Discovery of proteinaceous N-modification in lysine biosynthesis of Thermus thermophilus

摘要: Although the latter portion of lysine biosynthesis, conversion α-aminoadipate (AAA) to lysine, in Thermus thermophilus is similar arginine enzymes homologous ArgA and ArgJ are absent from pathway. Because known modify amino group glutamate avoid intramolecular cyclization intermediates, their absence suggests that pathway includes an alternative N-modification system. We reconstituted AAA found modified by attachment γ-carboxyl C-terminal Glu54 a small protein, LysW; side chain converted lysyl while still attached subsequently liberated LysW-lysine fusion. The fact biosynthetic recognize acidic globular domain LysW indicates acts as carrier protein or scaffold for enzymes. This study thus reveals previously unknown function primary metabolism.