Serial increase in the thermal stability of 3‐isopropylmalate dehydrogenase from Bacillus subtilis by experimental evolution
Author:
Affiliation:
1. Department of Molecular Biology, Tokyo University of Pharmacy and Life Science, Horinouchi, Hachioji 192‐03, Japan
2. Department of Life Science, Tokyo Institute of Technology, Nagatsuta, Midori‐ku, Yokohama 226, Japan
Funder
Science and Technology Center
University of Washington
Publisher
Wiley
Subject
Molecular Biology,Biochemistry
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.5560070319
Reference38 articles.
1. Spontaneous tandem sequence duplications reverse the thermal stability of carboxyl-terminal modified 3-isopropylmalate dehydrogenase
2. High Resistance of Escherichia coli Ribonuclease HI Variant with Quintuple Thermostabilizing Mutations to Thermal Denaturation, Acid Denaturation, and Proteolytic Degradation
3. Evolutionary molecular engineering based on RNA replication
4. Amino Acid Sequence Determinants of β-Lactamase Structure and Activity
5. Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2 Å resolution
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