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核酮糖-1,5-二磷酸羧化酶/加氧酶激活酶的分子机制:动态组装与核酮糖-1,5-二磷酸羧化酶重塑

Molecular mechanism of Rubisco activase: Dynamic assembly and Rubisco remodeling.

作者信息

Waheeda Kazi, Kitchel Heidi, Wang Quan, Chiu Po-Lin

机构信息

School of Molecular Sciences, Arizona State University, Tempe, AZ, United States.

Biodesign Center for Applied Structural Discovery, Arizona State University, Tempe, AZ, United States.

出版信息

Front Mol Biosci. 2023 Feb 10;10:1125922. doi: 10.3389/fmolb.2023.1125922. eCollection 2023.

Abstract

Ribulose-1,5-bisphosphate (RuBP) carboxylase-oxygenase (Rubisco) enzyme is the limiting step of photosynthetic carbon fixation, and its activation is regulated by its co-evolved chaperone, Rubisco activase (Rca). Rca removes the intrinsic sugar phosphate inhibitors occupying the Rubisco active site, allowing RuBP to split into two 3-phosphoglycerate (3PGA) molecules. This review summarizes the evolution, structure, and function of Rca and describes the recent findings regarding the mechanistic model of Rubisco activation by Rca. New knowledge in these areas can significantly enhance crop engineering techniques used to improve crop productivity.

摘要

1,5-二磷酸核酮糖羧化酶/加氧酶(Rubisco)是光合碳固定的限速步骤,其激活受共同进化的伴侣蛋白Rubisco活化酶(Rca)调控。Rca去除占据Rubisco活性位点的内在磷酸糖抑制剂,使1,5-二磷酸核酮糖(RuBP)裂解为两个3-磷酸甘油酸(3PGA)分子。本文综述了Rca的进化、结构和功能,并描述了关于Rca激活Rubisco的机制模型的最新研究结果。这些领域的新知识可以显著提升用于提高作物生产力的作物工程技术。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4b47/9951593/852cf119da98/fmolb-10-1125922-g001.jpg

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