Abstract
In Enterobacteriaceae the nonphosphorylated form of IIAGlc of the phosphoenolpyruvate-dependent phosphotransferase system (PTS) can inhibit the uptake and subsequent metabolism of glycerol and maltose by binding to, and inhibiting, glycerol kinase and the MalK protein of the maltose transport system, respectively. In this report we show that the IIAGlc-like domain of the membrane-bound IIN-acetylglucosamine (IINag) of the PTS can replace IIAGlc in a Salmonella typhimurium crr mutant strain that lacks all soluble IIAGlc. The inhibition was most severe in cells which were partially induced for the glycerol or maltose uptake systems. The Streptococcus thermophilus lactose transporter LacS, which also contains a IIAGlc-like domain, could not replace IIAGlc. Neither IINag nor LacS could replace IIAGlc in activation of adenylate cyclase.
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.
