Engineering enzyme activity using an expanded amino acid alphabet.

Autor:	Birch-Price Z; School of Chemistry, Manchester Institute of Biotechnology, University of Manchester, Manchester, M1 7DN, UK., Taylor CJ; School of Chemistry, Manchester Institute of Biotechnology, University of Manchester, Manchester, M1 7DN, UK., Ortmayer M; School of Chemistry, Manchester Institute of Biotechnology, University of Manchester, Manchester, M1 7DN, UK., Green AP; School of Chemistry, Manchester Institute of Biotechnology, University of Manchester, Manchester, M1 7DN, UK.
Jazyk:	angličtina
Zdroj:	Protein engineering, design & selection : PEDS [Protein Eng Des Sel] 2023 Jan 21; Vol. 36.
DOI:	10.1093/protein/gzac013
Abstrakt:	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. (© The Author(s) 2022. Published by Oxford University Press.)
Databáze:	MEDLINE
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