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Catalytic Adaptation of Psychrophilic Elastase
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Computational Biology and Bioinformatics.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology. Univ Tromso, Dept Chem, Hylleraas Ctr Quantum Mol Sci, N-9037 Tromso, Norway.
Univ Tromso, Dept Chem, Hylleraas Ctr Quantum Mol Sci, N-9037 Tromso, Norway.ORCID iD: 0000-0002-4681-8081
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2018 (English)In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 57, no 20, p. 2984-2993Article in journal (Refereed) Published
Abstract [en]

The class I pancreatic elastase from Atlantic salmon is considered to be a cold-adapted enzyme in view of the cold habitat, the reduced thermostability of the enzyme, and the fact that it is faster than its mesophilic porcine counterpart at room temperature. However, no experimental characterization of its catalytic properties at lower temperatures has actually been reported. Here we use extensive computer simulations of its catalytic reaction, at different temperatures and with different peptide substrates, to compare its characteristics with those of porcine pancreatic elastase, with which it shares 67% sequence identity. We find that both enzymes have a preference for smaller aliphatic residues at the P1 position, while the reaction rate with phenylalanine at P1 is predicted to be substantially lower. With the former class of substrates, the calculated reaction rates for salmon enzyme are consistently higher than those of the porcine ortholog at all temperatures examined, and the difference is most pronounced at the lowest temperature. As observed for other cold-adapted enzymes, this is caused by redistribution of the activation free energy in terms of enthalpy and entropy and can be linked to differences in the mobility of surface-exposed loops in the two enzymes. Such mobility changes are found to be reflected by characteristic sequence conservation patterns in psychrophilic and mesophilic species. Hence, calculations of mutations in a single surface loop show that the temperature dependence of the catalytic reaction is altered in a predictable way.

Place, publisher, year, edition, pages
2018. Vol. 57, no 20, p. 2984-2993
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:uu:diva-357569DOI: 10.1021/acs.biochem.8b00078ISI: 000433404600009PubMedID: 29726678OAI: oai:DiVA.org:uu-357569DiVA, id: diva2:1239734
Funder
Swedish Research CouncilKnut and Alice Wallenberg FoundationAvailable from: 2018-08-17 Created: 2018-08-17 Last updated: 2018-08-17Bibliographically approved

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Socan, JakaKazemi, MasoudÅqvist, Johan

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