An evolutionary approach to enzyme kinetics: Optimization of ordered mechanisms

DOI10.1007/BF02458290MaRDI QIDQ1319902zbMATH OpenOpenAlexFDO

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

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)

Recommendations

• Optimality principle and determination of kinetic constants for biochemical reactions
• CMMSE-17: general analytical laws for metabolic pathways
• A theoretical approach to the evolution and structural design of enzymatic networks; linear enzymatic chains, branched pathways and glycolysis of erythrocytes
• Why nature has elected Michaelis‐Menten kinetics for enzymes: a tentative rationale from variational calculus
• Linear compartmental systems. III. Application to enzymatic reactions

Cites work

• scientific article; zbMATH DE number 880332 (Why is no real title available?)
• 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

Cited in

(10)

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

This page was built for publication: An evolutionary approach to enzyme kinetics: Optimization of ordered mechanisms

Report a bug (only for logged in users!)Click here to report a bug for this page (MaRDI item Q1319902)