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LOVely enzymes – towards engineering light‐controllable biocatalysts

Light control over enzyme function represents a novel and exciting field of biocatalysis research. Blue‐light photoreceptors of the Light, Oxygen, Voltage (LOV) family have recently been investigated for their applicability as photoactive switches. We discuss here the primary photochemical events le...

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Detalles Bibliográficos
Autores principales: Krauss, Ulrich, Lee, Jeeyeon, Benkovic, Stephen J., Jaeger, Karl‐Erich
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Blackwell Publishing Ltd 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3815943/
https://www.ncbi.nlm.nih.gov/pubmed/21255302
http://dx.doi.org/10.1111/j.1751-7915.2009.00140.x
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author Krauss, Ulrich
Lee, Jeeyeon
Benkovic, Stephen J.
Jaeger, Karl‐Erich
author_facet Krauss, Ulrich
Lee, Jeeyeon
Benkovic, Stephen J.
Jaeger, Karl‐Erich
author_sort Krauss, Ulrich
collection PubMed
description Light control over enzyme function represents a novel and exciting field of biocatalysis research. Blue‐light photoreceptors of the Light, Oxygen, Voltage (LOV) family have recently been investigated for their applicability as photoactive switches. We discuss here the primary photochemical events leading to light activation of LOV domains as well as the proposed signal propagation mechanism to the respective effector domain. Furthermore, we describe the construction of LOV fusions to different effector domains, namely a dihydrofolate reductase from Escherichia coli and a lipase from Bacillus subtilis. Both fusion partners retained functionality, and alteration of enzyme activity by light was also demonstrated. Hence, it appears that fusion of LOV photoreceptors to functional enzyme target sites via appropriate linker structures may represent a straightforward strategy to design light controllable biocatalysts.
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spelling pubmed-38159432014-02-13 LOVely enzymes – towards engineering light‐controllable biocatalysts Krauss, Ulrich Lee, Jeeyeon Benkovic, Stephen J. Jaeger, Karl‐Erich Microb Biotechnol Minireview Light control over enzyme function represents a novel and exciting field of biocatalysis research. Blue‐light photoreceptors of the Light, Oxygen, Voltage (LOV) family have recently been investigated for their applicability as photoactive switches. We discuss here the primary photochemical events leading to light activation of LOV domains as well as the proposed signal propagation mechanism to the respective effector domain. Furthermore, we describe the construction of LOV fusions to different effector domains, namely a dihydrofolate reductase from Escherichia coli and a lipase from Bacillus subtilis. Both fusion partners retained functionality, and alteration of enzyme activity by light was also demonstrated. Hence, it appears that fusion of LOV photoreceptors to functional enzyme target sites via appropriate linker structures may represent a straightforward strategy to design light controllable biocatalysts. Blackwell Publishing Ltd 2010-01 2009-12-20 /pmc/articles/PMC3815943/ /pubmed/21255302 http://dx.doi.org/10.1111/j.1751-7915.2009.00140.x Text en Copyright © 2009 The Authors. Journal compilation © 2009 Society for Applied Microbiology and Blackwell Publishing Ltd
spellingShingle Minireview
Krauss, Ulrich
Lee, Jeeyeon
Benkovic, Stephen J.
Jaeger, Karl‐Erich
LOVely enzymes – towards engineering light‐controllable biocatalysts
title LOVely enzymes – towards engineering light‐controllable biocatalysts
title_full LOVely enzymes – towards engineering light‐controllable biocatalysts
title_fullStr LOVely enzymes – towards engineering light‐controllable biocatalysts
title_full_unstemmed LOVely enzymes – towards engineering light‐controllable biocatalysts
title_short LOVely enzymes – towards engineering light‐controllable biocatalysts
title_sort lovely enzymes – towards engineering light‐controllable biocatalysts
topic Minireview
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3815943/
https://www.ncbi.nlm.nih.gov/pubmed/21255302
http://dx.doi.org/10.1111/j.1751-7915.2009.00140.x
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