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

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...

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Detalles Bibliográficos
Autores principales: Gao, Sisi, Liu, Huanting, de Crécy-Lagard, Valérie, Zhu, Wen, Richards, Nigel G. J., Naismith, James H.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2019
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6927412/
https://www.ncbi.nlm.nih.gov/pubmed/31730149
http://dx.doi.org/10.1039/c9cc06975e
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author Gao, Sisi
Liu, Huanting
de Crécy-Lagard, Valérie
Zhu, Wen
Richards, Nigel G. J.
Naismith, James H.
author_facet Gao, Sisi
Liu, Huanting
de Crécy-Lagard, Valérie
Zhu, Wen
Richards, Nigel G. J.
Naismith, James H.
author_sort Gao, Sisi
collection PubMed
description 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.
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spelling pubmed-69274122020-01-30 PMP–diketopiperazine adducts form at the active site of a PLP dependent enzyme involved in formycin biosynthesis Gao, Sisi Liu, Huanting de Crécy-Lagard, Valérie Zhu, Wen Richards, Nigel G. J. Naismith, James H. Chem Commun (Camb) Chemistry 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. Royal Society of Chemistry 2019-12-14 2019-11-15 /pmc/articles/PMC6927412/ /pubmed/31730149 http://dx.doi.org/10.1039/c9cc06975e Text en This journal is © The Royal Society of Chemistry 2019 http://creativecommons.org/licenses/by/3.0/ This article is freely available. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence (CC BY 3.0)
spellingShingle Chemistry
Gao, Sisi
Liu, Huanting
de Crécy-Lagard, Valérie
Zhu, Wen
Richards, Nigel G. J.
Naismith, James H.
PMP–diketopiperazine adducts form at the active site of a PLP dependent enzyme involved in formycin biosynthesis
title PMP–diketopiperazine adducts form at the active site of a PLP dependent enzyme involved in formycin biosynthesis
title_full PMP–diketopiperazine adducts form at the active site of a PLP dependent enzyme involved in formycin biosynthesis
title_fullStr PMP–diketopiperazine adducts form at the active site of a PLP dependent enzyme involved in formycin biosynthesis
title_full_unstemmed PMP–diketopiperazine adducts form at the active site of a PLP dependent enzyme involved in formycin biosynthesis
title_short PMP–diketopiperazine adducts form at the active site of a PLP dependent enzyme involved in formycin biosynthesis
title_sort pmp–diketopiperazine adducts form at the active site of a plp dependent enzyme involved in formycin biosynthesis
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6927412/
https://www.ncbi.nlm.nih.gov/pubmed/31730149
http://dx.doi.org/10.1039/c9cc06975e
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