Related Experiment Video
Updated: Jun 17, 2026

09:42
Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
Published on: January 16, 2016
Modular control analysis of slipping enzymes.
1Humboldt-Universität zu Berlin, Institut für Biologie, Lehrstuhl für Theoretische Biophysik, Germany.
Bio Systems
|March 26, 1999
Summary
This study introduces a new theory for metabolic control by enzymes with multiple reactions. It quanties control by coupled reactions versus slippage, aiding understanding of complex metabolic pathways.
Area of Science:
- Biochemistry
- Metabolic Control Theory
- Non-equilibrium Thermodynamics
Background:
- Metabolic control theory traditionally models enzymes with single reactions.
- Enzymes catalyzing multiple, incompletely coupled reactions present unique control challenges.
- Understanding these 'slipping enzymes' is crucial for comprehending complex metabolic regulation.
Purpose of the Study:
- To develop a theoretical framework for analyzing metabolic control exerted by slipping enzymes.
- To quantitatively distinguish between control from coupled reactions and control from slippage.
- To provide a method for calculating control coefficients for these complex enzymes.
Main Methods:
- Building upon modular (top-down) metabolic control theory.
- Treating slipping enzymes as modules with multiple independent fluxes.
- Utilizing linear transformations of fluxes or their logarithms.
- Applying linear non-equilibrium thermodynamics to describe slipping enzymes.
Main Results:
- A quantitative distinction between coupled reaction control and slippage control is established.
- Control coefficients for slipping enzymes can be calculated using the proposed framework.
- The theory is demonstrated with examples like proton pumps and Na+, K+-ATPase.
Conclusions:
- The developed theory offers a robust method for analyzing metabolic control by slipping enzymes.
- This approach enhances the understanding of complex metabolic regulation and enzyme function.
- The framework integrates metabolic control theory with non-equilibrium thermodynamics for a comprehensive analysis.
More Related Videos
Related Concept Videos
Enzyme Kinetics
Enzymes speed up reactions by lowering the activation energy of the reactants. The speed at which the enzyme turns reactants into products is called the rate of reaction. Several factors impact the rate of reaction, including the number of available reactants. Enzyme kinetics is the study of how an enzyme changes the rate of a reaction.
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
Cooperative Allosteric Transitions
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Introduction to Mechanisms of Enzyme Catalysis
For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes a mild...
Cooperative Allosteric Transitions
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Introduction to Mechanisms of Enzyme Catalysis
For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes a mild...

