Mobility of four structural regions drives isoform-specific properties of photoenzyme LPOR in plants.

ABSTRACT: Light-dependent protochlorophyllide oxidoreductase (LPOR) is a photocatalytic enzyme in the chlorophyll biosynthetic pathway that underwent duplications in angiosperms, resulting in the emergence of multiple isoforms across various plant species. The physiological roles of these LPOR homologs remained unclear, so we selected six plant species with different number of isoforms of the enzyme, having diverse phylogenetic backgrounds, and characterized their properties in vitro. Our findings revealed that these isoforms vary in their affinity for the reaction product, chlorophyllide (Chlide), as well as for NADPH under lipid-free conditions and in reaction mixtures supplemented with plant lipids. Additionally, we observed differences in their oligomerization behavior. Our experimental approach

SUBMITTER: Gabruk M 

PROVIDER: S-EPMC11930087 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature