Serratia marcescens is a human pathogen often involved in hospital acquired infections. The enzyme tetrahydrodipicolinate N-succinyltransferase (DapD) from this source catalyzes succinyl transfer to an amine using the cofactor succinyl-CoA and converting tetrahydrodipicolinate (THDP) into N-succinyl-L-2-amino-6-oxopimelate. This is the committed metabolic step in the biosynthesis of L-lysine in bacteria. The immediate precursor to lysine is meso-diaminopimelate, an essential component to the peptidoglycan cell wall. Since lysine is an essential amino acid to humans, DapD is a target for novel antibiotic therapies. While extensive structural information is available for the enzyme, kinetic and mechanistic information is lacking. For the first time, DapD from S. marcescans has been cloned into a pET15b expression vector, overexpressed in E. coli host cells and purified. Initial kinetic characterization suggests a sequential mechanism for the order of substrate binding and product release.

Cloning, overexpression and purification of tetrahydrodipicolinate N-succinyltransferase (DapD) from Serratia marcescans

255th National Meeting (2018)

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