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Related Concept Videos

Introduction to Mechanisms of Enzyme Catalysis01:13

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...
Introduction to Mechanisms of Enzyme Catalysis01:13

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...
Evolution of New Traits in Microbes01:24

Evolution of New Traits in Microbes

Microorganisms evolve rapidly due to their large population sizes and short generation times, often exhibiting measurable changes within days under laboratory conditions. Natural selection acts on standing genetic variation, enabling the retention and amplification of beneficial traits that confer fitness advantages in changing environments.Adaptive Pigment Regulation in RhodobacterIn Rhodobacter, a genus of purple non-sulfur bacteria, light-harvesting pigments such as bacteriochlorophyll and...
Induced-fit Model01:13

Induced-fit Model

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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Ligand Binding and Linkage00:49

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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...

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Updated: May 19, 2026

In Vitro Directed Evolution of a Restriction Endonuclease with More Stringent Specificity
09:16

In Vitro Directed Evolution of a Restriction Endonuclease with More Stringent Specificity

Published on: March 25, 2020

Network context and selection in the evolution to enzyme specificity.

Hojung Nam1, Nathan E Lewis, Joshua A Lerman

  • 1Department of Bioengineering, University of California San Diego, La Jolla, CA 92093-0412, USA.

Science (New York, N.Y.)
|September 1, 2012
PubMed
Summary
This summary is machine-generated.

Enzymes evolved specificity from promiscuous ancestors. Specialist enzymes are essential, maintain high metabolic flux, and require more regulation than generalist enzymes, a trend conserved across domains.

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Mutagenesis and Functional Selection Protocols for Directed Evolution of Proteins in E. coli
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Last Updated: May 19, 2026

In Vitro Directed Evolution of a Restriction Endonuclease with More Stringent Specificity
09:16

In Vitro Directed Evolution of a Restriction Endonuclease with More Stringent Specificity

Published on: March 25, 2020

Mutagenesis and Functional Selection Protocols for Directed Evolution of Proteins in E. coli
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Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
06:50

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Published on: January 26, 2024

Area of Science:

  • Biochemistry
  • Metabolic Engineering
  • Evolutionary Biology

Background:

  • Enzymes are believed to have evolved high specificity from ancestral proteins with broader functions.
  • A significant portion of enzymes in metabolic networks exhibit promiscuity, catalyzing multiple reactions or acting on various substrates.

Purpose of the Study:

  • To investigate the functional and regulatory differences between generalist and specialist enzymes within metabolic networks.
  • To understand the evolutionary pressures driving enzyme specificity.

Main Methods:

  • Analysis of a genome-scale metabolic model of Escherichia coli.
  • Comparative analysis of enzyme properties including essentiality, metabolic flux, and regulatory requirements.
  • Examination of conserved properties across Archaea and Eukarya.

Main Results:

  • 37% of Escherichia coli enzymes are generalists, catalyzing 65% of known metabolic reactions.
  • Specialist enzymes are more frequently essential, maintain higher metabolic flux, and necessitate greater regulatory control compared to generalist enzymes.
  • These distinctions between generalist and specialist enzymes are conserved across Archaea and Eukarya.

Conclusions:

  • Metabolic network context and environmental conditions significantly influence the evolution of enzyme specificity.
  • Specialization in enzymes is driven by the need for essential functions, high metabolic flux, and precise regulation in dynamic environments.