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Towards Rational Computational Engineering of Psychrophilic Enzymes.

Jaka Sočan1, Geir Villy Isaksen2, Bjørn Olav Brandsdal2

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Cold-adapted enzymes use different energy partitioning for low-temperature catalysis. Surface loop mutations in elastases alter flexibility and thermodynamic activation parameters, mimicking cold adaptation.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Structural Biology

Background:

  • Psychrophilic enzymes exhibit high catalytic efficiency at low temperatures, differing from mesophilic counterparts in activation free energy partitioning.
  • This adaptation is linked to altered protein surface flexibility and characteristic sequence motifs in surface loops.

Purpose of the Study:

  • To investigate the impact of specific surface mutations on the temperature dependence of enzyme catalysis.
  • To examine how substituting residues between psychrophilic and mesophilic elastases affects their thermodynamic activation parameters and loop flexibility.

Main Methods:

  • Utilizing computer simulations to model 14 designed mutant enzyme variants of psychrophilic and mesophilic elastases.
  • Calculating thermodynamic activation parameters for the catalyzed peptide cleavage reaction under varying temperatures.

Main Results:

  • Mutations introducing psychrophilic loop residues into mesophilic elastases shifted activation parameters and loop flexibility towards psychrophilic characteristics.
  • Conversely, substituting mesophilic residues into psychrophilic elastases induced changes towards mesophilic properties.

Conclusions:

  • Surface loop flexibility plays a crucial role in the cold adaptation of enzyme catalysis.
  • Designed mutations can effectively modulate enzyme activity and thermodynamic properties, providing insights into enzyme evolution and engineering.