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The Versatile Biocatalyst of Cytochrome P450 CYP102A1: Structure, Function, and Engineering
Wild-type cytochrome P450 CYP102A1 from Bacillus megaterium is a highly efficient monooxygenase for the oxidation of long-chain fatty acids. The unique features of CYP102A1, such as high catalytic activity, expression yield, regio- and stereoselectivity, and self-sufficiency in electron transfer as...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10383305/ https://www.ncbi.nlm.nih.gov/pubmed/37513226 http://dx.doi.org/10.3390/molecules28145353 |
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author | Sun, Yudong Huang, Xiaoqiang Osawa, Yoichi Chen, Yuqing Eugene Zhang, Haoming |
author_facet | Sun, Yudong Huang, Xiaoqiang Osawa, Yoichi Chen, Yuqing Eugene Zhang, Haoming |
author_sort | Sun, Yudong |
collection | PubMed |
description | Wild-type cytochrome P450 CYP102A1 from Bacillus megaterium is a highly efficient monooxygenase for the oxidation of long-chain fatty acids. The unique features of CYP102A1, such as high catalytic activity, expression yield, regio- and stereoselectivity, and self-sufficiency in electron transfer as a fusion protein, afford the requirements for an ideal biocatalyst. In the past three decades, remarkable progress has been made in engineering CYP102A1 for applications in drug discovery, biosynthesis, and biotechnology. The repertoire of engineered CYP102A1 variants has grown tremendously, whereas the substrate repertoire is avalanched to encompass alkanes, alkenes, aromatics, organic solvents, pharmaceuticals, drugs, and many more. In this article, we highlight the major advances in the past five years in our understanding of the structure and function of CYP102A1 and the methodologies used to engineer CYP102A1 for novel applications. The objective is to provide a succinct review of the latest developments with reference to the body of CYP102A1-related literature. |
format | Online Article Text |
id | pubmed-10383305 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-103833052023-07-30 The Versatile Biocatalyst of Cytochrome P450 CYP102A1: Structure, Function, and Engineering Sun, Yudong Huang, Xiaoqiang Osawa, Yoichi Chen, Yuqing Eugene Zhang, Haoming Molecules Review Wild-type cytochrome P450 CYP102A1 from Bacillus megaterium is a highly efficient monooxygenase for the oxidation of long-chain fatty acids. The unique features of CYP102A1, such as high catalytic activity, expression yield, regio- and stereoselectivity, and self-sufficiency in electron transfer as a fusion protein, afford the requirements for an ideal biocatalyst. In the past three decades, remarkable progress has been made in engineering CYP102A1 for applications in drug discovery, biosynthesis, and biotechnology. The repertoire of engineered CYP102A1 variants has grown tremendously, whereas the substrate repertoire is avalanched to encompass alkanes, alkenes, aromatics, organic solvents, pharmaceuticals, drugs, and many more. In this article, we highlight the major advances in the past five years in our understanding of the structure and function of CYP102A1 and the methodologies used to engineer CYP102A1 for novel applications. The objective is to provide a succinct review of the latest developments with reference to the body of CYP102A1-related literature. MDPI 2023-07-12 /pmc/articles/PMC10383305/ /pubmed/37513226 http://dx.doi.org/10.3390/molecules28145353 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Sun, Yudong Huang, Xiaoqiang Osawa, Yoichi Chen, Yuqing Eugene Zhang, Haoming The Versatile Biocatalyst of Cytochrome P450 CYP102A1: Structure, Function, and Engineering |
title | The Versatile Biocatalyst of Cytochrome P450 CYP102A1: Structure, Function, and Engineering |
title_full | The Versatile Biocatalyst of Cytochrome P450 CYP102A1: Structure, Function, and Engineering |
title_fullStr | The Versatile Biocatalyst of Cytochrome P450 CYP102A1: Structure, Function, and Engineering |
title_full_unstemmed | The Versatile Biocatalyst of Cytochrome P450 CYP102A1: Structure, Function, and Engineering |
title_short | The Versatile Biocatalyst of Cytochrome P450 CYP102A1: Structure, Function, and Engineering |
title_sort | versatile biocatalyst of cytochrome p450 cyp102a1: structure, function, and engineering |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10383305/ https://www.ncbi.nlm.nih.gov/pubmed/37513226 http://dx.doi.org/10.3390/molecules28145353 |
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