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Simulations of the active transport of a neutral solute based on a kinase‐channel‐phosphatase topology
Author(s) -
Fiaty K.,
Charcosset C.,
Perrin B.,
Couturier R.,
Maïsterrena B.
Publication year - 2005
Publication title -
journal of computational chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.907
H-Index - 188
eISSN - 1096-987X
pISSN - 0192-8651
DOI - 10.1002/jcc.20160
Subject(s) - topology (electrical circuits) , phosphatase , membrane , substrate (aquarium) , membrane topology , active site , chemistry , kinase , membrane potential , biophysics , enzyme , membrane protein , biochemistry , biology , mathematics , ecology , combinatorics
Simulations of coupled interactions involving two opposite enzymatic reactions, solute diffusions, and electrostatic interactions between membrane charges and charged solutes were conducted under a fixed kinase‐channel‐phosphatase (KCP) topology oriented from the outside to the inside of a porous membrane structure. Depending on the kinase and phosphatase locations, we recently demonstrated that an active transport of a phosphorylated substrate may occur via the opposite topology, that is, a PCK topology. The present analysis demonstrates that, under a KCP membrane topology, which also behaves as a specific ATP‐dependent transporter, the active transport of a neutral substrate may occur. This analogous active transport appears to be dependent on the phosphatase location and on the membrane surface potentials. A broad analysis of the role played by the main parameters taken into account in the model was conducted in order to define precisely the physico‐chemical conditions and the membrane topology needed for the highest active transports within the shortest time. © 2004 Wiley Periodicals, Inc. J Comput Chem 26: 201–213, 2005