2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP succinyltransferase): THDP N-succinyltransferase catalyzes the conversion of tetrahydrodipicolinate and succinyl-CoA to N-succinyltetrahydrodipicolinate and CoA. It is the committed step in the succinylase pathway by which bacteria synthesize L-lysine and meso-diaminopimelate, a component of peptidoglycan. The enzyme is homotrimeric and each subunit contains an N-terminal region with alpha helices and hairpin loops, as well as a C-terminal region with a left-handed parallel alpha-helix (LbH) structural motif encoded by hexapeptide repeat motifs.
Comment:Active THP succinyltransferase is trimeric, with active sites located at the interface between two LbH subunits. The trimer structure contains three active sites and each subunit contributes to two active sites via residues located on two surfaces.
Comment:The structure evidence shows only the interaction of CoA and substrate to one interacting LbH subunit/surface.
Structure:1KGQ_A; Mycobacterium bovis THP succinyltransferase active site surface A binds the ligands, succinamide-CoA and L-2-Aminopimelate; defined at 3.5A contacts. - View structure with Cn3D
Lu S et al.(2020). "CDD/SPARCLE: the conserved domain database in 2020.",