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Towards Rational Computational Engineering of Psychrophilic Enzymes
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Computational Biology and Bioinformatics.
UiT Arctic Univ Norway, Hylleraas Ctr Quantum Mol Sci, Dept Chem, N-9037 Tromso, Norway.
UiT Arctic Univ Norway, Hylleraas Ctr Quantum Mol Sci, Dept Chem, N-9037 Tromso, Norway.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Computational Biology and Bioinformatics. UiT Arctic Univ Norway, Hylleraas Ctr Quantum Mol Sci, Dept Chem, N-9037 Tromso, Norway.ORCID iD: 0000-0003-2091-0610
2019 (English)In: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 9, article id 19147Article in journal (Refereed) Published
Abstract [en]

Cold-adapted enzymes from psychrophilic species achieve their high catalytic efficiency at low temperature by a different partitioning of the activation free energy into its enthalpic and entropic components, compared to orthologous mesophilic enzymes. Their lower activation enthalpy, partly compensated by an increased entropic penalty, has been suggested to originate from changes in flexibility of the protein surface. Multiple sequence alignments of psychrophilic and mesophilic enzymes also show characteristic motifs located in surface loops of the protein. Here, we use computer simulations to examine the effects of a number of designed surface mutations of psychrophilic and mesophilic elastases on the temperature dependence of the catalyzed peptide cleavage reaction. For each of 14 mutant enzyme variants we report calculations of their thermodynamic activation parameters. The results show that substitution of psychrophilic loop residues into the mesophilic enzyme consistently changes both the activation parameters and loop flexibilities towards the former, and vice versa for opposite substitutions.

Place, publisher, year, edition, pages
NATURE PUBLISHING GROUP , 2019. Vol. 9, article id 19147
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Biochemistry and Molecular Biology
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URN: urn:nbn:se:uu:diva-402233DOI: 10.1038/s41598-019-55697-4ISI: 000503186000003PubMedID: 31844096OAI: oai:DiVA.org:uu-402233DiVA, id: diva2:1386159
Funder
Swedish Research CouncilKnut and Alice Wallenberg FoundationThe Research Council of NorwayAvailable from: 2020-01-16 Created: 2020-01-16 Last updated: 2020-03-17Bibliographically approved
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