95
Views
2
CrossRef citations to date
0
Altmetric
Original Articles

Novel Substrate Specificity of Designer 3-Isopropylmalate Dehydrogenase Derived from Thermus thermophilus HB8

, , &
Pages 2695-2700 | Received 22 Jun 2001, Accepted 23 Aug 2001, Published online: 22 May 2014

  • 1) Tanaka, T., Kawano, N., and Oshima, T., Cloning of 3-isopropylmalate dehydrogenase gene of an extreme thermophile and partial purification of the gene product. J. Biochem., 89, 677-682 (1981).
  • 2) Kagawa, Y., Nojima, H., Nukiwa, N., Ishizuka, M., Nakajima, T., Yasuhara, T., Tanaka, T., and Oshima, T., High guanine plus cytosine content in the third letter of codons of an extreme thermophile. J. Biol. Chem., 259, 2956-2960 (1984).
  • 3) Yamada, T., Akutsu, N., Miyazaki, K., Kakinuma, K., Yoshida, M., and Oshima, T., 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., 108, 449-456 (1990).
  • 4) 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 2.2Å resolution. J. Mol. Biol., 222, 725-738 (1991).
  • 5) Hurley, J.H. and Dean, A.M., Structure of 3-isopropylmalate dehydrogenase in complex with NAD+: ligand-induced loop closing and mechanism for cofactor specificity. Structure, 2, 1007-1016 (1994).
  • 6) Kadono, S., Sakurai, M., Moriyama, H., Sato, M., Hayashi, Y., Oshima, T., and Tanaka, N., Ligand-induced changes in the conformation of 3-isopropylmalate dehydrogenase from Thermus thermophilus. J. Biochem., 118, 745-752 (1995).
  • 7) Yamada, T., Kakinuma, K., Endo, T., and Oshima, T., Stereospecificity of the hydride transfer reaction catalyzed by isopropylmalate dehydrogenase of thermophilic bacteria Thermus thermophilus. Chem. Lett., 1749-1752 (1987).
  • 8) Kakinuma, K., Ozawa, K., Fujimoto, Y., Akutsu, N., and Oshima, T., Stereochemistry of the decarboxylation reaction catalyzed by 3-isopropylmalate dehydrogenase from the thermophilic bacterium Thermus thermophilus. J. Chem. Soc., Chem. Commun., 17, 1190-1192 (1989).
  • 9) Kakinuma, K., Terasawa, H., Li, H.-Y., Miyazaki, K., and Oshima, T., Enantioselective synthesis of (2R,3S)-3-alkylmalic acids, competent substrates for 3-isopropylmalate dehydrogenase. Biosci. Biotechnol. Biochem., 57, 1916-1923 (1993).
  • 10) Terasawa, H., Miyazaki, K., Oshima, T., Eguchi, T., and Kakinuma, K., Synthesis of 2-O-methyl ether and 1-carboxamide derivatives of (2R,3S)-3-isopropylmalic acid and their interaction with thermophilic 3-isopropylmalate dehydrogenase. Biosci. Biotechnol. Biochem., 58, 870-873 (1994).
  • 11) Aoyama, T., Eguchi, T., Oshima, T., and Kakinuma, K., Synthesis of DL-threo-3-(1-fluoro-1-methylethyl)-and DL-threo-3-(1,1-difluoroethyl)malic acids. Mechanistic studies of 3-isopropylmalate dehydrogenase. J. Chem. Soc. Perkin Trans., 1, 1905-1912 (1995).
  • 12) Chiba, A., Eguchi, T., Oshima, T., and Kakinuma, K., Synthesis of conformationally restricted substrate analogs and their interaction with 3-isopropylmalate dehydrogenase derived from Thermus thermophilus. Tetrahedron, 53, 3537-3544 (1997).
  • 13) 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, 10422-10425 (1987).
  • 14) Hurley, J.H., Thorsness, P.E., Ramalingam, V., Helmers, N.H., Koshland, Jr., D.E., and Stroud, R. M., Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase. Proc. Natl. Acad. Sci. USA, 86, 8635-8639 (1989).
  • 15) Hurley, J.H., Dean, A.M., Sohl, J.L., Koshland, Jr., D.E., and Stroud, R.M., Regulation of an enzyme by phosphorylation at the active site. Science, 249, 1012-1016 (1990).
  • 16) Imada, K., Inagaki, K., Matsunami, H., Kawaguchi, H., Tanaka, H., Tanaka, N., and Namba, K., Structure of 3-isopropylmalate dehydrogenase in complex with 3-isopropylmalate at 2.0 A resolution: the role of Glu88 in the unique substrate-recognition mechanism. Structure, 6, 971-982 (1998).
  • 17) Clarke, A.R., Smith, C.J., Hart, K.W., Wilks, H.M., Chia, W.N., Lee, T.V., Birktoft, J.J., Banaszak, L.J., Barstow, D.A., Atkinson, T., and Holbrook, J.J., Rational construction of a 2-hydroxyacid dehydrogenase with new substrate specificity. Biochem. Biophys. Res. Commun., 148, 15-23 (1987).
  • 18) Lindberg, R.L.P. and Negishi, M., Alteration of mouse cytochrome P450coh substrate specificity by mutation of a single amino-acid residue. Nature, 339, 632-634 (1989).
  • 19) Kunkel, T.A., Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. USA, 82, 488-492 (1985).
  • 20) Kirino, H., Aoki, M., Aoshima, M., Hayashi, Y., Ohba, M., Yamagishi, A., Wakagi, T., and Oshima, T., 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).
  • 21) Fujita, M., Toyooka, Y., Tamegai, H., Eguchi, T., and Kakinuma, K., Arg-94 is crucial to the catalysis of 3-isopropylmalate dehydrogenase from Thermus thermophilus HB8. J. Mol. Catal. B: Enzym., 9, 149-155 (2000).
  • 22) Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
  • 23) Zhang, T. and Koshland, Jr., D.E., Modeling substrate binding in Thermus thermophilus isopropylmalate dehydrogenase. Protein Sci., 4, 84-92 (1995).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.