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Steady‐state kinetic behaviour of functioning‐dependent structures
Author(s) -
Thellier Michel,
Legent Guillaume,
Amar Patrick,
Norris Vic,
Ripoll Camille
Publication year - 2006
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2006.05425.x
Subject(s) - steady state (chemistry) , kinetics , enzyme kinetics , chemistry , enzyme , biochemistry , physics , active site , classical mechanics
A fundamental problem in biochemistry is that of the nature of the coordination between and within metabolic and signalling pathways. It is conceivable that this coordination might be assured by what we term functioning‐dependent structures (FDSs), namely those assemblies of proteins that associate with one another when performing tasks and that disassociate when no longer performing them. To investigate a role in coordination for FDSs, we have studied numerically the steady‐state kinetics of a model system of two sequential monomeric enzymes, E 1 and E 2 . Our calculations show that such FDSs can display kinetic properties that the individual enzymes cannot. These include the full range of basic input/output characteristics found in electronic circuits such as linearity, invariance, pulsing and switching. Hence, FDSs can generate kinetics that might regulate and coordinate metabolism and signalling. Finally, we suggest that the occurrence of terms representative of the assembly and disassembly of FDSs in the classical expression of the density of entropy production are characteristic of living systems.

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