|
|||||
|
|
Enzyme I: the gateway to the bacterial phosphoenolpyruvate:sugar phosphotransferase system. |
|
| Authors: | Ann Ginsburg Alan Peterkofsky |
| Institution: | Section of Protein Chemistry, Laboratory of Biochemistry, National Heart, Blood and Lung Institute, NIH, Bethesda, MD 20892, USA. aog@cu.nih.gov |
| 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: | enzyme I of the bacterial phosphoenolpyruvate:sugar phosphotransferase system (PTS) phosphorylation dimerization domain interactions active-site mutations thermal unfolding stability differential scanning calorimetry isothermal titration calorimetry sedimentation equilibrium analytical ultracentrifugation tryptophan fluorescence circular dichroism |
| 本文献已被 ScienceDirect 等数据库收录！ | |