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Title: Catalysis, dynamics and stability of enzymes under extreme conditions

Abstract

This project led to an unprecedented understanding of how enzymes can catalyze chemical reactions with such high catalytic turnover numbers. This was achieved by a detailed description of the free energy landscape of adenylate kinase using a combination of experimental atomic resolution techniques and computation. In this project, a systematic approach was developed how to characterize free energy landscapes with these biophysical methods. These approaches are directly transferable to other enzymes. In addition, we recreated the evolutionary pathway of enzyme evolution over about 3.5 billion years. The results shed light into how enzymes adapted to the decrease in temperature by increasing their catalytic power at lower temperatures. The data demonstrate fundamental principles of evolution such as active pressure versus passive drift. The adaptation of biocatalyst to extreme conditions such as high or low temperature, pressure (living deep at sea) or high salt was studied. Lessons learned from this project have major implications for catalysis in biotechnology.

Authors:
ORCiD logo [1]
  1. Brandeis University, Waltham, MA (United States)
Publication Date:
Research Org.:
Brandeis Univ., Waltham, MA (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1409299
Report Number(s):
DOE-BRANDEIS-15699
DOE Contract Number:  
FG02-05ER15699
Resource Type:
Technical Report
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY

Citation Formats

Kern, Dorothee. Catalysis, dynamics and stability of enzymes under extreme conditions. United States: N. p., 2017. Web. doi:10.2172/1409299.
Kern, Dorothee. Catalysis, dynamics and stability of enzymes under extreme conditions. United States. doi:10.2172/1409299.
Kern, Dorothee. Thu . "Catalysis, dynamics and stability of enzymes under extreme conditions". United States. doi:10.2172/1409299. https://www.osti.gov/servlets/purl/1409299.
@article{osti_1409299,
title = {Catalysis, dynamics and stability of enzymes under extreme conditions},
author = {Kern, Dorothee},
abstractNote = {This project led to an unprecedented understanding of how enzymes can catalyze chemical reactions with such high catalytic turnover numbers. This was achieved by a detailed description of the free energy landscape of adenylate kinase using a combination of experimental atomic resolution techniques and computation. In this project, a systematic approach was developed how to characterize free energy landscapes with these biophysical methods. These approaches are directly transferable to other enzymes. In addition, we recreated the evolutionary pathway of enzyme evolution over about 3.5 billion years. The results shed light into how enzymes adapted to the decrease in temperature by increasing their catalytic power at lower temperatures. The data demonstrate fundamental principles of evolution such as active pressure versus passive drift. The adaptation of biocatalyst to extreme conditions such as high or low temperature, pressure (living deep at sea) or high salt was studied. Lessons learned from this project have major implications for catalysis in biotechnology.},
doi = {10.2172/1409299},
journal = {},
number = ,
volume = ,
place = {United States},
year = {2017},
month = {11}
}