Journal article
Characterisation of dihydrodipicolinate synthase (DHDPS) from Bacillus anthracis
LJ Domigan, SW Scally, MJ Fogg, CA Hutton, MA Perugini, RCJ Dobson, AC Muscroft-Taylor, JA Gerrard, SRA Devenish
Biochimica Et Biophysica Acta Proteins and Proteomics | Published : 2009
Abstract
Bacillus anthracis is a Gram-positive spore-forming bacterium that is the causative agent of anthrax disease. The use of anthrax as a bioweapon has increased pressure for the development of an effective treatment. Dihydrodipicolinate synthase (DHDPS) catalyses the first committed step in the biosynthetic pathway yielding two essential bacterial metabolites, meso-diaminopimelate (DAP) and (S)-lysine. DHDPS is therefore a potential antibiotic target, as microbes require either lysine or DAP as a component of the cell wall. This paper is the first biochemical description of DHDPS from B. anthracis. Enzyme kinetic analyses, isothermal titration calorimetry (ITC), mass spectrometry and differenti..
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Awarded by Defense Threat Reduction Agency
Funding Acknowledgements
We would like to acknowledge the Defense Threat Reduction Agency (DTRA) (DTRA Project ID AB07CBT004) and the Australian Research Council for providing an Australian Postdoctoral Fellowship for MAP. ACMT is grateful to the Growth and Innovation Pilot Initiative for postdoctoral funding, and SRAD thanks the Foundation for Research, Science and Technology for postdoctoral funding (contract UOCX0603). RCJD acknowledges the C.R. Roper bequest for support. MJF is currently funded by the European Commission as part of BaSysBio (Bacillus Systems Biology), contract no. LSHG-CT-2006037469 under the 6th framework program "Priority 1 Life Sciences, Genomics and Biotechnology for Health". The authors thank Jackie Healy for voluptuous technical support, Marie Squire for mass spectrometry, and Grant Pearce for formidable discussion.