Work

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

Year: 2019

Type: article

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.

Source: Chemical Communications

DOI: 10.1039/c9cc06975e

Authors: Sisi Gao, Huanting Liu, Valérie de Crécy-Lagard, Wen Zhu, Nigel G. J. Richards, James H. Naismith

Institutions: University of St Andrews, Research Complex at Harwell, University of Florida, QB3, University of California System, Institute for Quantitative Biosciences, The University of Tokyo, University of California, Berkeley, Foundation for Applied Molecular Evolution, Cardiff University, Sichuan University, University of Oxford, Rosalind Franklin Institute, State Key Laboratory of Biotherapy

Language: English

Topic: Microbial Natural Products and Biosynthesis

Subfield: Pharmacology

Field: Medicine

Domain: Health Sciences

Open Access status: hybrid

Funders: Sichuan University, National Institutes of Health, Engineering and Physical Sciences Research Council, Biotechnology and Biological Sciences Research Council, National Institute of General Medical Sciences, H2020 European Research Council

Awards: Computational Studies of AEGIS Molecular Components, Rosalind Franklin Institute : Establishment Phase, Core Capability for Chemistry Research: Cardiff School of Chemistry Mass Spectrometry, Pyridoxal 5'-phosphate homeostasis in Escherichia coli, G6080725989

OpenAlex ID: W2987080839

FWCI: 1.081

Cites: 40

Cited by: 14

Related to: 10