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bioRxiv · 10.1101/2020.11.17.387829

Design to Data for mutants of β-glucosidase B from Paenibacillus polymyxa: L171M, H178M, M221L, E406W, N160E, F415M

Huang, X.·Kim, D. S.·Huang, P.·Vater, A. W.·Siegel, J. B.
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Abstract

Computational protein design is growing in popularity as a means to engineer enzymes. Currently, protein design algorithms can predict the stability and function of the enzymes to only a limited degree. Thus, further experimental data is required for training software to more accurately characterize the structure-function relationship of enzymes. To date, the Design2Data (D2D) database holds 129 single point mutations of {beta}-glucosidase B (BglB) characterized by kinetic and thermal stability biophysical parameters. In this study, we introduced six mutants into the BglB database and examined their catalytic activity and thermal stability: L171M, H178M, M221L, E406W, N160E, and F415M.

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Huang, X., Kim, D. S., Huang, P., Vater, A. W., Siegel, J. B.. 2020-11-18. Design to Data for mutants of β-glucosidase B from Paenibacillus polymyxa: L171M, H178M, M221L, E406W, N160E, F415M. https://doi.org/10.1101/2020.11.17.387829

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