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Approaches to engineer stability of beetle luciferases

Luciferase enzymes from fireflies and other beetles have many important applications in molecular biology, biotechnology, analytical chemistry and several other areas. Many novel beetle luciferases with promising properties have been reported in the recent years. However, actual and potential applic...

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Autores principales: Koksharov, Mikhail I., Ugarova, Natalia N.
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/PMC3962189/
https://www.ncbi.nlm.nih.gov/pubmed/24688645
http://dx.doi.org/10.5936/csbj.201209004
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author Koksharov, Mikhail I.
Ugarova, Natalia N.
author_facet Koksharov, Mikhail I.
Ugarova, Natalia N.
author_sort Koksharov, Mikhail I.
collection PubMed
description Luciferase enzymes from fireflies and other beetles have many important applications in molecular biology, biotechnology, analytical chemistry and several other areas. Many novel beetle luciferases with promising properties have been reported in the recent years. However, actual and potential applications of wild-type beetle luciferases are often limited by insufficient stability or decrease in activity of the enzyme at the conditions of a particular assay. Various examples of genetic engineering of the enhanced beetle luciferases have been reported that successfully solve or alleviate many of these limitations. This mini-review summarizes the recent advances in development of mutant luciferases with improved stability and activity characteristics. It discusses the common limitations of wild-type luciferases in different applications and presents the efficient approaches that can be used to address these problems.
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spelling pubmed-39621892014-03-31 Approaches to engineer stability of beetle luciferases Koksharov, Mikhail I. Ugarova, Natalia N. Comput Struct Biotechnol J Mini Review Luciferase enzymes from fireflies and other beetles have many important applications in molecular biology, biotechnology, analytical chemistry and several other areas. Many novel beetle luciferases with promising properties have been reported in the recent years. However, actual and potential applications of wild-type beetle luciferases are often limited by insufficient stability or decrease in activity of the enzyme at the conditions of a particular assay. Various examples of genetic engineering of the enhanced beetle luciferases have been reported that successfully solve or alleviate many of these limitations. This mini-review summarizes the recent advances in development of mutant luciferases with improved stability and activity characteristics. It discusses the common limitations of wild-type luciferases in different applications and presents the efficient approaches that can be used to address these problems. Research Network of Computational and Structural Biotechnology (RNCSB) Organization 2012-10-09 /pmc/articles/PMC3962189/ /pubmed/24688645 http://dx.doi.org/10.5936/csbj.201209004 Text en © Koksharov and Ugarova. 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
Koksharov, Mikhail I.
Ugarova, Natalia N.
Approaches to engineer stability of beetle luciferases
title Approaches to engineer stability of beetle luciferases
title_full Approaches to engineer stability of beetle luciferases
title_fullStr Approaches to engineer stability of beetle luciferases
title_full_unstemmed Approaches to engineer stability of beetle luciferases
title_short Approaches to engineer stability of beetle luciferases
title_sort approaches to engineer stability of beetle luciferases
topic Mini Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3962189/
https://www.ncbi.nlm.nih.gov/pubmed/24688645
http://dx.doi.org/10.5936/csbj.201209004
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