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Related Experiment Video

Updated: May 11, 2026

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

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

Published on: November 7, 2012

Designed divergent evolution of enzyme function.

Yasuo Yoshikuni¹, Thomas E Ferrin, Jay D Keasling

¹UCSF/UCB Joint Graduate Group in Bioengineering, Lawrence Berkeley National Laboratory, Berkeley, California 94710, USA.

|February 24, 2006

Summary

This summary is machine-generated.

Researchers engineered novel enzymes by understanding protein plasticity. This study demonstrates rational enzyme design by modifying plasticity residues in terpene synthases, creating specific and active biocatalysts.

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

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

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

Published on: March 25, 2020

Area of Science:

Biochemistry
Molecular Biology
Enzyme Engineering

Background:

Proteins with promiscuous functions evolve higher specificity and activity through small amino acid changes (plasticity).
Understanding this divergent molecular evolution can guide the design of more specific and active enzymes.
Plasticity residues in active sites are crucial for functional adaptability.

Purpose of the Study:

To investigate how plasticity residues contribute to molecular evolution.
To formulate a rational design methodology for enzyme engineering.
To construct novel terpene synthases with altered catalytic functions.

Main Methods:

Probed plasticity residues in the active site of the promiscuous gamma-humulene synthase.
Systematically recombined identified plasticity residues using a mathematical model.
Constructed and characterized novel terpene synthases.

Main Results:

Successfully engineered seven specific and active terpene synthases.
These novel enzymes utilize different reaction pathways to produce distinct sesquiterpene products.
Demonstrated the feasibility of exploiting protein scaffold evolvability.

Conclusions:

Rational enzyme design approaches based on plasticity are effective.
The study provides evidence for the utility of understanding molecular evolution in enzyme engineering.
Highlights the potential for creating tailored enzymes with desired specificities and activities.