Phosphorylation of aldose-6-phosphate reductase from Prunus persica leaves

Sugar-alcohols are major photosynthates in plants from the Rosaceae family. Expression of the gene encoding aldose-6-phosphate reductase (Ald6PRase), the critical enzyme for glucitol synthesis in rosaceous species, is regulated by physiological and environmental cues. Additionally, Ald6PRase is inhibited by small molecules (hexose-phosphates and inorganic orthophosphate) and oxidizing compounds. This work demonstrates that Ald6PRase from peach leaves is phosphorylated in planta at the N-terminus. We also show in vitro phosphorylation of recombinant Ald6PRase by a partially purified kinase extract from peach leaves containing Ca2+-dependent protein kinases (CDPKs). Moreover, phosphorylation of recombinant Ald6PRase was inhibited by hexose-phosphates, phosphoenolpyruvate and pyrophosphate. We further show that phosphorylation of recombinant Ald6PRase was maximal using recombinant CDPKs. Overall, our results suggest that phosphorylation could fine-tune the activity of Ald6PRase. •Aldose-6-phosphate reductase from peach leaves is phosphorylated in planta.•Dephosphorylation of aldose-6-phosphate reductase increased its enzymatic activity.•The recombinant enzyme was phosphorylated by a kinase extract from peach leaves.•Kinases from peach leaves are inhibited by hexose-phosphates.•The recombinant enzyme is preferentially phosphorylated by CDPKs.