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

doi:10.1039/C9CC06975E

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 journal › Article › peer-review

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 language	English
Pages (from-to)	14502-14505
Number of pages	4
Journal	Chemical Communications
Volume	55
Issue number	96
Early online date	15 Nov 2019
DOIs	https://doi.org/10.1039/C9CC06975E
Publication status	Published - 14 Dec 2019

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Gao_2019_CC_PLPdependent_CC
Copyright © 2019 The Author(s). Open Access Article. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence.
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Cite this

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

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.",

author = "Sisi Gao and Huanting Liu and \{de Cr{\'e}cy-Lagard\}, Val{\'e}rie and Wen Zhu and Richards, \{Nigel G. J.\} and Naismith, \{James H.\}",

note = "We 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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doi = "10.1039/C9CC06975E",

language = "English",

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T1 - PMP–diketopiperazine adducts form at the active site of a PLP dependent enzyme involved in formycin biosynthesis

AU - Gao, Sisi

AU - Liu, Huanting

AU - de Crécy-Lagard, Valérie

AU - Zhu, Wen

AU - Richards, Nigel G. J.

AU - Naismith, James H.

N1 - We 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).

PY - 2019/12/14

Y1 - 2019/12/14

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/85075807809

U2 - 10.1039/C9CC06975E

DO - 10.1039/C9CC06975E

M3 - Article

SN - 1359-7345

VL - 55

SP - 14502

EP - 14505

JO - Chemical Communications

JF - Chemical Communications

IS - 96

ER -

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

Abstract

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