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.
Highlights
Sisi Gao, ab Huanting Liu, b Valerie de Crecy-Lagard, c Wen Zhu, d Nigel G
ForI is a pyridoxal 50-phosphate (PLP)-dependent enzyme from the biosynthetic pathway of the C-nucleoside antibiotic formycin
We report that ForI forms novel pyridoxamine 50-phosphate (PMP)–diketopiperazine derivatives following incubation with both D and L cycloserine
Summary
Sisi Gao, ab Huanting Liu, b Valerie de Crecy-Lagard, c Wen Zhu, d Nigel G. In each external aldimine complex, the atoms of the diketopiperazine adduct originating from PLP adopt the same positions as observed for the PMP structure.
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
