of Rubisco activase have been elucidated. However, the mechanism of action of Rubisco activase remains elusive. This review discusses the need for and function of Rubisco activase and summarizes information about the properties and structure of Rubisco activase. The information is evaluated in the context of the mechanism of Rubisco activase.
引用
收藏
页码:1 / 11
页数:11
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