Data underlying the chapter Mechanistic insights in Lactobacillus brevis alcohol dehydrogenase: stability and active site role of Ser143 and Tyr156

doi:10.4121/af778919-5f7a-4b39-ae6d-92b563d44063.v1
The doi above is for this specific version of this dataset, which is currently the latest. Newer versions may be published in the future. For a link that will always point to the latest version, please use
doi: 10.4121/af778919-5f7a-4b39-ae6d-92b563d44063
Datacite citation style:
Jongkind, Ewald; Kools, Wouter; Pareek, Monika; Kamerlin, Lynn; Paul, Caroline (2024): Data underlying the chapter Mechanistic insights in Lactobacillus brevis alcohol dehydrogenase: stability and active site role of Ser143 and Tyr156. Version 1. 4TU.ResearchData. dataset. https://doi.org/10.4121/af778919-5f7a-4b39-ae6d-92b563d44063.v1
Other citation styles (APA, Harvard, MLA, Vancouver, Chicago, IEEE) available at Datacite
Dataset

This dataset contains data collected during experiments at Delft University of Technology, as chapter of the dissertation written by Ewald Jongkind. The aim of this work was to engineer an alcohol dehydrogenase from Lactobacillus brevis (LbADH), to enable reductive amination with this enzyme. Method consisted of docking studies of energy-minimized mutant enzymes designed with FuncLib, purifying these enzymes and screening the mutant enzymes for reductive amination. Dataset includes output files from the algorithm FuncLib, DNA sequences of the single mutant LbADHs, SDS-PAGEs showing the purification of all enzymes and the reaction screenings and activites of the enzymes, determined by UV-VIS, calculated in Excel. Dataset includes a draft Supporting information accompanied with the raw data used for this work.

history
  • 2024-08-02 first online, published, posted
publisher
4TU.ResearchData
format
.xlsx, .docx, .txt, .pdf, .cm5, .pptx, .pdb, .csv
organizations
TU Delft, Faculty of Applied Sciences, Department of Biotechnology;
Uppsala University, Department of Chemistry

DATA

files (7)