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Induced-fit Model

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Most chemical reactions in cells require enzymes—biological catalysts that speed up the reaction without being consumed or permanently changed. They reduce the activation energy needed to convert the reactants into products. Enzymes are proteins, that usually work by binding to a substrate—a reactant molecule that they act upon.
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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...

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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...

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Updated: Jul 7, 2026

The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis

The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis

Published on: March 17, 2010

A perspective on enzyme catalysis.

Stephen J Benkovic¹, Sharon Hammes-Schiffer

¹Department of Chemistry, 152 Davey Laboratory, Pennsylvania State University, University Park, PA 16802, USA. sjb1@psu.edu

Science (New York, N.Y.)

|August 30, 2003

Summary

This study examines enzyme catalysis hypotheses, highlighting how protein molecular motions, particularly in dihydrofolate reductase, are crucial for catalytic efficiency. Conserved residue networks influence enzyme structure and motion, impacting evolution and protein engineering.

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Area of Science:

Biochemistry
Theoretical Chemistry
Structural Biology

Background:

Enzymatic catalysis is fundamental to biological processes.
Numerous hypotheses have been proposed to explain enzyme mechanisms.
The role of protein dynamics in enzyme function remains an active area of research.

Purpose of the Study:

To scrutinize seminal hypotheses of enzymatic catalysis.
To investigate the impact of protein molecular motions on catalytic properties.
To explore the evolutionary and engineering implications of enzyme dynamics.

Main Methods:

Historical review of biochemical and theoretical perspectives on enzyme catalysis.
Analysis of molecular motions within proteins.
Case study using dihydrofolate reductase.

Main Results:

Enzyme catalytic efficiency is significantly influenced by internal molecular motions.
Coupled networks of conserved residues dictate protein structure and dynamics.
Dihydrofolate reductase serves as a model demonstrating these coupled networks.

Conclusions:

Protein molecular motions are integral to enzymatic catalysis.
Conserved residue networks play a key role in enzyme evolution and function.
Understanding these networks offers potential for advanced protein engineering.