ArticleBiotechnology for biofuels2018
An iterative computational design approach to increase the thermal endurance of a mesophilic enzyme.
Article in Biotechnology for biofuels, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 16 citations in OpenAlex.
- Accurate Prediction of Enzyme Thermostabilization with Rosetta Using AlphaFold Ensembles.Journal of chemical information and modeling · 2023Article
- Computational design of noncanonical amino acid-based thioether staples at N/C-terminal domains of multi-modular pullulanase for thermostabilization in enzyme catalysis.Computational and structural biotechnology journal · 2021Article
- To beat the heat - engineering of the most thermostable pyruvate decarboxylase to date.RSC advances · 2019Article
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
Abstract
backgroundStrategies for maximizing the microbial production of bio-based chemicals and fuels include eliminating branched points to streamline metabolic pathways. While this is often achieved by removing key enzymes, the introduction of nonnative enzymes can provide metabolic shortcuts, bypassing branched points to decrease the production of undesired side-products. Pyruvate decarboxylase (PDC) can provide such a shortcut in industrially promising thermophilic organisms; yet to date, this enzyme has not been found in any thermophilic organism. Incorporating nonnative enzymes into host organisms can be challenging in cases such as this, where the enzyme has evolved in a very different environment from that of the host.
resultsIn this study, we use computational protein design to engineer the
conclusionsWe find that increases in melting temperature (
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