Title of article :
Enzyme I: The Gateway to the Bacterial Phosphoenolpyruvate: Sugar Phosphotransferase System
Author/Authors :
Ginsburg، نويسنده , , Ann and Peterkofsky، نويسنده , , Alan، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2002
Abstract :
Regulatory aspects of the bacterial phosphoenolpyruvate (PEP):sugar phosphotransferase system (PTS) are reviewed. The structure and conformational stability of the first protein (enzyme I) of the PTS, as well as the requirement for enzyme I to dimerize for autophosphorylation by PEP in the presence of MgCl2 are discussed.
Keywords :
thermal unfolding , active-site mutations , Isothermal titration calorimetry , Differential scanning calorimetry , stability , Analytical ultracentrifugation , circular dichroism , enzyme I of the bacterial phosphoenolpyruvate:sugar phosphotransferase system (PTS) , phosphorylation , dimerization , domain interactions , sedimentation equilibrium , tryptophan fluorescence
Journal title :
Archives of Biochemistry and Biophysics
Journal title :
Archives of Biochemistry and Biophysics
