메뉴 건너뛰기




Volumn 5, Issue 1, 2001, Pages 17-22

Selection of stabilized 3-isopropylmalate dehydrogenase of Saccharomyces cerevisiae using the host-vector system of an extreme thermophile, Thermus thermophilus

Author keywords

3 Isopropylmalate dehydrogenase; Evolutionary engineering; Saccharomyces cerevisiae; Thermostability; Thermus thermophilus

Indexed keywords

3 ISOPROPYLMALATE DEHYDRATASE; 3-ISOPROPYLMALATE DEHYDRATASE; GLYCEROL; HYDROLYASE; LEUCINE;

EID: 0035259956     PISSN: 14310651     EISSN: None     Source Type: Journal    
DOI: 10.1007/s007920000168     Document Type: Article
Times cited : (40)

References (28)
  • 1
    • 0029908683 scopus 로고    scopus 로고
    • Spontaneous tandem sequence duplications reverse the thermal stability of carboxyl-terminal modified 3-isopropylmalate dehydrogenase
    • Akanuma S, Yamagishi A, Tanaka N, Oshima T (1996) Spontaneous tandem sequence duplications reverse the thermal stability of carboxyl-terminal modified 3-isopropylmalate dehydrogenase. J Bacteriol 178:6300-6304
    • (1996) J Bacteriol , vol.178 , pp. 6300-6304
    • Akanuma, S.1    Yamagishi, A.2    Tanaka, N.3    Oshima, T.4
  • 2
    • 0031935580 scopus 로고    scopus 로고
    • Serial increase in the thermal stability of 3-isopropylmalate dehydrogenase from Bacillus subtilis by experimental evolution
    • Akanuma S, Yamagishi A, Tanaka N, Oshima T (1998) Serial increase in the thermal stability of 3-isopropylmalate dehydrogenase from Bacillus subtilis by experimental evolution. Protein Sci 7:698-705
    • (1998) Protein Sci , vol.7 , pp. 698-705
    • Akanuma, S.1    Yamagishi, A.2    Tanaka, N.3    Oshima, T.4
  • 3
    • 0033106205 scopus 로고    scopus 로고
    • Further improvement of the thermal stability of a partially stabilized Bacillus subtilis 3-isopropylmalate dehydrogenase variant by random and site-directed mutagenesis
    • Akanuma S, Yamagishi A, Tanaka N, Oshima T (1999) Further improvement of the thermal stability of a partially stabilized Bacillus subtilis 3-isopropylmalate dehydrogenase variant by random and site-directed mutagenesis. Eur J Biochem 260:499-504
    • (1999) Eur J Biochem , vol.260 , pp. 499-504
    • Akanuma, S.1    Yamagishi, A.2    Tanaka, N.3    Oshima, T.4
  • 4
    • 0018564346 scopus 로고
    • Transformation in yeast: Development of a hybrid cloning vector and isolation of the CAN1 gene
    • Amst
    • Broach JR, Strathern JN, Hicks JB (1979) Transformation in yeast: development of a hybrid cloning vector and isolation of the CAN1 gene. Gene (Amst) 8:121-123
    • (1979) Gene , vol.8 , pp. 121-123
    • Broach, J.R.1    Strathern, J.N.2    Hicks, J.B.3
  • 6
    • 0029881741 scopus 로고    scopus 로고
    • A stable intermediate in the thermal unfolding process of a chimeric 3-isopropylmalate dehydrogenase between a thermophilic and a mesophilic enzyme
    • Hayashi-Iwasaki Y, Numata K, Yamagishi A, 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 enzyme. Protein Sci 5:511-516
    • (1996) Protein Sci , vol.5 , pp. 511-516
    • Hayashi-Iwasaki, Y.1    Numata, K.2    Yamagishi, A.3    Yutani, K.4    Sakurai, M.5    Tanaka, N.6    Oshima, T.7
  • 7
    • 0032730861 scopus 로고    scopus 로고
    • Directed evolution of thermostable kanamycin-resistance gene: A convenient selection marker for Thermus thermophilus
    • Tokyo
    • Hoseki J, Yano T, Koyama Y, Kuramitsu S, Kagamiyama H (1999) Directed evolution of thermostable kanamycin-resistance gene: a convenient selection marker for Thermus thermophilus. J Biochem (Tokyo) 126:951-956
    • (1999) J Biochem , vol.126 , pp. 951-956
    • Hoseki, J.1    Yano, T.2    Koyama, Y.3    Kuramitsu, S.4    Kagamiyama, H.5
  • 8
    • 0019142274 scopus 로고
    • Leucine biosynthesis in Saccharomyces cerevisiae. Purification and characterization of ß-isopropylmalate dehydrogenase
    • Hsu YP, Kohlhaw GB (1980) Leucine biosynthesis in Saccharomyces cerevisiae. Purification and characterization of ß-isopropylmalate dehydrogenase. J Biol Chem 255:7255-7260
    • (1980) J Biol Chem , vol.255 , pp. 7255-7260
    • Hsu, Y.P.1    Kohlhaw, G.B.2
  • 9
    • 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
  • 10
    • 0032528935 scopus 로고    scopus 로고
    • Structure of 3-isopropylmalate dehydrogenase in complex with 3-isopropylmalate at 2.0 Å resolution: The role of Glu88 in the unique substrate-recognition mechanism
    • Lond
    • Imada K, Inagaki K, Matsunami H, Kawaguchi H, Tanaka H, Tanaka N, Namba K (1998) Structure of 3-isopropylmalate dehydrogenase in complex with 3-isopropylmalate at 2.0 Å resolution: the role of Glu88 in the unique substrate-recognition mechanism. Structure (Lond) 6:971-982
    • (1998) Structure , vol.6 , pp. 971-982
    • Imada, K.1    Inagaki, K.2    Matsunami, H.3    Kawaguchi, H.4    Tanaka, H.5    Tanaka, N.6    Namba, K.7
  • 11
    • 0028091179 scopus 로고
    • Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus
    • Kirino H, Aoki M, Aoshima M, Hayashi Y, Ohba M, Yamagishi A, Wakagi T, Oshima T (1994) Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus. Eur J Biochem 220:275-281
    • (1994) Eur J Biochem , vol.220 , pp. 275-281
    • Kirino, H.1    Aoki, M.2    Aoshima, M.3    Hayashi, Y.4    Ohba, M.5    Yamagishi, A.6    Wakagi, T.7    Oshima, T.8
  • 12
    • 0024197688 scopus 로고
    • ß-Isopropylmalate dehydrogenase from yeast
    • Kohlhaw GB (1988) ß-Isopropylmalate dehydrogenase from yeast. Methods Enzymol 166:429-435
    • (1988) Methods Enzymol , vol.166 , pp. 429-435
    • Kohlhaw, G.B.1
  • 13
    • 0030028478 scopus 로고    scopus 로고
    • Further stabilization of 3-isopropylmalate dehydrogenase of an extreme thermophile, Thermus thermophilus, by a suppressor mutation method
    • Kotsuka T, Akanuma S, Tomuro M, Yamagishi A, Oshima T (1996) Further stabilization of 3-isopropylmalate dehydrogenase of an extreme thermophile, Thermus thermophilus, by a suppressor mutation method. J Bacteriol 178:723-727
    • (1996) J Bacteriol , vol.178 , pp. 723-727
    • Kotsuka, T.1    Akanuma, S.2    Tomuro, M.3    Yamagishi, A.4    Oshima, T.5
  • 14
    • 0022448655 scopus 로고
    • Genetic transformation of the extreme thermophile Thermus thermophilus and of other Thermus spp
    • Koyama Y, Hoshino T, Tomizuka N, Furukawa K (1986) Genetic transformation of the extreme thermophile Thermus thermophilus and of other Thermus spp. J Bacteriol 166:338-340
    • (1986) J Bacteriol , vol.166 , pp. 338-340
    • Koyama, Y.1    Hoshino, T.2    Tomizuka, N.3    Furukawa, K.4
  • 16
    • 0028303486 scopus 로고
    • A rapid and efficient one-tube PCR-based mutagenesis technique using Pfu DNA polymerase
    • Picard V, Ersdal BE, Lu A, Bock SC (1994) A rapid and efficient one-tube PCR-based mutagenesis technique using Pfu DNA polymerase. Nucleic Acids Res 22:2587-2591
    • (1994) Nucleic Acids Res , vol.22 , pp. 2587-2591
    • Picard, V.1    Ersdal, B.E.2    Lu, A.3    Bock, S.C.4
  • 17
    • 0030028764 scopus 로고    scopus 로고
    • Glycerol decreases the volume and compressibility of protein interior
    • Priev A, Almagor A, Yedgar S, Gavish B (1996) Glycerol decreases the volume and compressibility of protein interior. Biochemistry 35:2061-2066
    • (1996) Biochemistry , vol.35 , pp. 2061-2066
    • Priev, A.1    Almagor, A.2    Yedgar, S.3    Gavish, B.4
  • 18
    • 0031015603 scopus 로고    scopus 로고
    • A mutation at the interface between domains causes rearrangement of domains in 3-isopropylmalate dehydrogenase
    • Qu C, Akanuma S, Moriyama H, Tanaka N, Oshima T (1997) A mutation at the interface between domains causes rearrangement of domains in 3-isopropylmalate dehydrogenase. Protein Eng 10:45-52
    • (1997) Protein Eng , vol.10 , pp. 45-52
    • Qu, C.1    Akanuma, S.2    Moriyama, H.3    Tanaka, N.4    Oshima, T.5
  • 22
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer WP (1994) Rapid evolution of a protein in vitro by DNA shuffling. Nature (Lond) 370:389-391
    • (1994) Nature (Lond) , vol.370 , pp. 389-391
    • Stemmer, W.P.1
  • 23
    • 0029154808 scopus 로고
    • Screening of stable proteins in an extreme thermophile, Thermus thermophilus
    • Tamakoshi M, Yamagishi A, Oshima T (1995) Screening of stable proteins in an extreme thermophile, Thermus thermophilus. Mol Microbiol 16:1031-1036
    • (1995) Mol Microbiol , vol.16 , pp. 1031-1036
    • Tamakoshi, M.1    Yamagishi, A.2    Oshima, T.3
  • 25
    • 0032487743 scopus 로고    scopus 로고
    • The organization of the leuC, leuD and leuB genes of the extreme thermophile Thermus thermophilus
    • Amst
    • Tamakoshi M, Yamagishi A, Oshima T (1998) The organization of the leuC, leuD and leuB genes of the extreme thermophile Thermus thermophilus. Gene (Amst) 222:125-132
    • (1998) Gene , vol.222 , pp. 125-132
    • Tamakoshi, M.1    Yamagishi, A.2    Oshima, T.3
  • 26
    • 0033047665 scopus 로고    scopus 로고
    • An efficient gene replacement and deletion system for an extreme thermophile, Thermus thermophilus
    • Tamakoshi M, Yaoi T, Oshima T, Yamagishi A (1999) An efficient gene replacement and deletion system for an extreme thermophile, Thermus thermophilus. FEMS Microbiol Lett 173:431-437
    • (1999) FEMS Microbiol Lett , vol.173 , pp. 431-437
    • Tamakoshi, M.1    Yaoi, T.2    Oshima, T.3    Yamagishi, A.4
  • 27
    • 0031567156 scopus 로고    scopus 로고
    • Crystal structures of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus
    • Wallon G, Kryger G, Lovett ST, Oshima T, Ringe D, Petsko GA (1997) Crystal structures of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus. J Mol Biol 266:1016-1031
    • (1997) J Mol Biol , vol.266 , pp. 1016-1031
    • Wallon, G.1    Kryger, G.2    Lovett, S.T.3    Oshima, T.4    Ringe, D.5    Petsko, G.A.6
  • 28
    • 0032973026 scopus 로고    scopus 로고
    • Directed evolution converts subtilisin E into a functional equivalent of thermitase
    • Zhao H, Arnold FH (1999) Directed evolution converts subtilisin E into a functional equivalent of thermitase. Protein Eng 12:47-53
    • (1999) Protein Eng , vol.12 , pp. 47-53
    • Zhao, H.1    Arnold, F.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.