Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
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...
Conservative Site-specific Recombination and Phase Variation02:53

Conservative Site-specific Recombination and Phase Variation

Because the DNA segments are cut and reorganized in a direction-specific manner, site-specific recombination has emerged as an efficient genetic engineering technique. Flippase and Cyclization recombinases or Flp and Cre, respectively, are two members of the tyrosine recombinase family derived from bacteriophages, that are used to mediate site-specific DNA insertions, deletions, and targeted expression of proteins in mammalian cell lines.
The recognition sites for Cre recombinase called LoxP...
Exon Recombination02:32

Exon Recombination

The evolution of new genes is critical for speciation. Exon recombination, also known as exon shuffling or domain shuffling, is an important means of new gene formation. It is observed across vertebrates, invertebrates, and in some plants such as potatoes and sunflowers. During exon recombination, exons from the same or different genes recombine and produce new exon-intron combinations, which might evolve into new genes. 
Exon shuffling follows “splice frame rules.” Each exon has three reading...
Introduction to Enzymes01:22

Introduction to Enzymes

The use of enzymes by humans dates to 7000 BCE. Humans first used enzymes to ferment sugars and produce alcohol without knowing that this was an enzyme-catalyzed reaction. Wilhelm Kuhne coined the term 'enzyme' in 1877 from the Greek words ‘en’ meaning ‘in’ or ‘within’ and ‘zyme’ meaning ‘yeast.’
Most enzymes are proteins that speed up biochemical reactions without being consumed. Enzymes contain one or more active sites that bind the substrates and convert them into products. Many enzymes also...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

The Discovery of <i>N</i> <sup>2</sup>,<i>N</i> <sup>2</sup>‑Dimethylguanine Hydrolases Unravels General Molecular Principles of Enzyme Evolvability and Promiscuity.

ACS catalysis·2026
Same author

On the Origin of Substrate Specificity of Enzymes from the Amidohydrolase Superfamily.

Angewandte Chemie (International ed. in English)·2025
Same author

A naturally occurring standalone TrpB enzyme provides insights into allosteric communication within tryptophan synthase.

Protein science : a publication of the Protein Society·2025
Same author

Photocontrolling the Enantioselectivity of a Phosphotriesterase via Incorporation of a Light-Responsive Unnatural Amino Acid.

JACS Au·2025
Same author

Conformational Modulation of a Mobile Loop Controls Catalysis in the (βα)<sub>8</sub>-Barrel Enzyme of Histidine Biosynthesis HisF.

JACS Au·2024
Same author

Validation of aminodeoxychorismate synthase and anthranilate synthase as novel targets for bispecific antibiotics inhibiting conserved protein-protein interactions.

Applied and environmental microbiology·2024
Same journal

Overlapping gut microbiome signatures in aging and disease are characterized by enrichment of medication-associated oral microbes in the gut.

FEBS letters·2026
Same journal

Csk binding to integrin β3 is regulated by tyrosine and threonine phosphorylation of β3.

FEBS letters·2026
Same journal

Mixed-class J-domain protein scaffolds promote expanded aggregate handling and multivalent Hsp70 engagement during functional disaggregase assembly.

FEBS letters·2026
Same journal

Design and analysis strategies for robust microbiome ageing research.

FEBS letters·2026
Same journal

Three phosphatase families form a community: The phosphohydrolases that act upon inositol pyrophosphates.

FEBS letters·2026
Same journal

Cell geometry and membrane protein crowding constrain Escherichia coli growth rate, overflow metabolism, respiration, and maintenance energy.

FEBS letters·2026
See all related articles

Related Experiment Video

Updated: Jun 26, 2026

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
13:30

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes

Published on: November 7, 2012

Reconstructing enzyme evolution by protein engineering.

Lukas Drexler1, Markus R Busch2, Reinhard Sterner1

  • 1Institute of Biophysics and Physical Biochemistry, Regensburg Center for Biochemistry, University of Regensburg, Germany.

FEBS Letters
|June 25, 2026
PubMed
Summary
This summary is machine-generated.

Protein engineering methods reveal enzyme evolution from simple scaffolds to complex functions. This research traces how enzymes adapted over time, even evolving to degrade human-made pollutants.

Keywords:
ancestral sequence reconstructiondirected evolutionenzymesmolecular evolutionprotein engineeringrational design

More Related Videos

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

Protein Engineering by Yeast Surface Display
05:49

Protein Engineering by Yeast Surface Display

Published on: November 29, 2024

Related Experiment Videos

Last Updated: Jun 26, 2026

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
13:30

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes

Published on: November 7, 2012

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

Protein Engineering by Yeast Surface Display
05:49

Protein Engineering by Yeast Surface Display

Published on: November 29, 2024

Area of Science:

  • Biochemistry
  • Evolutionary Biology
  • Protein Engineering

Background:

  • Understanding enzyme evolution is crucial for comprehending the diversity of modern enzymes.
  • Enzymes have evolved from simpler ligand-binding proteins since the origin of life.

Purpose of the Study:

  • To review how protein engineering techniques elucidate enzyme evolutionary processes.
  • To explore the emergence of enzyme diversity, substrate specificity, and complex enzyme structures.
  • To examine enzyme adaptation to environmental changes and the evolution of new functions.

Main Methods:

  • Computational and experimental retracing of evolutionary processes.
  • Protein engineering techniques including rational design and directed evolution.
  • Ancestral sequence reconstruction and analysis of enzyme property interdependence.

Main Results:

  • Elucidation of how first enzymes emerged from ligand-binding protein scaffolds.
  • Understanding the diversification of enzymes with similar catalytic mechanisms but different substrate specificities.
  • Demonstration of natural selection driving the formation of oligomeric enzyme complexes from monomers.

Conclusions:

  • Protein engineering is a powerful tool for reconstructing enzyme evolutionary history.
  • Enzymes have evolved complex functions and adaptations in response to environmental pressures.
  • Rapid enzyme evolution enables the degradation of novel anthropogenic substances.