EI of the Phosphotransferase System of Escherichia coli: Mathematical Modeling Approach to Analysis of Its Kinetic Properties. (8th February 2011)

• Record Type: Journal Article
• Authors: Karelina, T. A.; Ma, H.; Goryanin, I.; Demin, O. V.
• Other Names: Burghardt Thomas P. Academic Editor.
• Is Part Of: Journal of biophysics. Volume 2011(2011)
• Publication Date: 2011-02-08
• Subjects: Biophysics -- Periodicals; Biophysics; Biophysical Phenomena; Biophysics; Periodical; Periodicals; Electronic journals; Fulltext; Internet Resources; Periodicals; 571.4
• DOI: 10.1155/2011/579402
• Languages: English
• ISSNs: 1687-8000

Abstract

Abstract : The mathematical model of the operation of the first enzyme of the Escherichia coli phosphotransferase system, EI, is proposed. Parameters of the kinetic model describing the operation of EI under different conditions are identified on the basis of a large amount of known experimental data. The verified model is employed to predict modes of operation of EI under both in vivo physiological conditions and in vitro nonphysiological conditions. The model predicts that under in vivo physiological conditions, the rate of phosphotransfer from EI to the second protein of the phosphotransferase system HPr by the dimer is much higher than by the monomer. A hypothesis is proposed on the basis of calculations that the transfer by a monomer plays a role in the regulation of chemotaxis. At submicromolar pyruvate concentration, the model predicts nonmonotonic dependence of the phosphotransfer rate on the substrate (PEP) concentration.