Structural highlights
Function
A0A6I8WFW1_9ACTN
Publication Abstract from PubMed
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.
PMP-diketopiperazine adducts form at the active site of a PLP dependent enzyme involved in formycin biosynthesis.,Gao S, Liu H, de Crecy-Lagard V, Zhu W, Richards NGJ, Naismith JH Chem Commun (Camb). 2019 Nov 28;55(96):14502-14505. doi: 10.1039/c9cc06975e. PMID:31730149[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gao S, Liu H, de Crécy-Lagard V, Zhu W, Richards NGJ, Naismith JH. PMP-diketopiperazine adducts form at the active site of a PLP dependent enzyme involved in formycin biosynthesis. Chem Commun (Camb). 2019 Nov 28;55(96):14502-14505. PMID:31730149 doi:10.1039/c9cc06975e
