Plastidial phosphoglucose isomerase undergoes thioredoxin-mediated redox modification without altering catalytic activity.

ABSTRACT: Thioredoxin (Trx)-mediated redox regulation is a posttranslational mechanism that controls enzyme activity by reversibly switching the oxidation/reduction states of Cys residues. In plant cells, numerous enzymes across diverse biological systems have been suggested as targets of redox regulation; however, a complete understanding is lacking. In this study, we report that phosphoglucose isomerase (PGI) in plastids represents a novel class of redox-sensitive enzymes. PGI catalyzes the reversible interconversion of fructose 6-phosphate and glucose 6-phosphate and operates at the branch point between the Calvin-Benson cycle and the starch synthesis pathway in plastids. Using an affinity chromatography-based method, we found that plastidial PGI physically interacts with Trx in a redox-dependent

SUBMITTER: Nishide S 

PROVIDER: S-EPMC12751066 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature