The total quasi-steady-state for multiple alternative substrate reactions

被引:2
作者
Besya, Azimberdy [1 ]
Rao, Shodhan [1 ,2 ]
机构
[1] Univ Ghent, Ctr Biosyst & Biotech Data Sci, Global Campus,119 Songdomunhwa Ro, Incheon 21985, South Korea
[2] Univ Ghent, Dept Data Anal & Math Modelling, Coupure Links 653, B-9000 Ghent, Belgium
关键词
Singular perturbation analysis; Linearization; Taylor series; Matrix methods; Enzyme kinetics; Approximate solutions; MICHAELIS-MENTEN KINETICS; ENZYME-KINETICS; APPROXIMATION; ASSUMPTION; VALIDITY;
D O I
10.1007/s10910-022-01339-6
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
The Michaelis-Menten-Briggs-Haldane approximation and its extension, the total quasi-steady-state approximation (tQSSA) are famous assumptions for simplification of mathematical modeling of enzyme-substrate reactions. These approximations and their validity conditions are well studied for a single substrate reaction system. However, the extension of these studies for the tQSSA of the general case of multiple substrate reactions is yet to be performed precisely due to the consequent non-linear expressions for tQSSA. In this paper, we introduce a linearization method for equations governing the tQSSA of multiple substrate reactions to obtain an analytical solution for the evolution of concentrations of reactants that is valid throughout the whole time period. In addition, we provide the validity conditions of the tQSSA for multiple substrate reaction systems using the singular perturbation analysis method.
引用
收藏
页码:841 / 861
页数:21
相关论文
共 16 条
[1]   UNIFORM ASYMPTOTIC EXPANSIONS BEYOND THE tQSSA FOR THE GOLDBETER-KOSHLAND SWITCH [J].
Bersani, A. M. ;
Borri, A. ;
Milanesi, A. ;
Tomassetti, G. ;
Vellucci, P. .
SIAM JOURNAL ON APPLIED MATHEMATICS, 2020, 80 (03) :1123-1152
[2]  
Bersani AM, 2017, COMMUN APPL IND MATH, V8, P81, DOI 10.1515/caim-2017-0005
[3]  
Bersani A.M., 2019, Commun. Appl. Ind. Math., V10, P162, DOI [10.1515/caim-2019-0019, DOI 10.1515/CAIM-2019-0019]
[4]   Asymptotics and numerical analysis for enzymatic auxiliary reactions [J].
Bersani, Alberto Maria ;
Borri, Alessandro ;
Tosti, Maria Elisa .
CONTINUUM MECHANICS AND THERMODYNAMICS, 2021, 33 (03) :851-872
[5]   Extending the quasi-steady state approximation by changing variables [J].
Borghans, JAM ;
DeBoer, RJ ;
Segel, LA .
BULLETIN OF MATHEMATICAL BIOLOGY, 1996, 58 (01) :43-63
[6]   A note on the kinetics of enzyme action. [J].
Briggs, GE ;
Haldane, JBS .
BIOCHEMICAL JOURNAL, 1925, 19 (02) :338-339
[7]   A perturbation solution of Michaelis-Menten kinetics in a "total" framework [J].
Dell'Acqua, Guido ;
Bersani, Alberto Maria .
JOURNAL OF MATHEMATICAL CHEMISTRY, 2012, 50 (05) :1136-1148
[8]  
Lin CC., 1988, CLASSICS APPL MATH, DOI [10.1137/1.9781611971347, DOI 10.1137/1.9781611971347]
[9]  
Michaelis L, 1913, BIOCHEM Z, V49, P333
[10]   The total quasi-steady-state approximation for fully competitive enzyme reactions [J].
Pedersen, Morten Gram ;
Bersani, Alberto M. ;
Bersani, Enrico .
BULLETIN OF MATHEMATICAL BIOLOGY, 2007, 69 (01) :433-457