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dc.contributor.authorGao, Sisi
dc.contributor.authorLiu, Huanting
dc.contributor.authorde Crécy-Lagard, Valérie
dc.contributor.authorZhu, Wen
dc.contributor.authorRichards, Nigel G. J.
dc.contributor.authorNaismith, James H.
dc.identifier.citationGao , S , Liu , H , de Crécy-Lagard , V , Zhu , W , Richards , N G J & Naismith , J H 2019 , ' PMP–diketopiperazine adducts form at the active site of a PLP dependent enzyme involved in formycin biosynthesis ' , Chemical Communications , vol. 55 , no. 96 , pp. 14502-14505 .
dc.identifier.otherPURE: 264469784
dc.identifier.otherPURE UUID: a762f10e-55fe-469a-9032-609a1e3e0f85
dc.identifier.otherBibtex: C9CC06975E
dc.identifier.otherScopus: 85075807809
dc.identifier.otherWOS: 000499480200021
dc.descriptionWe 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).en
dc.description.abstractForI 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.
dc.relation.ispartofChemical Communicationsen
dc.rightsCopyright © 2019 The Author(s). Open Access Article. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence.en
dc.subjectQD Chemistryen
dc.titlePMP–diketopiperazine adducts form at the active site of a PLP dependent enzyme involved in formycin biosynthesisen
dc.typeJournal articleen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews.School of Chemistryen
dc.contributor.institutionUniversity of St Andrews.Biomedical Sciences Research Complexen
dc.description.statusPeer revieweden

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