Engineering enzyme activity using an expanded amino acid alphabet
Abstract Enzyme design and engineering strategies are typically constrained by the limited size of nature’s genetic alphabet, comprised of only 20 canonical amino acids. In recent years, site-selective incorporation of non-canonical amino acids (ncAAs) via an expanded genetic code has emerged as a p...
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| Published in | Protein engineering, design and selection Vol. 36 |
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| Main Authors | , , , |
| Format | Journal Article |
| Language | English |
| Published |
England
Oxford University Press
21.01.2023
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| Subjects | |
| Online Access | Get full text |
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| Abstract | Abstract
Enzyme design and engineering strategies are typically constrained by the limited size of nature’s genetic alphabet, comprised of only 20 canonical amino acids. In recent years, site-selective incorporation of non-canonical amino acids (ncAAs) via an expanded genetic code has emerged as a powerful means of inserting new functional components into proteins, with hundreds of structurally diverse ncAAs now available. Here, we highlight how the emergence of an expanded repertoire of amino acids has opened new avenues in enzyme design and engineering. ncAAs have been used to probe complex biological mechanisms, augment enzyme function and, most ambitiously, embed new catalytic mechanisms into protein active sites that would be challenging to access within the constraints of nature’s genetic code. We predict that the studies reviewed in this article, along with further advances in genetic code expansion technology, will establish ncAA incorporation as an increasingly important tool for biocatalysis in the coming years. |
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| AbstractList | Enzyme design and engineering strategies are typically constrained by the limited size of nature’s genetic alphabet, comprised of only 20 canonical amino acids. In recent years, site-selective incorporation of non-canonical amino acids (ncAAs) via an expanded genetic code has emerged as a powerful means of inserting new functional components into proteins, with hundreds of structurally diverse ncAAs now available. Here, we highlight how the emergence of an expanded repertoire of amino acids has opened new avenues in enzyme design and engineering. ncAAs have been used to probe complex biological mechanisms, augment enzyme function and, most ambitiously, embed new catalytic mechanisms into protein active sites that would be challenging to access within the constraints of nature’s genetic code. We predict that the studies reviewed in this article, along with further advances in genetic code expansion technology, will establish ncAA incorporation as an increasingly important tool for biocatalysis in the coming years. Abstract Enzyme design and engineering strategies are typically constrained by the limited size of nature’s genetic alphabet, comprised of only 20 canonical amino acids. In recent years, site-selective incorporation of non-canonical amino acids (ncAAs) via an expanded genetic code has emerged as a powerful means of inserting new functional components into proteins, with hundreds of structurally diverse ncAAs now available. Here, we highlight how the emergence of an expanded repertoire of amino acids has opened new avenues in enzyme design and engineering. ncAAs have been used to probe complex biological mechanisms, augment enzyme function and, most ambitiously, embed new catalytic mechanisms into protein active sites that would be challenging to access within the constraints of nature’s genetic code. We predict that the studies reviewed in this article, along with further advances in genetic code expansion technology, will establish ncAA incorporation as an increasingly important tool for biocatalysis in the coming years. Enzyme design and engineering strategies are typically constrained by the limited size of nature's genetic alphabet, comprised of only 20 canonical amino acids. In recent years, site-selective incorporation of non-canonical amino acids (ncAAs) via an expanded genetic code has emerged as a powerful means of inserting new functional components into proteins, with hundreds of structurally diverse ncAAs now available. Here, we highlight how the emergence of an expanded repertoire of amino acids has opened new avenues in enzyme design and engineering. ncAAs have been used to probe complex biological mechanisms, augment enzyme function and, most ambitiously, embed new catalytic mechanisms into protein active sites that would be challenging to access within the constraints of nature's genetic code. We predict that the studies reviewed in this article, along with further advances in genetic code expansion technology, will establish ncAA incorporation as an increasingly important tool for biocatalysis in the coming years.Enzyme design and engineering strategies are typically constrained by the limited size of nature's genetic alphabet, comprised of only 20 canonical amino acids. In recent years, site-selective incorporation of non-canonical amino acids (ncAAs) via an expanded genetic code has emerged as a powerful means of inserting new functional components into proteins, with hundreds of structurally diverse ncAAs now available. Here, we highlight how the emergence of an expanded repertoire of amino acids has opened new avenues in enzyme design and engineering. ncAAs have been used to probe complex biological mechanisms, augment enzyme function and, most ambitiously, embed new catalytic mechanisms into protein active sites that would be challenging to access within the constraints of nature's genetic code. We predict that the studies reviewed in this article, along with further advances in genetic code expansion technology, will establish ncAA incorporation as an increasingly important tool for biocatalysis in the coming years. |
| Author | Green, Anthony P Taylor, Christopher J Birch-Price, Zachary Ortmayer, Mary |
| Author_xml | – sequence: 1 givenname: Zachary surname: Birch-Price fullname: Birch-Price, Zachary email: zachary.price@postgrad.manchester.ac.uk – sequence: 2 givenname: Christopher J surname: Taylor fullname: Taylor, Christopher J email: christopher.taylor-10@postgrad.manchester.ac.uk – sequence: 3 givenname: Mary surname: Ortmayer fullname: Ortmayer, Mary email: mary.ortmayer@manchester.ac.uk – sequence: 4 givenname: Anthony P orcidid: 0000-0003-0454-1798 surname: Green fullname: Green, Anthony P email: anthony.green@manchester.ac.uk |
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| Keywords | non-canonical amino acids genetic code expansion directed evolution |
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Enzyme design and engineering strategies are typically constrained by the limited size of nature’s genetic alphabet, comprised of only 20 canonical... Enzyme design and engineering strategies are typically constrained by the limited size of nature’s genetic alphabet, comprised of only 20 canonical amino... Enzyme design and engineering strategies are typically constrained by the limited size of nature's genetic alphabet, comprised of only 20 canonical amino... |
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| SubjectTerms | Amino Acids - chemistry Amino Acids - genetics Biocatalysis Cloning, Molecular Genetic Code - genetics Proteins - chemistry Review |
| Title | Engineering enzyme activity using an expanded amino acid alphabet |
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