Trans-Kingdom Enzyme Shared by Chlamydia and Plants for Synthesis of Diaminopimelate͞lysine
L,L-diaminopimelate aminotransferase, a trans-kingdom enzyme shared by Chlamydia and plants for synthesis of diaminopimelate͞lysine Andrea J. McCoy*, Nancy E. Adams*, Andre´O. Hudson†, Charles Gilvarg‡, Thomas Leustek†, and Anthony T. Maurelli*§ *Department of Microbiology and Immunology, F Edward He´bert School of Medicine, Uniformed Services University of the Health Sciences, 4301 Jones Bridge Road, Bethesda, MD 20814-4799; †Biotech Center and Department of Plant Biology and Pathology, Rutgers University, 59 Dudley Road, New Brunswick, NJ 08901-8520; and ‡Department of Molecular Biology, Princeton University, Princeton, NJ 08544 Communicated by Roy Curtiss, Arizona State University, Tempe, AZ, October 2, 2006 (received for review July 15, 2006) The synthesis of meso-diaminopimelic acid (m-DAP) in bacteria is we refer to the four-step synthesis of THDP as the upper m-DAP essential for both peptidoglycan and lysine biosynthesis. From synthesis pathway. From THDP, three variant pathways have genome sequencing data, it was unclear how bacteria of the been defined for m-DAP synthesis in the bacteria: the succin Chlamydiales order would synthesize m-DAP in the absence of ylase, acetylase, and dehydrogenase pathways. The succinylase dapD, dapC, and dapE, which are missing from the genome. Here, pathway uses succinylated intermediates and is the most widely we assessed the biochemical capacity of Chlamydia trachomatis distributed in bacteria. Genes encoding THDP succinyltrans- serovar L2 to synthesize m-DAP. Expression of the chlamydial asd, ferase (dapD) and N-succinyl-L,L-DAP desuccinylase (dapE) dapB, and dapF genes in the respective Escherichia coli m-DAP have been characterized, whereas two enzymes, DapC and auxotrophic mutants restored the mutants to DAP prototrophy.
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