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Genetically engineered proteins with two active sites for enhanced biocatalysis and synergistic chemo- and biocatalysis

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Genetically engineered proteins with two active sites for enhanced biocatalysis and synergistic chemo- and biocatalysis. / Alonso, Sandra; Santiago, Gerard; Cea-Rama, Isabel et al.
In: Nature Catalysis, Vol. 3, No. 3, 03.2020, p. 319-328.

Research output: Contribution to journal › Article › peer-review

HarvardHarvard

Alonso, S, Santiago, G, Cea-Rama, I, Fernandez-Lopez, L, Coscolín, C, Modregger, J, Ressmann, AK, Martinez-Martinez, M, Marrero, H, Bargiela, R, Pita, M, Gonzalez-Alfonso, JL, Briand, ML, Rojo, D, Barbas, C, Plou, FJ, Golyshin, P, Shahgaldian, P, Sanz-Aparicio, J, Guallar, V & Ferrer, M 2020, 'Genetically engineered proteins with two active sites for enhanced biocatalysis and synergistic chemo- and biocatalysis', Nature Catalysis, vol. 3, no. 3, pp. 319-328. https://doi.org/10.1038/s41929-019-0394-4

APA

Alonso, S., Santiago, G., Cea-Rama, I., Fernandez-Lopez, L., Coscolín, C., Modregger, J., Ressmann, A. K., Martinez-Martinez, M., Marrero, H., Bargiela, R., Pita, M., Gonzalez-Alfonso, J. L., Briand, M. L., Rojo, D., Barbas, C., Plou, F. J., Golyshin, P., Shahgaldian, P., Sanz-Aparicio, J., ... Ferrer, M. (2020). Genetically engineered proteins with two active sites for enhanced biocatalysis and synergistic chemo- and biocatalysis. Nature Catalysis, 3(3), 319-328. https://doi.org/10.1038/s41929-019-0394-4

CBE

Alonso S, Santiago G, Cea-Rama I, Fernandez-Lopez L, Coscolín C, Modregger J, Ressmann AK, Martinez-Martinez M, Marrero H, Bargiela R, et al. 2020. Genetically engineered proteins with two active sites for enhanced biocatalysis and synergistic chemo- and biocatalysis. Nature Catalysis. 3(3):319-328. https://doi.org/10.1038/s41929-019-0394-4

MLA

Alonso, Sandra et al. "Genetically engineered proteins with two active sites for enhanced biocatalysis and synergistic chemo- and biocatalysis". Nature Catalysis. 2020, 3(3). 319-328. https://doi.org/10.1038/s41929-019-0394-4

VancouverVancouver

Alonso S, Santiago G, Cea-Rama I, Fernandez-Lopez L, Coscolín C, Modregger J et al. Genetically engineered proteins with two active sites for enhanced biocatalysis and synergistic chemo- and biocatalysis. Nature Catalysis. 2020 Mar;3(3):319-328. Epub 2019 Dec 16. doi: 10.1038/s41929-019-0394-4

Author

Alonso, Sandra ; Santiago, Gerard ; Cea-Rama, Isabel et al. / Genetically engineered proteins with two active sites for enhanced biocatalysis and synergistic chemo- and biocatalysis. In: Nature Catalysis. 2020 ; Vol. 3, No. 3. pp. 319-328.

RIS

TY - JOUR

T1 - Genetically engineered proteins with two active sites for enhanced biocatalysis and synergistic chemo- and biocatalysis

AU - Alonso, Sandra

AU - Santiago, Gerard

AU - Cea-Rama, Isabel

AU - Fernandez-Lopez, Laura

AU - Coscolín, Cristina

AU - Modregger, Jan

AU - Ressmann, Anna K.

AU - Martinez-Martinez, Monica

AU - Marrero, Helena

AU - Bargiela, Rafael

AU - Pita, Marcos

AU - Gonzalez-Alfonso, Jose L.

AU - Briand, Manon L.

AU - Rojo, David

AU - Barbas, Coral

AU - Plou, Francisco J

AU - Golyshin, Peter

AU - Shahgaldian, Patrick

AU - Sanz-Aparicio, Julia

AU - Guallar, Víctor

AU - Ferrer, Manuel

PY - 2020/3

Y1 - 2020/3

N2 - Enzyme engineering has allowed not only the de novo creation of active sites catalysing known biological reactions with rates close to diffusion limits, but also the generation of abiological sites performing new-to-nature reactions. However, the catalytic advantages of engineering multiple active sites into a single protein scaffold are yet to be established. Here, we report on proteins with two active sites of biological and/or abiological origin, for improved natural and non-natural catalysis. The approach increased the catalytic properties, such as enzyme efficiency, substrate scope, stereoselectivity and optimal temperature window, of an esterase containing two biological sites. Then, one of the active sites was metamorphosed into a metal-complex chemocatalytic site for oxidation and Friedel–Crafts alkylation reactions, facilitating synergistic chemo- and biocatalysis in a single protein. The transformations of 1-naphthyl acetate into 1,4-naphthoquinone (conversion approx. 100%) and vinyl crotonate and benzene into 3-phenylbutyric acid (≥83%; e.e. >99.9%) were achieved in one pot with this artificial multifunctional metalloenzyme.

AB - Enzyme engineering has allowed not only the de novo creation of active sites catalysing known biological reactions with rates close to diffusion limits, but also the generation of abiological sites performing new-to-nature reactions. However, the catalytic advantages of engineering multiple active sites into a single protein scaffold are yet to be established. Here, we report on proteins with two active sites of biological and/or abiological origin, for improved natural and non-natural catalysis. The approach increased the catalytic properties, such as enzyme efficiency, substrate scope, stereoselectivity and optimal temperature window, of an esterase containing two biological sites. Then, one of the active sites was metamorphosed into a metal-complex chemocatalytic site for oxidation and Friedel–Crafts alkylation reactions, facilitating synergistic chemo- and biocatalysis in a single protein. The transformations of 1-naphthyl acetate into 1,4-naphthoquinone (conversion approx. 100%) and vinyl crotonate and benzene into 3-phenylbutyric acid (≥83%; e.e. >99.9%) were achieved in one pot with this artificial multifunctional metalloenzyme.

UR - https://static-content.springer.com/esm/art%3A10.1038%2Fs41929-019-0394-4/MediaObjects/41929_2019_394_MOESM1_ESM.pdf

U2 - 10.1038/s41929-019-0394-4

DO - 10.1038/s41929-019-0394-4

M3 - Article

VL - 3

SP - 319

EP - 328

JO - Nature Catalysis

JF - Nature Catalysis

SN - 2520-1158

IS - 3

ER -