PMP–diketopiperazine adducts form at the active site of a PLP dependent enzyme involved in formycin biosynthesis

Sisi Gao, Huanting Liu, Valérie de Crécy-Lagard, Wen Zhu, Nigel G. J. Richards, James H. Naismith

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)

Abstract

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.
Original languageEnglish
Pages (from-to)14502-14505
Number of pages4
JournalChemical Communications
Volume55
Issue number96
Early online date15 Nov 2019
DOIs
Publication statusPublished - 14 Dec 2019

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