메뉴 건너뛰기




Volumn 179, Issue 4, 1997, Pages 1174-1179

Molecular and phylogenetic characterization of isopropylmalate dehydrogenase of a thermoacidophilic archaeon, Sulfolobus sp. strain 7

Author keywords

[No Author keywords available]

Indexed keywords

MALATE DEHYDROGENASE;

EID: 0031039159     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.4.1174-1179.1997     Document Type: Article
Times cited : (21)

References (42)
  • 1
    • 0028941917 scopus 로고
    • Root of the universal tree of life based on ancient aminoacyl-tRNA synthetase gene duplications
    • Brown, J. R., and W. F. Doolittle. 1995. Root of the universal tree of life based on ancient aminoacyl-tRNA synthetase gene duplications. Proc. Natl. Acad. Sci. USA 92:2441-2445.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2441-2445
    • Brown, J.R.1    Doolittle, W.F.2
  • 2
    • 0024530633 scopus 로고
    • Gene structure, organization and expression in archaebacteria
    • Brown, J. W., C. J. Daniels, and J. N. Reeve. 1989. Gene structure, organization and expression in archaebacteria. Crit. Rev. Microbiol. 16:287-338.
    • (1989) Crit. Rev. Microbiol. , vol.16 , pp. 287-338
    • Brown, J.W.1    Daniels, C.J.2    Reeve, J.N.3
  • 4
    • 0027432796 scopus 로고
    • + -isocitrate dehydrogenase with altered isocitrate binding sites: Contribution of IDH1 and IDH2 subunits to regulation and catalysis
    • + -isocitrate dehydrogenase with altered isocitrate binding sites: contribution of IDH1 and IDH2 subunits to regulation and catalysis. Biochemistry 32:9323-9328.
    • (1993) Biochemistry , vol.32 , pp. 9323-9328
    • Cupp, J.R.1    McAlister-Henn, L.2
  • 5
    • 0024278531 scopus 로고
    • The membrane-associated ATPase from Sulfolobus acidocaldarius is distantly related to F1-ATPase as assessed from the primary structure of its alpha-subunit
    • Denda, K., J. Konishi, T. Oshima, T. Date, and M. Yoshida. 1988. The membrane-associated ATPase from Sulfolobus acidocaldarius is distantly related to F1-ATPase as assessed from the primary structure of its alpha-subunit. J. Biol. Chem. 263:6012-6015.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6012-6015
    • Denda, K.1    Konishi, J.2    Oshima, T.3    Date, T.4    Yoshida, M.5
  • 8
    • 0029944211 scopus 로고    scopus 로고
    • Conservation of aconitase residues revealed by multiple sequence analysis. Implications for structure/function relationship
    • Frishman, D., and W. Hentze. 1996. Conservation of aconitase residues revealed by multiple sequence analysis. Implications for structure/function relationship. Eur. J. Biochem. 239:197-200.
    • (1996) Eur. J. Biochem. , vol.239 , pp. 197-200
    • Frishman, D.1    Hentze, W.2
  • 9
    • 0022423889 scopus 로고
    • Use of intermediate partitioning to calculate intrinsic isotope effects for the reaction catalyzed by malic enzyme
    • Grissom, C., and W. W. Cleland. 1985. Use of intermediate partitioning to calculate intrinsic isotope effects for the reaction catalyzed by malic enzyme. Biochemistry 12:944-948.
    • (1985) Biochemistry , vol.12 , pp. 944-948
    • Grissom, C.1    Cleland, W.W.2
  • 10
    • 0040914011 scopus 로고
    • ρ-σ-π analysis; method for the correlation of biological activity and chemical structure
    • Hansch, C., and T. Fujita. 1964. ρ-σ-π analysis; method for the correlation of biological activity and chemical structure. J. Am. Chem. Soc. 86(8):5175-5180.
    • (1964) J. Am. Chem. Soc. , vol.86 , Issue.8 , pp. 5175-5180
    • Hansch, C.1    Fujita, T.2
  • 11
    • 0025004005 scopus 로고
    • Subunit location and sequences of the cysteinyl peptides of pig heart NAD-dependent isocitrate dehydrogenase
    • Huang, Y. C., and R. F. Colman. 1990. Subunit location and sequences of the cysteinyl peptides of pig heart NAD-dependent isocitrate dehydrogenase. Biochemistry 29:8266-8273.
    • (1990) Biochemistry , vol.29 , pp. 8266-8273
    • Huang, Y.C.1    Colman, R.F.2
  • 13
    • 0028774536 scopus 로고
    • +: Ligand-induced loop closing and mechanism for cofactor specificity
    • +: ligand-induced loop closing and mechanism for cofactor specificity. Structure 15(2):1007-1016.
    • (1994) Structure , vol.15 , Issue.2 , pp. 1007-1016
    • Hurley, J.H.1    Dean, A.M.2
  • 15
    • 0026334204 scopus 로고
    • Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2 Å resolution
    • Imada, K., M. Sato, N. Tanaka, Y. Katsube, Y. Matsuura, and T. Oshima. 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
  • 16
    • 0027972087 scopus 로고
    • Functional and evolutionary implications of a [3Fe-4S] cluster of the dicluster-type ferredoxin from the thermoacidophilic archaeon, Sulfolobus sp. strain 7
    • Iwasaki, T., T. Wakagi, Y. Isogai, K. Tanaka, T. Iizuka, and T. Oshima. 1994. Functional and evolutionary implications of a [3Fe-4S] cluster of the dicluster-type ferredoxin from the thermoacidophilic archaeon, Sulfolobus sp. strain 7. J. Biol. Chem. 269:29444-29450.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29444-29450
    • Iwasaki, T.1    Wakagi, T.2    Isogai, Y.3    Tanaka, K.4    Iizuka, T.5    Oshima, T.6
  • 17
    • 0029617402 scopus 로고
    • Resolution of the aerobic respiratory system of the thermoacidophilic archaeon. Sulfolobus sp. strain 7. the archaeal novel respiratory complex II (succinate: Caldariellaquinone oxidoreductase complex) inherently lacks heme group
    • Iwasaki, T., T. Wakagi, and T. Oshima. 1995. Resolution of the aerobic respiratory system of the thermoacidophilic archaeon. Sulfolobus sp. strain 7. The archaeal novel respiratory complex II (succinate: caldariellaquinone oxidoreductase complex) inherently lacks heme group. J. Biol. Chem. 270:30902-30908.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30902-30908
    • Iwasaki, T.1    Wakagi, T.2    Oshima, T.3
  • 18
    • 0028997589 scopus 로고
    • Sulredoxin: A novel iron-sulfur protein of the thermoacidophilic archaeon Sulfolobus sp. strain 7 with a Rieske-type [2Fe-2S] center
    • Iwasaki, T., Y. Isogai, T. Iizuka, and T. Oshima. 1995. Sulredoxin: a novel iron-sulfur protein of the thermoacidophilic archaeon Sulfolobus sp. strain 7 with a Rieske-type [2Fe-2S] center. J. Bacteriol. 177:2576-2582.
    • (1995) J. Bacteriol. , vol.177 , pp. 2576-2582
    • Iwasaki, T.1    Isogai, Y.2    Iizuka, T.3    Oshima, T.4
  • 19
    • 0028853604 scopus 로고
    • Ligand-induced changes in the conformation of 3-isopropylmalate dehydrogenase from Thermits thermophilus
    • Kadono, S., M. Sakurai, H. Moriyama, M. Sato, Y. Hayashi, T. Oshima, and N. Tanaka. 1995. Ligand-induced changes in the conformation of 3-isopropylmalate dehydrogenase from Thermits thermophilus. J. Biochem. 118:745-752.
    • (1995) J. Biochem. , vol.118 , pp. 745-752
    • Kadono, S.1    Sakurai, M.2    Moriyama, H.3    Sato, M.4    Hayashi, Y.5    Oshima, T.6    Tanaka, N.7
  • 20
    • 0027515241 scopus 로고
    • 3-Isopropylmalate dehydrogenase from chemolithoautotroph Thiobacillus ferrooxidans: DNA sequence, enzyme purification, and characterization
    • Kawaguchi, H., K. Inagaki, Y. Kuwata, H. Tanaka, and T. Tano. 1993. 3-Isopropylmalate dehydrogenase from chemolithoautotroph Thiobacillus ferrooxidans: DNA sequence, enzyme purification, and characterization. J. Biochem. 114:370-377.
    • (1993) J. Biochem. , vol.114 , pp. 370-377
    • Kawaguchi, H.1    Inagaki, K.2    Kuwata, Y.3    Tanaka, H.4    Tano, T.5
  • 21
    • 0025280662 scopus 로고
    • Subunit structure, expression, and function of NAD(H)-specific isocitrate dehydrogenase in Saccharomyces cerevisiae
    • Keys, D. A., and L. McAlister-Henn. 1990. Subunit structure, expression, and function of NAD(H)-specific isocitrate dehydrogenase in Saccharomyces cerevisiae. J. Bacteriol. 172:4280-4287.
    • (1990) J. Bacteriol. , vol.172 , pp. 4280-4287
    • Keys, D.A.1    McAlister-Henn, L.2
  • 22
    • 0028091179 scopus 로고
    • Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thennophilus
    • kirino, H., M. Aoki, M. Aoshima, Y. Hayashi, M. Ohba, A. Yamagishi, T. Wakagi, and T. Oshima. 1994. Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thennophilus. 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
  • 23
    • 14444285107 scopus 로고
    • Positive selection for uracil auxotrophs of the sulfur-dependent thermophilic archaebacterium Sulfobus acidocaldarius by use of 5-fluoroorotic acid
    • Kondo, S., A. Yamagishi, and T. Oshima. 1991. Positive selection for uracil auxotrophs of the sulfur-dependent thermophilic archaebacterium Sulfobus acidocaldarius by use of 5-fluoroorotic acid. J. Bacteriol. 175:1532-1536.
    • (1991) J. Bacteriol. , vol.175 , pp. 1532-1536
    • Kondo, S.1    Yamagishi, A.2    Oshima, T.3
  • 24
    • 0028047371 scopus 로고
    • Co-enzyme specificity of 3-isopropylmalate dehydrogenase from Thermus thermophilus HB8
    • Miyazaki, K., and T. Oshima. 1994. Co-enzyme specificity of 3-isopropylmalate dehydrogenase from Thermus thermophilus HB8. Protein Eng. 7(3):401-403.
    • (1994) Protein Eng. , vol.7 , Issue.3 , pp. 401-403
    • Miyazaki, K.1    Oshima, T.2
  • 25
    • 0027504526 scopus 로고
    • Kinetic analysis on the substrate specificity of 3-isopropylmalale dehydrogenase
    • Miyazaki, K., K. Kakinuma, H. Terasawa, and T. Oshima. 1993. Kinetic analysis on the substrate specificity of 3-isopropylmalale dehydrogenase. FEBS Lett. 332:35-36.
    • (1993) FEBS Lett. , vol.332 , pp. 35-36
    • Miyazaki, K.1    Kakinuma, K.2    Terasawa, H.3    Oshima, T.4
  • 28
    • 0028986679 scopus 로고
    • Thermal stability of chimeric isopropylmalate dehydrogenase gene constructed from a thermophile and a mesophile
    • Numata, K., M. Muro, N. Akutsu, Y. Hosoh, A. Yamagishi, and T. Oshima. 1995. Thermal stability of chimeric isopropylmalate dehydrogenase gene constructed from a thermophile and a mesophile. Protein Eng. 8:39-43.
    • (1995) Protein Eng. , vol.8 , pp. 39-43
    • Numata, K.1    Muro, M.2    Akutsu, N.3    Hosoh, Y.4    Yamagishi, A.5    Oshima, T.6
  • 29
    • 0022350311 scopus 로고
    • Sequence of the 16S rRNA gene from the thermoacidophilic archaebacterium Sulfolobus sulfataricus and its evolutionary implications
    • Olsen, G. J., N. R. Pace, M. Nuell, B. P. Kaime, R. Gupta, and C. R. Woese. 1985. Sequence of the 16S rRNA gene from the thermoacidophilic archaebacterium Sulfolobus sulfataricus and its evolutionary implications. J. Mol. Evol. 22:301-307.
    • (1985) J. Mol. Evol. , vol.22 , pp. 301-307
    • Olsen, G.J.1    Pace, N.R.2    Nuell, M.3    Kaime, B.P.4    Gupta, R.5    Woese, C.R.6
  • 30
    • 0028055018 scopus 로고
    • The winds of (evolutionary) change: Breathing new life into microbiology
    • Olsen, G. J., C. R. Woese, and R. Overbeek. 1994. The winds of (evolutionary) change: breathing new life into microbiology. J. Bacteriol. 176:1-6.
    • (1994) J. Bacteriol. , vol.176 , pp. 1-6
    • Olsen, G.J.1    Woese, C.R.2    Overbeek, R.3
  • 31
    • 0028221519 scopus 로고
    • Three-dimensional structures of chimeric enzymes between Bacillus subtilis and Thermus thermophilus 3-isopropylmalate dehydrogenases
    • Onodera, K., M. Sakurai, H. Moriyama, N. Tanaka, K. Numata, T. Oshima, M. Sato, and Y. Katsube. 1994. Three-dimensional structures of chimeric enzymes between Bacillus subtilis and Thermus thermophilus 3-isopropylmalate dehydrogenases. Protein Eng. 7(4):453-459.
    • (1994) Protein Eng. , vol.7 , Issue.4 , pp. 453-459
    • Onodera, K.1    Sakurai, M.2    Moriyama, H.3    Tanaka, N.4    Numata, K.5    Oshima, T.6    Sato, M.7    Katsube, Y.8
  • 32
    • 0001590511 scopus 로고
    • Kinetic mechanism and reaction pathway of Thermus thermophilus isopropylmalate dehydrogenase
    • Pirrung, M., H. Han, and D. Nunn. 1994. Kinetic mechanism and reaction pathway of Thermus thermophilus isopropylmalate dehydrogenase. J. Org. Chem. 59:2423-2429.
    • (1994) J. Org. Chem. , vol.59 , pp. 2423-2429
    • Pirrung, M.1    Han, H.2    Nunn, D.3
  • 36
    • 0001351894 scopus 로고
    • Rapid attainment of sedimentation equilibrium
    • Van Holde, K. E., and R. L. Baldwin. 1958. Rapid attainment of sedimentation equilibrium. J. Phys. Chem. 62:734-743.
    • (1958) J. Phys. Chem. , vol.62 , pp. 734-743
    • Van Holde, K.E.1    Baldwin, R.L.2
  • 37
    • 0023388573 scopus 로고
    • Purification and properties of NADH dehydrogenase from a thermoacidophilic archaebacterium Sulfolobus acidocaldarius
    • Wakao, H., T. Wakagi, and T. Oshima. 1987. Purification and properties of NADH dehydrogenase from a thermoacidophilic archaebacterium Sulfolobus acidocaldarius. J. Biochem. 102:255-262.
    • (1987) J. Biochem. , vol.102 , pp. 255-262
    • Wakao, H.1    Wakagi, T.2    Oshima, T.3
  • 38
    • 0025300402 scopus 로고
    • Towards a natural system of organisms: Proposal for the domains Archaea, Bacteria, and Eukarya
    • Woese, C. R., O. Kandler, and M. L. Wheelis. 1990. Towards a natural system of organisms: proposal for the domains Archaea, Bacteria, and Eukarya. Proc. Natl. Acad. Sci. USA 87:4576-4579.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4576-4579
    • Woese, C.R.1    Kandler, O.2    Wheelis, M.L.3
  • 39
    • 0025108577 scopus 로고
    • Purification, catalytic properties, and thermal stability of Threo-Ds-3-isopropylmalate dehydrogenase coded by leuB gene from an extreme thermophile, Thermits thermophilus strain HB8
    • Yamada, T., N. Akutsu, K. Miyazaki, K. Kakinuma, M. Yoshida, and T. Oshima. 1990. Purification, catalytic properties, and thermal stability of Threo-Ds-3-isopropylmalate dehydrogenase coded by leuB gene from an extreme thermophile, Thermits thermophilus strain HB8. J. Biochem. 108:449-456.
    • (1990) J. Biochem. , vol.108 , pp. 449-456
    • Yamada, T.1    Akutsu, N.2    Miyazaki, K.3    Kakinuma, K.4    Yoshida, M.5    Oshima, T.6
  • 40
    • 0029127497 scopus 로고
    • Purification and characterization of 3-isopropylmalate dehydrogenase from a thermoacidophilic archaebacterium, Sulfolobus sp. strain 7
    • Yoda, E., Y. Anraku, H. Kirino, T. Wakagi, and T. Oshima. 1995. Purification and characterization of 3-isopropylmalate dehydrogenase from a thermoacidophilic archaebacterium, Sulfolobus sp. strain 7. FEMS Microbiol. Lett. 131:243-247.
    • (1995) FEMS Microbiol. Lett. , vol.131 , pp. 243-247
    • Yoda, E.1    Anraku, Y.2    Kirino, H.3    Wakagi, T.4    Oshima, T.5
  • 42
    • 0028901535 scopus 로고
    • Modeling substrate binding in Thermus themophilus isopropylmalate dehydrogenase
    • Zhang, T., and D. E. Koshland, Jr. 1995. Modeling substrate binding in Thermus themophilus isopropylmalate dehydrogenase. Protein Sci. 4:84-92.
    • (1995) Protein Sci. , vol.4 , pp. 84-92
    • Zhang, T.1    Koshland Jr., D.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.