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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. and Naismith, James H. 2019. PMP-diketopiperazine adducts form at the active site of a PLP dependent enzyme involved in formycin biosynthesis. Chemical Communications 55 (96) , pp. 14502-14505. 10.1039/C9CC06975E

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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.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Chemistry
Publisher: Royal Society of Chemistry
ISSN: 1359-7345
Funders: BBSRC
Date of First Compliant Deposit: 3 January 2020
Date of Acceptance: 16 October 2019
Last Modified: 06 Jan 2020 12:30
URI: http://orca-mwe.cf.ac.uk/id/eprint/128171

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