Steady-state kinetic behaviour of functioning-dependent structures.
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.
Thellier
Michel
M
Laboratoire 'Assemblages moléculaires: modélisation et imagerie SIMS', Faculté des Sciences de l'Université de Rouen, Mont-Saint-Aignan Cedex, France. Michel.Thellier@univ-rouen.fr
Legent
Guillaume
G
Amar
Patrick
P
Norris
Vic
V
Ripoll
Camille
C
D019281:Dimerization; D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism*; D006706:Homeostasis; D007700:Kinetics; D008956:Models, Chemical; D008958:Models, Molecular; D009097:Multienzyme Complexes / Q000737:chemistry* / Q000378:metabolism*; D015398:Signal Transduction
D004798:Enzymes; D009097:Multienzyme Complexes