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Volumn 3, Issue 4, 1999, Pages 259-262

Studies on interdomain interaction of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus, by constructing chimeric enzymes

Author keywords

3 lsopropylmalate dehydrogenase; Chimeric proteins; Differential scanning calorimetry; Interdomain interaction; Thermophilic enzymes; Thermostability; Thermus thermophilus

Indexed keywords

3 ISOPROPYLMALATE DEHYDROGENASE; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; BACTERIAL GENE; CHIMERA; ENZYME CONFORMATION; ENZYME DENATURATION; ENZYME STABILITY; ENZYME SYNTHESIS; PROTEIN INTERACTION; THERMAL DENATURATION;

EID: 0033226828     PISSN: 14310651     EISSN: None     Source Type: Journal    
DOI: 10.1007/s007920050125     Document Type: Article
Times cited : (5)

References (6)
  • 1
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    • Hayashi-Iwasaki Y, Numata K, Yamagishi Y, Yutani K, Sakurai M, Tanaka N, Oshima T (1996) A stable intermediate in the thermal unfolding process of a chimeric 3-isopropylmalate dehydrogenase between a thermophilic and a mesophilic enzymes. Protein Sci 5:511-516
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    • Hayashi-Iwasaki, Y.1    Numata, K.2    Yamagishi, Y.3    Yutani, K.4    Sakurai, M.5    Tanaka, N.6    Oshima, T.7
  • 2
    • 0026334204 scopus 로고
    • Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2 Å resolution
    • Imada K, Sato M, Tanaka N, Katsube Y, Matsuura Y, Oshima T (1991) Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2 Å resolution. J Mol Biol 222:725-738
    • (1991) J Mol Biol , vol.222 , pp. 725-738
    • Imada, K.1    Sato, M.2    Tanaka, N.3    Katsube, Y.4    Matsuura, Y.5    Oshima, T.6
  • 3
    • 0028986679 scopus 로고
    • Thermal stability of chimeric isopropylmalate dehydrogenase genes constructed from a thermophile and a mesophile
    • Naumata K, Muro M, Akutsu N, Nosoh Y, Yamagishi A, Oshima T (1995) Thermal stability of chimeric isopropylmalate dehydrogenase genes constructed from a thermophile and a mesophile. Protein Eng 8:39-43
    • (1995) Protein Eng , vol.8 , pp. 39-43
    • Naumata, K.1    Muro, M.2    Akutsu, N.3    Nosoh, Y.4    Yamagishi, A.5    Oshima, T.6
  • 4
    • 0028221519 scopus 로고
    • Three-dimensional structure of chimeric enzymes between Bacillus subtilis and Thermus thermophilus 3-isopropylmalate dehydrogenases
    • Onodera K, Sakurai M, Tanaka N, Numata K, Yamagishi A, Oshima T, Sato M, Katsube Y (1994) Three-dimensional structure of chimeric enzymes between Bacillus subtilis and Thermus thermophilus 3-isopropylmalate dehydrogenases. Protein Eng 7:453-459
    • (1994) Protein Eng , vol.7 , pp. 453-459
    • Onodera, K.1    Sakurai, M.2    Tanaka, N.3    Numata, K.4    Yamagishi, A.5    Oshima, T.6    Sato, M.7    Katsube, Y.8
  • 5
    • 0019888515 scopus 로고
    • Comparative thermodynamic study of pepsinogen and pepsin structure
    • Privalov PL, Mateo PL, Khechinashvili NK (1981) Comparative thermodynamic study of pepsinogen and pepsin structure. J Mol Biol 152:445-464
    • (1981) J Mol Biol , vol.152 , pp. 445-464
    • Privalov, P.L.1    Mateo, P.L.2    Khechinashvili, N.K.3
  • 6
    • 0025108577 scopus 로고
    • Purification, catalytic properties, and thermal stability of threo-Ds-3-isopropylmalate dehydrogenase coded by leuB gene from an extreme thermophile, Thermus thermophilus strain HB8
    • Yamada T, Akutsu N, Miyazaki K, Kakinuma K, Yoshida M. Oshima T (1990) Purification, catalytic properties, and thermal stability of threo-Ds-3-isopropylmalate dehydrogenase coded by leuB gene from an extreme thermophile, Thermus thermophilus strain HB8. J Biochem (Tokyo) 108:449-456
    • (1990) J Biochem (Tokyo) , vol.108 , pp. 449-456
    • Yamada, T.1    Akutsu, N.2    Miyazaki, K.3    Kakinuma, K.4    Yoshida, M.5    Oshima, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.