Jump to main content
Jump to site search

Issue 96, 2019
Previous Article Next Article

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

Author affiliations

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.

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

Back to tab navigation

Supplementary files

Article information


Submitted
06 Sep 2019
Accepted
16 Oct 2019
First published
15 Nov 2019

This article is Open Access

Chem. Commun., 2019,55, 14502-14505
Article type
Communication

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

S. Gao, H. Liu, V. de Crécy-Lagard, W. Zhu, N. G. J. Richards and J. H. Naismith, Chem. Commun., 2019, 55, 14502
DOI: 10.1039/C9CC06975E

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. Material from this article can be used in other publications provided that the correct acknowledgement is given with the reproduced material.

Reproduced material should be attributed as follows:

  • For reproduction of material from NJC:
    [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the Centre National de la Recherche Scientifique (CNRS) and the RSC.
  • For reproduction of material from PCCP:
    [Original citation] - Published by the PCCP Owner Societies.
  • For reproduction of material from PPS:
    [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the European Society for Photobiology, the European Photochemistry Association, and RSC.
  • For reproduction of material from all other RSC journals:
    [Original citation] - Published by The Royal Society of Chemistry.

Information about reproducing material from RSC articles with different licences is available on our Permission Requests page.


Social activity

Search articles by author

Spotlight

Advertisements