ArticleScientific reports2016
Probing the role of cation-π interaction in the thermotolerance and catalytic performance of endo-polygalacturonases.
Article in Scientific reports, 2016. 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.
- CAZyme fold architecture is conserved between disparate environments despite extreme sequence divergence.mSystems · 2026Article
- Enhancing stability of enzymes for industrial applications: molecular insights and emerging approaches.World journal of microbiology & biotechnology · 2025Review
- Removal of N-terminal tail changes the thermostability of the low-temperature-active exo-inulinase InuAGN25.Bioengineered · 2020Article
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9 authors.
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Abstract
Understanding the dynamics of the key pectinase, polygalacturonase, and improving its thermotolerance and catalytic efficiency are of importance for the cost-competitive bioconversion of pectic materials. By combining structure analysis and molecular dynamics (MD) simulations, eight mutagenesis sites having the potential to form cation-π interactions were identified in the widely used fungal endo-polygalacturonase PG63. In comparison to the wild-type, three single mutants H58Y, T71Y and T304Y showed improved thermostability (the apparent T
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