Abstract
Griseoviridin (GV) is an A-type streptogramin antibiotic displaying antimicrobial activity and acting synergistically with viridogrisein (VG). Bioinformatic analyses reveal SgvP as the sole cytochrome P450 enzyme in the GV/VG gene cluster. To explore the role of SgvP in the GV/VG pathway, we inactivated the sgvP gene. The resulting ΔsgvP mutant generated two new products: GV-1 and GV-2, both lacking the CS bridge. In trans complementation of the sgvP gene into the ΔsgvP mutant strain partially restores GV production. Feeding [1-(13) C]-labeled cysteine to the wild-type strain led to enrichment of C-7 in the GV scaffold, thus verifying that the CS bond in GV is formed through direct coupling of the free SH group provided by the side chain of cysteine. The above results highlight the significance of SgvP in CS bond formation in griseoviridin biosynthesis.
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.
