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Transaminases for industrial biocatalysis: novel enzyme discovery
ABSTRACT: Transaminases (TAms) are important enzymes for the production of chiral amines for the pharmaceutical and fine chemical industries. Novel TAms for use in these industries have been discovered using a range of approaches, including activity-guided methods and homologous sequence searches fr...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Berlin Heidelberg
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7228992/ https://www.ncbi.nlm.nih.gov/pubmed/32300853 http://dx.doi.org/10.1007/s00253-020-10585-0 |
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author | Kelly, Stephen A. Mix, Stefan Moody, Thomas S. Gilmore, Brendan F. |
author_facet | Kelly, Stephen A. Mix, Stefan Moody, Thomas S. Gilmore, Brendan F. |
author_sort | Kelly, Stephen A. |
collection | PubMed |
description | ABSTRACT: Transaminases (TAms) are important enzymes for the production of chiral amines for the pharmaceutical and fine chemical industries. Novel TAms for use in these industries have been discovered using a range of approaches, including activity-guided methods and homologous sequence searches from cultured microorganisms to searches using key motifs and metagenomic mining of environmental DNA libraries. This mini-review focuses on the methods used for TAm discovery over the past two decades, analyzing the changing trends in the field and highlighting the advantages and drawbacks of the respective approaches used. This review will also discuss the role of protein engineering in the development of novel TAms and explore possible directions for future TAm discovery for application in industrial biocatalysis. KEY POINTS: • The past two decades of TAm enzyme discovery approaches are explored. • TAm sequences are phylogenetically analyzed and compared to other discovery methods. • Benefits and drawbacks of discovery approaches for novel biocatalysts are discussed. • The role of protein engineering and future discovery directions is highlighted. |
format | Online Article Text |
id | pubmed-7228992 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Springer Berlin Heidelberg |
record_format | MEDLINE/PubMed |
spelling | pubmed-72289922020-05-18 Transaminases for industrial biocatalysis: novel enzyme discovery Kelly, Stephen A. Mix, Stefan Moody, Thomas S. Gilmore, Brendan F. Appl Microbiol Biotechnol Mini-Review ABSTRACT: Transaminases (TAms) are important enzymes for the production of chiral amines for the pharmaceutical and fine chemical industries. Novel TAms for use in these industries have been discovered using a range of approaches, including activity-guided methods and homologous sequence searches from cultured microorganisms to searches using key motifs and metagenomic mining of environmental DNA libraries. This mini-review focuses on the methods used for TAm discovery over the past two decades, analyzing the changing trends in the field and highlighting the advantages and drawbacks of the respective approaches used. This review will also discuss the role of protein engineering in the development of novel TAms and explore possible directions for future TAm discovery for application in industrial biocatalysis. KEY POINTS: • The past two decades of TAm enzyme discovery approaches are explored. • TAm sequences are phylogenetically analyzed and compared to other discovery methods. • Benefits and drawbacks of discovery approaches for novel biocatalysts are discussed. • The role of protein engineering and future discovery directions is highlighted. Springer Berlin Heidelberg 2020-04-16 2020 /pmc/articles/PMC7228992/ /pubmed/32300853 http://dx.doi.org/10.1007/s00253-020-10585-0 Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Mini-Review Kelly, Stephen A. Mix, Stefan Moody, Thomas S. Gilmore, Brendan F. Transaminases for industrial biocatalysis: novel enzyme discovery |
title | Transaminases for industrial biocatalysis: novel enzyme discovery |
title_full | Transaminases for industrial biocatalysis: novel enzyme discovery |
title_fullStr | Transaminases for industrial biocatalysis: novel enzyme discovery |
title_full_unstemmed | Transaminases for industrial biocatalysis: novel enzyme discovery |
title_short | Transaminases for industrial biocatalysis: novel enzyme discovery |
title_sort | transaminases for industrial biocatalysis: novel enzyme discovery |
topic | Mini-Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7228992/ https://www.ncbi.nlm.nih.gov/pubmed/32300853 http://dx.doi.org/10.1007/s00253-020-10585-0 |
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