PROJECT #16925 RESEARCH FOR UNSPECIFIED
FOLDING PERFORMANCE PROFILE
Halorubrum lacusprofundi is a microorganism found in the extremely cold and hypersaline Deep Lake, Antarctica. This microorganism has a polyextremophilic β-galactosidase that works to break down carbohydrates. Recent work from the DasSarma group identified six key amino acid residues in β-galactosidase which, when mutated with amino acids conserved in homologs from mesophilic haloarchaea, induced significant changes to the catalytic efficiency of the enzyme and its temperature dependence (1).
We are running molecular simulations of β-galactosidase and its mutated variants to explore how these subtle sequence changes affect the behavior of this enzyme at various temperatures. We will analyze the trajectory data to formulate explanations for the mechanisms that cause differences in catalytic efficiencies.
In the future, a better understanding of how evolved mutations help optimize enzyme efficiency may lead to improved methods for computational enzyme design.
- Laye, V. J., Karan, R., Kim, J.-M., Pecher, W. T., DasSarma, P., & DasSarma, S. (2017). Key amino acid residues conferring enhanced enzyme activity at cold temperatures in an Antarctic polyextremophilic β-galactosidase. Proceedings of the National Academy of Sciences of the United States of America, 114(47), 12530–12535. http://doi.org/10.1073/pnas.1711542114
Manager(s): Prof. Vincent Voelz
Institution: Temple University
PROJECT WORK UNIT SUMMARY
PROJECT FOLDING PPD AVERAGES BY CPU BETA
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