Expression and interaction of AGPase subunits reveal functional enzyme complexes in barley.

ABSTRACT: In the starch biosynthetic pathway of Poaceae plants, ADP-glucose pyrophosphorylase (AGPase) serves as the rate-limiting enzyme that catalyzes the conversion of glucose-1-phosphate (G1P) and ATP to ADP-glucose, the immediate precursor for starch synthesis. Despite its fundamental role, the molecular characteristics and regulation of AGPase in barley (Hordeum vulgare L.) remain poorly understood. This study systematically investigated the expression dynamics during barley grain development and subunit interactions of AGPase in vitro. Our findings revealed distinct spatiotemporal expression patterns among AGPase, with preferential accumulation during late grain-filling stages. Co-immunoprecipitation coupled with mass spectrometry (Co-IP/MS) demonstrated specific physical interactions

SUBMITTER: Cheng Z 

PROVIDER: S-EPMC12571849 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature