Abstract
YggS is a member of the pyridoxal 5′-phosphate (PLP)-binding protein family (COG0325), which is conserved across domains and has been implicated in maintaining the homeostasis of B6 vitamers. Vu et al. (e00383-20) show that strains devoid of YggS accumulate PLP in the growth medium. By replacing the native pathway for de novo PLP synthesis in Salmonella enterica with a heterologous PLP synthase, they show an epistatic interaction between YggS and PdxH, the pyridoxine 5′-phosphate (PNP)/pyridoxamine 5′-phosphate (PMP) oxidase. Together, YggS and PdxH may modulate the cycling of PLP→PMP→PLP.
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.
