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Engineering Non-Heme Mono- and Dioxygenases for Biocatalysis

Oxygenases are ubiquitous enzymes that catalyze the introduction of one or two oxygen atoms to unreactive chemical compounds. They require reduction equivalents from NADH or NADPH and comprise metal ions, metal ion complexes, or coenzymes in their active site. Thus, for industrial purposes, oxygenas...

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Detalles Bibliográficos
Autores principales: Dror, Adi, Fishman, Ayelet
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Research Network of Computational and Structural Biotechnology (RNCSB) Organization 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3962191/
https://www.ncbi.nlm.nih.gov/pubmed/24688652
http://dx.doi.org/10.5936/csbj.201209011
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author Dror, Adi
Fishman, Ayelet
author_facet Dror, Adi
Fishman, Ayelet
author_sort Dror, Adi
collection PubMed
description Oxygenases are ubiquitous enzymes that catalyze the introduction of one or two oxygen atoms to unreactive chemical compounds. They require reduction equivalents from NADH or NADPH and comprise metal ions, metal ion complexes, or coenzymes in their active site. Thus, for industrial purposes, oxygenases are most commonly employed using whole cell catalysis, to alleviate the need for co-factor regeneration. Biotechnological applications include bioremediation, chiral synthesis, biosensors, fine chemicals, biofuels, pharmaceuticals, food ingredients and polymers. Controlling activity and selectivity of oxygenases is therefore of great importance and of growing interest to the scientific community. This review focuses on protein engineering of non-heme monooxygenases and dioxygenases for generating improved or novel functionalities. Rational mutagenesis based on x-ray structures and sequence alignment, as well as random methods such as directed evolution, have been utilized. It is concluded that knowledge-based protein engineering accompanied with targeted libraries, is most efficient for the design and tuning of biocatalysts towards novel substrates and enhanced catalytic activity while minimizing the screening efforts.
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spelling pubmed-39621912014-03-31 Engineering Non-Heme Mono- and Dioxygenases for Biocatalysis Dror, Adi Fishman, Ayelet Comput Struct Biotechnol J Mini Review Oxygenases are ubiquitous enzymes that catalyze the introduction of one or two oxygen atoms to unreactive chemical compounds. They require reduction equivalents from NADH or NADPH and comprise metal ions, metal ion complexes, or coenzymes in their active site. Thus, for industrial purposes, oxygenases are most commonly employed using whole cell catalysis, to alleviate the need for co-factor regeneration. Biotechnological applications include bioremediation, chiral synthesis, biosensors, fine chemicals, biofuels, pharmaceuticals, food ingredients and polymers. Controlling activity and selectivity of oxygenases is therefore of great importance and of growing interest to the scientific community. This review focuses on protein engineering of non-heme monooxygenases and dioxygenases for generating improved or novel functionalities. Rational mutagenesis based on x-ray structures and sequence alignment, as well as random methods such as directed evolution, have been utilized. It is concluded that knowledge-based protein engineering accompanied with targeted libraries, is most efficient for the design and tuning of biocatalysts towards novel substrates and enhanced catalytic activity while minimizing the screening efforts. Research Network of Computational and Structural Biotechnology (RNCSB) Organization 2012-10-23 /pmc/articles/PMC3962191/ /pubmed/24688652 http://dx.doi.org/10.5936/csbj.201209011 Text en © Dror and Fishman. 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
Dror, Adi
Fishman, Ayelet
Engineering Non-Heme Mono- and Dioxygenases for Biocatalysis
title Engineering Non-Heme Mono- and Dioxygenases for Biocatalysis
title_full Engineering Non-Heme Mono- and Dioxygenases for Biocatalysis
title_fullStr Engineering Non-Heme Mono- and Dioxygenases for Biocatalysis
title_full_unstemmed Engineering Non-Heme Mono- and Dioxygenases for Biocatalysis
title_short Engineering Non-Heme Mono- and Dioxygenases for Biocatalysis
title_sort engineering non-heme mono- and dioxygenases for biocatalysis
topic Mini Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3962191/
https://www.ncbi.nlm.nih.gov/pubmed/24688652
http://dx.doi.org/10.5936/csbj.201209011
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