JBC Transcription and Nuclear Factor Monoclonals

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kukuruzinska, M. A.
Right arrow Articles by Roseman, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kukuruzinska, M. A.
Right arrow Articles by Roseman, S.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J. Biol. Chem., Vol. 259, Issue 19, 11679-11681, Oct, 1984

Subunit association of enzyme I of the Salmonella typhimurium phosphoenolpyruvate: glycose phosphotransferase system. Temperature dependence and thermodynamic properties

MA Kukuruzinska, BW Turner, GK Ackers and S Roseman

The bacterial phosphoenolpyruvate:glycose phosphotransferase system plays an essential role in diverse physiological phenomena. To perform these functions, the system is stringently regulated, although the underlying molecular regulatory mechanisms have not been established. A potential target for this type of regulation is the first protein in the phosphotransfer sequence, Enzyme I, which catalyzes the following reaction: P-enolpyruvate + Enzyme I Mg2+ in equilibrium phospho-I + pyruvate. We reported previously that Enzyme I from Salmonella typhimurium consists of identical subunits which associate in a temperature-dependent manner; the mode of association was found to be either monomer-dimer or isodesmic. The association reaction has now been investigated by analytical gel chromatography at 8, 11, and 23 degrees C. At each temperature, the mode of association was strictly monomer-dimer. The apparent association equilibrium constant, K'a, increased dramatically with temperature, with an enthalpy of 54.8 +/- 6.3 kcal/mol. At 23 degrees C, K'a decreased slightly when the enzyme solution contained either Mg2+ or phosphoenolpyruvate. However, when both ligands were present, i.e. under conditions where Enzyme I is phosphorylated, K'a decreased significantly (25-fold at 11 degrees C and 50-fold at 23 degrees C). These results are in accord with a model for the action of Enzyme I which involves a cycle of association and dissociation. This model has potentially important implications for regulating Enzyme I and the bacterial phosphoenolpyruvate:glycose phosphotransferase system.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Biophys. JHome page
E. Hurtado-Gomez, O. Abian, F. J. Munoz, M. J. Hernaiz, A. Velazquez-Campoy, and J. L. Neira
Defining the Epitope Region of a Peptide from the Streptomyces coelicolor Phosphoenolpyruvate:Sugar Phosphotransferase System Able to Bind to the Enzyme I
Biophys. J., August 1, 2008; 95(3): 1336 - 1348.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
A. Teplyakov, K. Lim, P.-P. Zhu, G. Kapadia, C. C. H. Chen, J. Schwartz, A. Howard, P. T. Reddy, A. Peterkofsky, and O. Herzberg
Structure of phosphorylated enzyme I, the phosphoenolpyruvate:sugar phosphotransferase system sugar translocation signal protein
PNAS, October 31, 2006; 103(44): 16218 - 16223.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
JoseA. Marquez, S. Reinelt, B. Koch, R. Engelmann, W. Hengstenberg, and K. Scheffzek
Structure of the Full-length Enzyme I of the Phosphoenolpyruvate-dependent Sugar Phosphotransferase System
J. Biol. Chem., October 27, 2006; 281(43): 32508 - 32515.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
H. V. Patel, K. A. Vyas, R. Savtchenko, and S. Roseman
The Monomer/Dimer Transition of Enzyme I of the Escherichia coli Phosphotransferase System
J. Biol. Chem., June 30, 2006; 281(26): 17570 - 17578.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
M. N. Dimitrova, A. Peterkofsky, and A. Ginsburg
Opposing effects of phosphoenolpyruvate and pyruvate with Mg2+ on the conformational stability and dimerization of phosphotransferase enzyme I from Escherichia coli
Protein Sci., September 1, 2003; 12(9): 2047 - 2056.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L. F. Garcia-Alles, K. Flukiger, J. Hewel, R. Gutknecht, C. Siebold, S. Schurch, and B. Erni
Mechanism-based Inhibition of Enzyme I of the Escherichia coli Phosphotransferase System. CYSTEINE 502 IS AN ESSENTIAL RESIDUE
J. Biol. Chem., February 22, 2002; 277(9): 6934 - 6942.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. M. Rohwer, N. D. Meadow, S. Roseman, H. V. Westerhoff, and P. W. Postma
Understanding Glucose Transport by the Bacterial Phosphoenolpyruvate:Glycose Phosphotransferase System on the Basis of Kinetic Measurements in Vitro
J. Biol. Chem., November 3, 2000; 275(45): 34909 - 34921.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1984 by the American Society for Biochemistry and Molecular Biology.