An evolutionary approach to enzyme kinetics: Optimization of ordered mechanisms

DOI10.1007/BF02458290zbMATH Open0796.92013OpenAlexW4233642943MaRDI QIDQ1319902FDOQ1319902

Authors: Thomas Wilhelm, Edda Hoffmann-Klipp, Reinhart Heinrich 

Publication date: 9 October 1994

Published in: Bulletin of Mathematical Biology (Search for Journal in Brave)

Full work available at URL: https://doi.org/10.1007/bf02458290

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zbMATH Keywords

nonlinear optimizationconcentrationscomplete set of solutionsbi-uni- mechanismscalculation of rate constantsequilibrium constantmaximal reaction ratesMichaelis constantsone-substrate-one-product reactionsoptimal kinetic designoptimal kinetic parametersordered uni-uni- reactionsunbranched enzymic reactions

Mathematics Subject Classification ID

Differential games and control (49N70) Pursuit and evasion games (49N75) Kinetics in biochemical problems (pharmacokinetics, enzyme kinetics, etc.) (92C45) Chemical kinetics in thermodynamics and heat transfer (80A30)

Cites Work

• A theoretical approach to the evolution and structural design of enzymatic networks; linear enzymatic chains, branched pathways and glycolysis of erythrocytes
• Minimization of intermediate concentrations as a suggested optimality principle for biochemical networks. I: Theoretical analysis
• Title not available (Why is that?)

Cited In (10)

• Modelling, steady state analysis and optimization of the catalytic efficiency of the triosephosphate isomerase
• CMMSE-17: general analytical laws for metabolic pathways
• Evolution of enzyme levels in metabolic pathways: a theoretical approach. II
• A search for maximum species abundances in ecological communities under conditional diversity optimization
• How to derive flux control coefficients from the rate equations of classical enzyme kinetics
• Optimizing enzymatic catalysts for rapid turnover of substrates with low enzyme sequestration
• Towards the construction of a mathematically rigorous framework for the modelling of evolutionary fitness
• Reduction of intrinsic kinetic and thermodynamic barriers for enzyme-catalysed proton transfers from carbon acid substrates
• Kinetic and thermodynamic constraints for the structural design of glycolysis
• A theoretical approach to the evolution and structural design of enzymatic networks; linear enzymatic chains, branched pathways and glycolysis of erythrocytes

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