Research Advances in Plant Pyruvate Kinase

Pyruvate kinase (PK) is the terminal rate-limiting enzyme of glycolysis and occupies a central position in plant energy metabolism and carbon skeleton allocation. Plant PK isoenzymes comprise the cytosolic pyruvate kinase (PKc) and the plastidic pyruvate kinase (PKp), which differ markedly in gene origin, protein structure, subcellular localization, and physiological function, exhibiting independent evolutionary histories and functional diversification. Recent studies have revealed that PKc possesses dynamic subcellular distribution, allowing it to shuttle among the cytosol, mitochondria, and nucleus, where it participates in stress responses and epigenetic regulation through protein–protein interactions. PKp is localized to plastids and connects carbon metabolism with lipid biosynthesis and the methylerythritol phosphate (MEP) pathway by supplying pyruvate, thereby playing critical roles in seed development and oil accumulation. This review comprehensively summarizes recent advances in plant PKc and PKp concerning protein structure and subunit composition, tissue-specific expression, subcellular localization, protein interaction networks, activity regulation, and their effects on plant growth, development, and stress responses. In addition, phylogenetic tree, motif, and domain analyses of pyruvate kinase genes from Oryza sativa (rice), Glycine max (soybean), Gossypium hirsutum (cotton), Solanum tuberosum (potato), Arachis hypogaea (peanut), and Arabidopsis thaliana, as well as promoter cis-element analyses, are performed. This review aims to provide theoretical references for crop quality improvement and stress-resilient breeding.