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 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.
Institute of Molecular Enzyme Technology, Heinrich-Heine-University Duesseldorf, Research Centre Juelich, D-52426-Juelich, Germany.
Ulrich
U
Krauss
Jeeyeon
J
Lee
Stephen J
SJ
Benkovic
Karl-Erich
KE
Jaeger
D001412:Bacillus subtilis / Q000201:enzymology* / Q000235:genetics; D004798:Enzymes / Q000235:genetics* / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D008027:Light; D015202:Protein Engineering; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism
D004798:Enzymes; D011993:Recombinant Fusion Proteins
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