浙江农业学报 ›› 2026, Vol. 38 ›› Issue (7): 1493-1506.DOI: 10.3969/j.issn.1004-1524.20250424

• 综述 • 上一篇    下一篇

淀粉磷酸化酶的双向调控机制及其在植物淀粉代谢与抗逆性中的作用

王雨(), 朱芳漪, 张冲, 逄洪波, 贺海升, 张颖*()   

  1. 沈阳师范大学 生命科学学院, 辽宁 沈阳 110034
  • 收稿日期:2025-06-09 出版日期:2026-07-25 发布日期:2026-08-20
  • 作者简介:王雨,研究方向为植物逆境分子生物学。E-mail:18341552627@163.com
  • 通讯作者: *张颖,E-mail: f5944@163.com
  • 基金资助:
    辽宁省应用基础研究项目(2022JH2/101300179);辽宁省基本科研项目(LJ232410166068);辽宁省基本科研项目(LJ232410166084);大学生创新创业项目;辽宁省属本科高校基本科研业务费创新团队支持计划专项(LJ202410166052);国家留学基金委项目(202208210182)

Bidirectional regulatory mechanisms of starch phosphorylase and their roles in plant starch metabolism and stress resistance

WANG Yu(), ZHU Fangyi, ZHANG Chong, PANG Hongbo, HE Haisheng, ZHANG Ying*()   

  1. College of Life Sciences, Shenyang Normal University, Shenyang 110034, China
  • Received:2025-06-09 Published:2026-07-25 Online:2026-08-20

摘要:

淀粉磷酸化酶(starch phosphorylase, SP)是植物淀粉代谢中的关键酶,通过可逆磷酸解反应双向调控淀粉的合成与降解。高等植物中质体型磷酸化酶(plastidial phosphorylase, PHO1)和胞质型磷酸化酶(cytosolic phosphorylase, PHO2)在底物特异性与功能上存在显著差异,其中PHO1主要参与淀粉合成,而PHO2则与麦芽糖代谢相关。SP主要由N末端、调节域、L80结构域与催化域组成,L80结构域可通过磷酸化和蛋白酶体降解动态调控酶活性。催化机制中,PHO1偏好支链淀粉合成,PHO2则倾向于磷酸解降解;葡萄糖-1-磷酸(glucose-1-phosphate, Glc-1-P)与无机磷酸(inorganic phosphate, Pi)等代谢物的浓度和金属离子,通过影响反应方向与活性协同调控代谢平衡。SP具有多重生理功能,不仅通过延长葡聚糖链、分解淀粉直接参与淀粉代谢,还在光合作用中调节Pi稳态,并通过多酶复合体优化碳分配,增强植物抗逆性。本文系统综述了SP作为植物淀粉代谢核心枢纽调节器的双向调控机制及其在协调碳流分配、维持Pi稳态和增强非生物胁迫抗性中的核心作用,强调了其通过形成动态多酶复合体实现功能可塑性以适应环境变化的独特机制。然而目前关于SP多酶复合体的空间构象与动态组装调控网络,及其在不同物种间功能分化的分子演化机制仍未完全阐明。未来研究需结合结构生物学与多组学技术,深入挖掘SP在碳-磷代谢交叉调控中的非经典途径,并应用基因编辑技术定向优化SP活性或复合体组装,从而为靶向改良作物淀粉代谢效率、产量与抗逆性提供新视角和潜在靶点。

关键词: 淀粉磷酸化酶, 淀粉代谢, 可逆磷酸解, 抗逆性, 复合体

Abstract:

Starch phosphorylase (SP) is a key enzyme in plant starch metabolism, bidirectionally regulating starch synthesis and degradation through reversible phosphorolysis. Plastidial phosphorylase (PHO1) and cytosolic phosphorylase (PHO2) in higher plants exhibit significant differences in substrate specificity and function. PHO1 is primarily involved in starch synthesis, while PHO2 is associated with maltose metabolism. SP is mainly composed of an N-terminal region, a regulatory domain, an L80 domain, and a catalytic domain. The L80 domain can dynamically regulate enzyme activity through phosphorylation and proteasome-mediated degradation. Regarding the catalytic mechanism, PHO1 prefers amylopectin synthesis, whereas PHO2 tends to catalyze phosphorolytic degradation. The concentrations of metabolites such as glucose-1-phosphate (Glc-1-P) and inorganic phosphate (Pi), as well as metal ions, synergistically regulate metabolic balance by influencing reaction direction and enzyme activity. SP possesses multiple physiological functions. It not only directly participates in starch metabolism by elongating glucan chains and degrading starch but also regulates Pi homeostasis in photosynthesis and optimizes carbon allocation through multi-enzyme complexes to enhance plant stress resistance. This paper systematically reviews the bidirectional regulatory mechanism of SP as a core hub regulator in plant starch metabolism and its central role in coordinating carbon flow distribution, maintaining Pi homeostasis, and improving abiotic stress tolerance. It highlights SP's unique mechanism of achieving functional plasticity via the formation of dynamic multi-enzyme complexes to adapt to environmental changes. However, the spatial conformation and dynamic assembly regulatory networks of SP multi-enzyme complexes, as well as the molecular evolutionary mechanisms underlying its functional differentiation across species, remain incompletely elucidated. Future research should integrate structural biology and multi-omics technologies to explore the non-canonical pathways of SP in the cross-regulation of carbon and phosphorus metabolism, and apply gene-editing techniques for the targeted optimization of SP activity or complex assembly, thus offering new perspectives and potential targets for the targeted improvement of crop starch metabolism efficiency, yield and stress resistance.

Key words: starch phosphorylase, starch metabolism, reversible phosphordysis, stress resistance, complex

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