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Rational approaches for engineering novel functionalities in carbon-carbon bond forming enzymes
Enzymes that catalyze carbon-carbon bond formation can be exploited as biocatalyst for synthetic organic chemistry. However, natural enzymes frequently do not possess the required properties or specificities to catalyze industrially useful transformations. This mini-review describes recent work usin...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Research Network of Computational and Structural Biotechnology (RNCSB) Organization
2012
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3962088/ https://www.ncbi.nlm.nih.gov/pubmed/24688644 http://dx.doi.org/10.5936/csbj.201209003 |
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author | Baker, Perrin Seah, Stephen Y. K. |
author_facet | Baker, Perrin Seah, Stephen Y. K. |
author_sort | Baker, Perrin |
collection | PubMed |
description | Enzymes that catalyze carbon-carbon bond formation can be exploited as biocatalyst for synthetic organic chemistry. However, natural enzymes frequently do not possess the required properties or specificities to catalyze industrially useful transformations. This mini-review describes recent work using knowledge-guided site-specific mutagenesis of key active site residues to alter substrate specificity, stereospecificity and reaction specificity of these enzymes. In addition, examples of de novo designed enzymes that catalyze C-C bond reactions not found in nature will be discussed. |
format | Online Article Text |
id | pubmed-3962088 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Research Network of Computational and Structural Biotechnology (RNCSB) Organization |
record_format | MEDLINE/PubMed |
spelling | pubmed-39620882014-03-31 Rational approaches for engineering novel functionalities in carbon-carbon bond forming enzymes Baker, Perrin Seah, Stephen Y. K. Comput Struct Biotechnol J Mini Review Enzymes that catalyze carbon-carbon bond formation can be exploited as biocatalyst for synthetic organic chemistry. However, natural enzymes frequently do not possess the required properties or specificities to catalyze industrially useful transformations. This mini-review describes recent work using knowledge-guided site-specific mutagenesis of key active site residues to alter substrate specificity, stereospecificity and reaction specificity of these enzymes. In addition, examples of de novo designed enzymes that catalyze C-C bond reactions not found in nature will be discussed. Research Network of Computational and Structural Biotechnology (RNCSB) Organization 2012-10-02 /pmc/articles/PMC3962088/ /pubmed/24688644 http://dx.doi.org/10.5936/csbj.201209003 Text en © Baker and Seah. http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly cited. |
spellingShingle | Mini Review Baker, Perrin Seah, Stephen Y. K. Rational approaches for engineering novel functionalities in carbon-carbon bond forming enzymes |
title | Rational approaches for engineering novel functionalities in carbon-carbon bond forming enzymes |
title_full | Rational approaches for engineering novel functionalities in carbon-carbon bond forming enzymes |
title_fullStr | Rational approaches for engineering novel functionalities in carbon-carbon bond forming enzymes |
title_full_unstemmed | Rational approaches for engineering novel functionalities in carbon-carbon bond forming enzymes |
title_short | Rational approaches for engineering novel functionalities in carbon-carbon bond forming enzymes |
title_sort | rational approaches for engineering novel functionalities in carbon-carbon bond forming enzymes |
topic | Mini Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3962088/ https://www.ncbi.nlm.nih.gov/pubmed/24688644 http://dx.doi.org/10.5936/csbj.201209003 |
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