Open AccessRequirement for a Functional Respiration-Coupled D-Fructose Transport System for Induction of Phosphoenolpyruvate: D-Fructose Phosphotransferase Activity
Author(s) -
Ellen B. Wolfson,
Terry A. Krulwich
Publication year - 1974
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.71.5.1739
Subject(s) - pep group translocation , phosphoenolpyruvate carboxykinase , fructose , biochemistry , phosphotransferase , fructokinase , chemistry , permease , biology , enzyme , mutant , gene
Previous studies have shown thatArthrobacter pyridinolis can transport D-fructose or L-rhamnose using either a phosphoenolpyruvate:hexose phosphotransferase (phosphoenol pyruvate:protein phosphotransferase, EC 2.7.3.9) system or a respiration-coupled transport system which requires the presence of exogenous L-malate. A mutant, AP4374, which is deficient in the D-fructose-specific component of the respiration-coupled system can grow on L-rhamnose using the phosphotransferase system, but cannot grow on D-fructose at all. AP4374 fails to produce the inducible D-fructose-specific phosphotransferase components (enzyme II and factor III) when grown in the presence of D-fructose. These results indicate a requirement for a functional respiration-coupled transport system for induction of the phosphotransferase system. The results further suggest that sufficient free D-fructose (or D-fructose 6-phosphate derived from it) must be present inside the cell in order for induction of the phosphotransferase system to occur. The entry of sufficient fructose to cause induction of the phosphotransferase system cannot occur by facilitated diffusion in the absence of energy coupling.