Poster Presentation The 42nd Lorne Conference on Protein Structure and Function 2017

Genetic and structural analysis of L,L-diaminopimelate aminotransferase (#256)

Anthony Weatherhead 1 , Renwick Dobson 1 2 , Andre Hudson 1
  1. Biomolecular Interaction Center, University of Canterbury, Christchurch, Canterbury, New Zealand
  2. Bio21 Institute, University of Melbourne, Melbourne, Victoria, Australia

Despite the urgent need for the development of novel antibiotics to combat the drastic rise in the number of antibiotic resistant bacteria, only a few novel antibiotics have been developed in recent times.  In pathogenic bacteria, such as Chlamydia trachomatis, diaminopimelate aminotransferase catalyses a specific reaction in the diaminopimelate/lysine anabolic pathway that is necessary for both cell wall peptidoglycan and amino acid protein synthesis.  We have identified the enzyme L,L-diaminopimelate aminotransferase (DapL) as a novel and attractive target for  narrow-spectrum antibiotic development given, 1)  its role in cell wall peptidoglycan biosynthesis; 2)  role in the biosynthesis of the amino acid lysine; and 3) its presence in certain bacterial lineages.  This project will work towards the development of antibiotics that are specific for DapL in pathogenic bacteria.