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With the increased incidence of tuberculosis (TB) caused by  Mycobacterium tuberculosis  there is an urgent need for new and better anti-tubercular drugs. N-succinyl- L , L -diaminopimelic acid desuccinylase (DapE) is a key enzyme in the succinylase pathway for the biosynthesis of meso-diaminopimelic acid (meso-DAP) and  L -lysine. DapE is a zinc containing metallohydrolase which hydrolyses N-succinyl  L , L  diaminopimelic acid ( L , L -NSDAP) to  L , L -diaminopimelic acid ( L , L -DAP) and succinate.  M. tuberculosis  DapE (MtDapE) was cloned, over-expressed and purified as an N-terminal hexahistidine ((His) 6 ) tagged fusion containing one zinc ion per DapE monomer. We redesigned the DAP synthetic pathway to generate  L , L -NSDAP and other  L , L -NSDAP derivatives and have characterised MtDapE with these substrates. In contrast to its other Gram negative homologues, the MtDapE was insensitive to inhibition by  L -captopril which we show is consistent with novel mycobacterial alterations in the binding site of this drug.

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Reconstruction of diaminopimelic acid biosynthesis allows characterisation of Mycobacterium tuberculosis N-succinyl-L,L-diaminopimelic acid desuccinylase