Photorhabdus luminescens is a Gram-negative bacterium known for its symbiotic relationship with nematodes and its pathogenicity towards a broad spectrum of insects . Specifically, Photorhabdus luminescens subsp. laumondii strain TT01, is a symbiont of the nematode Heterorhabditis bacteriophora . Within this bacterium exists an enzyme called 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase, commonly referred to as dapD . This enzyme is a crucial component in the lysine biosynthesis pathway . The recombinant form of this enzyme is produced in a host organism, often Escherichia coli, for research and industrial applications .
DapD is an N-succinyltransferase that participates in the synthesis of lysine, an essential amino acid . P. luminescens utilizes a variety of virulence factors to kill insects, and the metabolic pathways, including lysine synthesis, are vital for its survival and pathogenicity .
The production of recombinant dapD typically involves cloning the dapD gene from Photorhabdus luminescens subsp. laumondii into an expression vector and transforming it into E. coli . The recombinant protein is then expressed in E. coli and purified using affinity chromatography, often employing a His tag .
Recombinant dapD can be utilized in various research applications:
Enzyme Activity Assays: To study the enzymatic activity and kinetics of dapD .
Structural Studies: For determining the crystal structure of dapD and its complexes with substrates or inhibitors .
Drug Discovery: As a target for developing new antimicrobial agents, considering the importance of lysine biosynthesis in bacterial survival .
KEGG: plu:plu0669
STRING: 243265.plu0669