Thermostabilization of a chimeric enzyme by residue substitutions: Four amino acid residues in loop regions are responsible for the thermostability of Thermus thermophilus isopropylmalate dehydrogenase

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1545, Issue 1-2, 2001, Pages 174-183

  Numata, Koichi ^a   Hayashi Iwasaki, Yoko ^b   Kawaguchi, Jitsutaro ^a   Sakurai, Masahiro ^a   Moriyama, Hideaki ^a   Tanaka, Nobuo ^a   Oshima, Tairo ^b  

^a TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

^b TOKYO UNIVERSITY OF PHARMACY AND LIFE SCIENCES   (Japan)

Author keywords

3 Isopropylmalate dehydrogenase; Chimera; Protein stability; Site directed mutagenesis; Thermus thermophilus

Indexed keywords

3 ISOPROPYLMALATE DEHYDROGENASE; AMINO ACID; CHIMERIC PROTEIN;

ARTICLE; BACILLUS SUBTILIS; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME DENATURATION; ENZYME STABILITY; NONHUMAN; PRIORITY JOURNAL; REACTION ANALYSIS; SITE DIRECTED MUTAGENESIS; THERMOSTABILITY; THERMUS THERMOPHILUS;

3-ISOPROPYLMALATE DEHYDROGENASE; ALCOHOL OXIDOREDUCTASES; ARGININE; BACILLUS SUBTILIS; BACTERIAL PROTEINS; CHEMISTRY, PHYSICAL; ELECTROSTATICS; GLYCINE; HEAT; LEUCINE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN DENATURATION; RECOMBINANT FUSION PROTEINS; THERMUS THERMOPHILUS;

BACILLUS SUBTILIS; THERMUS THERMOPHILUS;

EID: 0035830685     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(00)00275-2     Document Type: Article

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