Spontaneous tandem sequence duplications reverse the thermal stability of carboxyl-terminal modified 3-isopropylmalate dehydrogenase
Author:
Affiliation:
1. Department of Life Science, Tokyo Institute of Technology, Yokohama, Japan. akanuma@ls.toyaku.ac.jp.
Abstract
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Link
https://journals.asm.org/doi/pdf/10.1128/jb.178.21.6300-6304.1996
Reference19 articles.
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2. Changes in the substrate specificities of an enzyme during directed evolution of new functions;Hall B. G.;Biochemistry,1981
3. Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2 Å resolution;Imada K.;J. Mol. Biol.,1991
4. High guanine plus cytosine content in the third letter of codons of an extreme thermophile;Kagawa Y.;J. Biol. Chem.,1984
5. Hydrophobic interaction at the subunit interface contributes to the thermal stability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus;Kirino H.;Eur. J. Biochem.,1994
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3. Rates of Unfolding, Rather than Refolding, Determine Thermal Stabilities of Thermophilic, Mesophilic, and Psychrotrophic 3-Isopropylmalate Dehydrogenases;Biochemistry;2007-09-22
4. Selection of stabilized 3-isopropylmalate dehydrogenase of Saccharomyces cerevisiae using the host-vector system of an extreme thermophile, Thermus thermophilus;Extremophiles;2001-02
5. Crystal structures of 3-isopropylmalate dehydrogenases with mutations at the C-terminus: crystallographic analyses of structure–stability relationships;Protein Engineering, Design and Selection;2000-04
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