Steady-state kinetic behaviour of functioning-dependent structures

被引:16
作者
Thellier, Michel [1 ]
Legent, Guillaume
Amar, Patrick
Norris, Vic
Ripoll, Camille
机构
[1] Univ Rouen, Fac Sci, CNRS,SIMS, FRE 2829,Lab Assemblages Mol Modelisat & Imagerie, F-76821 Mont St Aignan, France
[2] Univ Paris Sud, Rech Informat Lab, Orsay, France
[3] Genopole R, Epigenom Project, Evry, France
关键词
enzyme kinetics; metabolic or signalling pathways; mathematical modelling; protein associations;
D O I
10.1111/j.1742-4658.2006.05425.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:4287 / 4299
页数:13
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