Enzyme I: The Gateway to the Bacterial Phosphoenolpyruvate: Sugar Phosphotransferase System

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...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Archives of Biochemistry and Biophysics 2002-01, Vol.397 (2), p.273-278
Hauptverfasser:	Ginsburg, Ann, Peterkofsky, Alan
Format:	Artikel
Sprache:	eng
Schlagworte:	active-site mutations analytical ultracentrifugation circular dichroism differential scanning calorimetry Dimerization domain interactions enzyme I of the bacterial phosphoenolpyruvate:sugar phosphotransferase system (PTS) Gene Expression Regulation, Enzymologic isothermal titration calorimetry Models, Biological Phosphoenolpyruvate Sugar Phosphotransferase System - metabolism Phosphorylation Phosphotransferases (Nitrogenous Group Acceptor) - metabolism Protein Denaturation Protein Structure, Tertiary sedimentation equilibrium stability thermal unfolding Thermodynamics tryptophan fluorescence
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Beschreibung
Zusammenfassung:	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.
ISSN:	0003-9861 1096-0384
DOI:	10.1006/abbi.2001.2603