Enzymes with noncanonical amino acids
Jingming Zhao1, Ashleigh J Burke1, Anthony P Green1
1Manchester Institute of Biotechnology, School of Chemistry, University of Manchester, 131 Princess Street, Manchester M1 7DN, UK.
Current Opinion in Chemical Biology
|March 13, 2020
Summary
Scientists are expanding the protein alphabet beyond 20 amino acids using genetic code expansion. This enables novel enzyme engineering for improved biocatalysts and new catalytic functions.
Area of Science:
- Biochemistry
- Synthetic Biology
- Enzyme Engineering
Background:
- Traditional enzyme engineering relies on 20 canonical amino acids.
- Genetic code expansion (GCE) allows site-specific incorporation of diverse noncanonical amino acids (ncAAs).
Purpose of the Study:
- To highlight how an expanded amino acid alphabet advances enzyme engineering.
- To showcase the utility of ncAAs in understanding enzyme mechanisms and designing novel biocatalysts.
Main Methods:
- Utilizing genetic code expansion techniques to introduce ncAAs into proteins.
- Applying these engineered proteins to study enzyme mechanisms and improve biocatalyst performance.
Main Results:
- ncAAs provide powerful tools for probing complex enzyme mechanisms.
- Incorporation of ncAAs enhances biocatalyst activity and stability.
- Enzymes with novel catalytic functions, inaccessible with canonical amino acids, can be designed.
Conclusions:
- The expanded amino acid alphabet opens new frontiers in enzyme engineering.
- Advancements in GCE technology will accelerate the adoption of ncAAs in biocatalysis research.
- ncAAs are crucial for developing next-generation enzymes with tailored properties and functions.
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