PMP–diketopiperazine adducts form at the active site of a PLP dependent enzyme involved in formycin biosynthesis
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ForI is a PLP-dependent enzyme from the biosynthetic pathway of the C-nucleoside antibiotic formycin. Cycloserine is thought to inhibit PLP-dependent enzymes by irreversibly forming a PMP–isoxazole. We now report that ForI forms novel PMP–diketopiperazine derivatives following incubation with both d and l cycloserine. This unexpected result suggests chemical diversity in the chemistry of cycloserine inhibition.
Gao , S , Liu , H , de Crécy-Lagard , V , Zhu , W , Richards , N G J & Naismith , J H 2019 , ' PMP–diketopiperazine adducts form at the active site of a PLP dependent enzyme involved in formycin biosynthesis ' , Chemical Communications , vol. 55 , no. 96 , pp. 14502-14505 . https://doi.org/10.1039/C9CC06975E
Copyright © 2019 The Author(s). Open Access Article. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence.
DescriptionWe thank Mr ThomasWilliams for mass spectrometry, acquired using LCMS equipment funded by the EPSRC (EP/L027240/1). JHN is funded by the ERC (TNT-NCB 339367), NGJR by the BBSRC (BB/P018017/1) and VdCL by NIH (R01GM129793).
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