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J. Biol. Chem., Vol. 275, Issue 45, 34909-34921, November 10, 2000
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From the The kinetic parameters in vitro of
the components of the phosphoenolpyruvate:glycose
phosphotransferase system (PTS) in enteric bacteria were collected. To
address the issue of whether the behavior in vivo of the
PTS can be understood in terms of these enzyme kinetics, a detailed
kinetic model was constructed. Each overall phosphotransfer reaction
was separated into two elementary reactions, the first entailing
association of the phosphoryl donor and acceptor into a complex and the
second entailing dissociation of the complex into dephosphorylated
donor and phosphorylated acceptor. Literature data on the
Km values and association constants of PTS proteins
for their substrates, as well as equilibrium and rate constants for the
overall phosphotransfer reactions, were related to the rate constants
of the elementary steps in a set of equations; the rate constants could
be calculated by solving these equations simultaneously. No kinetic
parameters were fitted. As calculated by the model, the kinetic
parameter values in vitro could describe experimental
results in vivo when varying each of the PTS protein concentrations individually while keeping the other protein
concentrations constant. Using the same kinetic constants, but
adjusting the protein concentrations in the model to those present in
cell-free extracts, the model could reproduce experiments in
vitro analyzing the dependence of the flux on the total PTS
protein concentration. For modeling conditions in vivo it
was crucial that the PTS protein concentrations be implemented at their
high in vivo values. The model suggests a new
interpretation of results hitherto not understood; in vivo,
the major fraction of the PTS proteins may exist as complexes with
other PTS proteins or boundary metabolites, whereas in
vitro, the fraction of complexed proteins is much smaller.
Understanding Glucose Transport by the Bacterial
Phosphoenolpyruvate:Glycose Phosphotransferase System on the
Basis of Kinetic Measurements in Vitro*
§¶,
,, Department of Biochemistry, University of
Stellenbosch, Private Bag X1, 7602 Matieland, South Africa, the
§ E. C. Slater Institute, BioCentrum Amsterdam,
University of Amsterdam, Plantage Muidergracht 12, NL-1018 TV
Amsterdam, The Netherlands, the Department of Biology, The Johns
Hopkins University, Baltimore, Maryland 21218-2685, and the
** Institute for Molecular Biological Sciences, BioCentrum
Amsterdam, Vrije Universiteit, De Boelelaan 1087, NL-1081 HV Amsterdam, The Netherlands
*
This study was supported by the South African Foundation for
Research Development, the Harry Crossley Foundation and the
Netherlands Organization for Scientific Research.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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