What is it about?

Almost all bacteria, including Chlamydia, make a cell wall composed of unusual chemical components. These building blocks are not found in humans so enzymes used to construct the cell wall are excellent targets for antibiotics, like penicillin. One unique building block is D-glutamate. This study discovered that Chlamydia uses an unexpected enzyme, diaminopimelate epimerase (DapF), to synthesize D-glutamate. Chlamydial DapF is also used to make diaminopimelate, another component of the cell wall. Its dual function suggests that DapF is a primordial enzyme, a vestige of early microbial life on this planet

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Why is it important?

While this study has important implications for the evolution of bacterial pathogens, it also reveals a novel 2 for 1 target for drug development. A drug that can inhibit DapF function would cripple Chlamydia cell wall synthesis by blocking synthesis of two essential cell wall components. The absence of any human enzyme similar to DapF would also make the drug selective for targeting Chlamydia without harming the host.

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This page is a summary of: Chlamydia trachomatis dapF Encodes a Bifunctional Enzyme Capable of Both D-Glutamate Racemase and Diaminopimelate Epimerase Activities, mBio, April 2018, ASM Journals,
DOI: 10.1128/mbio.00204-18.
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