메뉴 건너뛰기




Volumn 580, Issue 16, 2006, Pages 3867-3871

The effects of multiple ancestral residues on the Thermus thermophilus 3-isopropylmalate dehydrogenase

Author keywords

3 Isopropylmalate dehydrogenase; Ancestral residue; Protein stability; Thermus thermophilus

Indexed keywords

3 ISOPROPYLMALATE DEHYDROGENASE; ALANINE; ASPARAGINE; GLUTAMIC ACID; LEUCINE; MUTANT PROTEIN; PROLINE; THREONINE; VALINE;

EID: 33745358763     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.06.012     Document Type: Article
Times cited : (12)

References (13)
  • 1
    • 0037900194 scopus 로고    scopus 로고
    • Hyperthermostabilization of Bacillus licheniformis alpha-amylase and modulation of its stability over a 50 degrees C temperature range
    • Declerck N., Machius M., Joyet P., Wiegand G., Huber R., and Gaillardin C. Hyperthermostabilization of Bacillus licheniformis alpha-amylase and modulation of its stability over a 50 degrees C temperature range. Protein Eng. 16 (2003) 287-293
    • (2003) Protein Eng. , vol.16 , pp. 287-293
    • Declerck, N.1    Machius, M.2    Joyet, P.3    Wiegand, G.4    Huber, R.5    Gaillardin, C.6
  • 3
    • 0037246131 scopus 로고    scopus 로고
    • Protein engineering to improve the thermostability of glucoamylase from Aspergillus awamori based on molecular dynamics simulations
    • Liu H.L., and Wang W.C. Protein engineering to improve the thermostability of glucoamylase from Aspergillus awamori based on molecular dynamics simulations. Protein Eng. 16 (2003) 19-25
    • (2003) Protein Eng. , vol.16 , pp. 19-25
    • Liu, H.L.1    Wang, W.C.2
  • 4
    • 0029922615 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase from Thermotoga maritima: strategies of protein stabilization
    • Jaenicke R. Glyceraldehyde-3-phosphate dehydrogenase from Thermotoga maritima: strategies of protein stabilization. FEMS Microbiol. Rev. 18 (1996) 215-224
    • (1996) FEMS Microbiol. Rev. , vol.18 , pp. 215-224
    • Jaenicke, R.1
  • 5
    • 0023645302 scopus 로고
    • Inactivation of isocitrate dehydrogenase by phosphorylation is mediated by the negative charge of the phosphate
    • Thorsness P.E., and Koshland Jr. D.E. Inactivation of isocitrate dehydrogenase by phosphorylation is mediated by the negative charge of the phosphate. J. Biol. Chem. 262 (1987) 10422-10425
    • (1987) J. Biol. Chem. , vol.262 , pp. 10422-10425
    • Thorsness, P.E.1    Koshland Jr., D.E.2
  • 6
    • 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., and Oshima T. Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2 Å resolution. J. Mol. Biol. 222 (1991) 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
  • 7
    • 0034986432 scopus 로고    scopus 로고
    • Ancestral residues stabilizing 3-isopropylmalate dehydrogenase of an extreme thermophile: experimental evidence supporting the thermophilic common ancestor hypothesis
    • Miyazaki J., Nakaya S., Suzuki T., Tamakoshi M., Oshima T., and Yamagishi A. Ancestral residues stabilizing 3-isopropylmalate dehydrogenase of an extreme thermophile: experimental evidence supporting the thermophilic common ancestor hypothesis. J. Biochem. (Tokyo) 129 (2001) 777-782
    • (2001) J. Biochem. (Tokyo) , vol.129 , pp. 777-782
    • Miyazaki, J.1    Nakaya, S.2    Suzuki, T.3    Tamakoshi, M.4    Oshima, T.5    Yamagishi, A.6
  • 8
    • 15944381217 scopus 로고    scopus 로고
    • Thermostability of ancestral mutants of Caldococcus noboribetus isocitrate dehydrogenase
    • Iwabata H., Watanabe K., Ohkuri T., Yokobori S., and Yamagishi A. Thermostability of ancestral mutants of Caldococcus noboribetus isocitrate dehydrogenase. FEMS Microbiol. Lett. 243 (2005) 393-398
    • (2005) FEMS Microbiol. Lett. , vol.243 , pp. 393-398
    • Iwabata, H.1    Watanabe, K.2    Ohkuri, T.3    Yokobori, S.4    Yamagishi, A.5
  • 9
    • 29144522906 scopus 로고    scopus 로고
    • Designing thermostable proteins: Ancestral mutants of 3-isopropylmalate dehydrogenase designed by using a phylogenetic tree
    • Watanabe K., Ohkuri T., Yokobori S., and Yamagishi A. Designing thermostable proteins: Ancestral mutants of 3-isopropylmalate dehydrogenase designed by using a phylogenetic tree. J. Mol. Biol. 355 (2006) 664-674
    • (2006) J. Mol. Biol. , vol.355 , pp. 664-674
    • Watanabe, K.1    Ohkuri, T.2    Yokobori, S.3    Yamagishi, A.4
  • 10
    • 0028303486 scopus 로고
    • A rapid and efficient one-tube PCR-based mutagenesis technique using Pfu DNA polymerase
    • Picard V., Ersdal-Badju E., Lu A., and Bock S.C. A rapid and efficient one-tube PCR-based mutagenesis technique using Pfu DNA polymerase. Nucleic Acids Res. 22 (1994) 2587-2591
    • (1994) Nucleic Acids Res. , vol.22 , pp. 2587-2591
    • Picard, V.1    Ersdal-Badju, E.2    Lu, A.3    Bock, S.C.4
  • 11
    • 0033851275 scopus 로고    scopus 로고
    • Purification and characterization of recombinant 3-isopropylmalate dehydrogenase from Thermus thermophilus and other microorganisms
    • Hayashi Y., and Oshima T. Purification and characterization of recombinant 3-isopropylmalate dehydrogenase from Thermus thermophilus and other microorganisms. Method Enzymol. 324 (2000) 301-323
    • (2000) Method Enzymol. , vol.324 , pp. 301-323
    • Hayashi, Y.1    Oshima, T.2
  • 12
    • 0022538679 scopus 로고
    • Cumulative effect of intragenic amino-acid replacements on the thermostability of a protein
    • Matsumura M., Yasumura S., and Aiba S. Cumulative effect of intragenic amino-acid replacements on the thermostability of a protein. Nature 323 (1986) 356-358
    • (1986) Nature , vol.323 , pp. 356-358
    • Matsumura, M.1    Yasumura, S.2    Aiba, S.3
  • 13
    • 0029585945 scopus 로고
    • Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive
    • Zhang X.J., Baase W.A., Shoichet B.K., Wilson K.P., and Matthews B.W. Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. Protein Eng. 8 (1995) 1017-1022
    • (1995) Protein Eng. , vol.8 , pp. 1017-1022
    • Zhang, X.J.1    Baase, W.A.2    Shoichet, B.K.3    Wilson, K.P.4    Matthews, B.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.