Control of plant enzyme activity by reversible protein phosphorylation
作者： Steven C. Huber , Joan L. Huber , Robert W. McMichael
DOI: 10.1016/S0074-7696(08)62086-0
关键词:
摘要: Publisher Summary Protein phosphorylation is considered one of the most studied posttranslational-modification mechanisms affecting protein structure and function. This chapter reviews regulation plant enzymes by phosphorylation. It focuses on known to be regulated reversible explores how this mechanism post-translational modification may serve coordinate flux through major metabolic pathways. Most phosphorylated are leaf proteins status many phosphoproteins altered in response light. Phosphorylation numerous chloroplast stromal can observed when intact spinach chloroplasts provided [32P]Pi light or extracts given [γ-32P] vitro. One enzyme that undergoes pyruvate Pi dikinase (PPDK). found highest activities leaves C4 species certain crassulacean acid metabolism (CAM) plants, where it plays an important role photosynthesis catalyzing regeneration phosphoenolpyruvate (PEP), which primary CO2 acceptor. The dark modulation PPDK activity mimicked vitro ADP-dependent inactivation a Pi-dependent activation.
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