Recombinant E.coli acpS protein

The acpS gene encodes acyl carrier protein synthase (AcpS), a key enzyme involved in the post-translational modification of apo-acyl carrier protein (apo-ACP) to its active holo-ACP form. Holo-ACP plays an essential role in fatty acid biosynthesis across bacteria, plants, and some eukaryotes, serving as a cofactor for shuttling intermediates during fatty acid elongation. AcpS catalyzes the transfer of a 4'-phosphopantetheine (PPant) group from coenzyme A (CoA) to a conserved serine residue on apo-ACP, a critical activation step for functional participation in type II fatty acid synthase (FAS) systems.

Recombinant AcpS proteins are engineered through heterologous expression systems (e.g., E. coli) for structural and functional studies. Its crystal structure reveals a trimeric organization with conserved active sites, enabling substrate recognition and catalysis. Research on AcpS has gained attention due to its potential as a therapeutic target in pathogenic bacteria, as fatty acid biosynthesis is vital for bacterial membrane formation. Inhibitors of AcpS could lead to novel antibiotics, particularly against drug-resistant strains. Additionally, recombinant AcpS is utilized in metabolic engineering to optimize holo-ACP production for biosynthesis of fatty acid-derived biofuels, polyketides, and other high-value compounds. Studies also explore its role in polyunsaturated fatty acid (PUFA) synthesis in industrial microorganisms. The enzyme's stability, activity, and compatibility with other FAS components remain active research areas, driving advances in both basic enzymology and biotechnological applications.