Conversion of the coenzyme specificity of isocitrate dehydrogenase by module replacement

Journal of Biochemistry

Volumn 119, Issue 5, 1996, Pages 1014-1018

  Yaoi, Takuro ^a   Miyazaki, Kentaro ^a,c   Oshima, Taíro ^a,e   Komukai, Yutaka ^b,d   Go, Mitiko ^b  

^a TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

^b NAGOYA UNIVERSITY   (Japan)

^c NATL INST BIOSCI HUM TECHNOL   (Japan)

^d Nippon Chemiphar Co Ltd   (Japan)

^e TOKYO UNIVERSITY OF PHARMACY AND LIFE SCIENCES   (Japan)

Author keywords

Coenzyme specificity; Exon shuffling hypothesis; Module; Molecular recognition; Protein engineering

Indexed keywords

ISOCITRATE DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

AMINO ACID SUBSTITUTION; ARTICLE; COENZYME; ENZYME SPECIFICITY; ENZYME STABILITY; MUTANT; NONHUMAN; THERMOPHILIC BACTERIUM;

BACTERIA (MICROORGANISMS);

EID: 0030008575     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021316     Document Type: Article

References (29)

1. Imada, K., Sato, M., Matsuura, Y., Katsube, Y., and Oshima, T. (1991) Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus, at 2.2 A resolution. J. Mol. Biol. 222, 725-738
2. + complexes. Biochemistry 30, 8671-8678
3. Miyazaki, K., Eguchi, H., Yamagishi, A., Wakagi, T., and Oshima, T. (1992) Molecular cloning of the isocitrate dehydrogenase gene of an extreme thermophile, Thermus thermophilus HB8. Appl. Environ. Microbiol. 58, 93-98
4. Tanaka, T., Kawano, N., and Oshima, T. (1981) Cloning of 3-isopropylmalate dehydrogenase gene of an extreme thermophile and partial purification of the gene product. J. Biochem. 89, 677-682
5. Kirino, H., Aoki, M., Aoshima, M., Hayashi, Y., Ohba, M., Yamagishi, A., Wakagi, T., and 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
6. +-dependent isocitrate dehydrogenase from Saccharomyces cerevisiae. J. Biol. Chem. 276, 16417-16423
7. Miyazaki, K. and Oshima, T. (1994) Co-enzyme specificity of 3-isopropylmalate dehydrogenase from Thermus thermophilus HB8. Protein Eng. 7, 401-403
8. Yaoi, T., Miyazaki, K., and Oshima, T. (1994) Roles of Arg231 and Tyr284 of Thermus thermophilus isocitrate dehydrogenase in the coenzyme specificity. FEBS Lett. 355, 171-172
9. Kadono, S., Sakurai, M., Moriyama, H., Sato, M., Hayashi, Y., Oshima, T., and Tanaka, N. (1995) Ligand-induced changes in the conformation of 3-isopropylmalate dehydrogenase from Thermus thermophilus. J. Biochem. 118, 745-752
10. Oshima, T., Yaoi, T., and Go, M. (1995) Module replacement converted coenzyme specificity of isocitrate dehydrogenase in Tracing Biological Evolution in Protein and Gene Structures (Go, M. and Schimmel, P., eds.) pp. 197-203, Elsevier, Amsterdam
11. Kunkel, T.A. (1985) Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. USA 82, 488-492
12. Miyazaki, K., Yaoi, T., and Oshima, T. (1994) Expression, purification, and substrate specificity of isocitrate dehydrogenase from Thermus thermophilus HB8. Eur. J. Biochem. 221, 899-903
13. Go, M. and Nosaka, M. (1987) Protein architecture and the origin of introns. Cold Spring Harbor Symp. Quant. Biol. 52, 915-924
14. Noguti, T., Sakakibara, H., and Go, M. (1993) Localization of hydrogen-bonds within modules in barnase. Proteins 16, 357-363
15. Kraulis, P.J. (1991) MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950
16. Ohzeki, M., Yaoi, T., Moriyama, H., Oshima, T., and Tanaka, N. (1995) Crystallization and preliminary X-ray studies of isocitrate dehydrogenase from Thermus thermophilus HB8. J. Biochem. 118, 679-680
17. Yaoi, T., Miyazaki, K., and Oshima, T. (1995) His273 of 3-isopropylmalate dehydrogenase from Thermus thermophilus HB8 is involved in the coenzyme binding. Biochem. Biophys. Res. Commun. 210, 733-737
18. Scrutton, N.S., Berry, A., and Perham, R.N. (1990) Redesign of the coenzyme specificity of a dehydrogenase by protein engineering. Nature 343, 38-43
19. Bocanegra, J.A., Scrutton, N.S., and Perham, R.N. (1993) Creation of an NADP-dependent pyruvate dehydrogenase multienzyme complex by protein engineering. Biochemistry 32, 2737-2740
20. Nishiyama, M., Birktoft, J.J., and Beppu, T. (1993) Alteration of coenzyme specificity of malate dehydrogenase from Thermus flavus by site-directed mutagenesis. J. Biol. Chem. 268, 4656-4660
21. Go, M. (1981) Correlation of DNA exonic regions with protein structural units in haemoglobin. Nature 291, 90-92
22. Go, M. (1983) Modular structural units, exons, and function in chicken lysozyme. Proc. Natl. Acad. Sci. USA 80, 1964-1968
23. Go, M. (1985) Protein structures and split genes. Adv. Biophys. 19, 91-131
24. Gilbert, W. and Glynias, M. (1993) On the ancient nature of introns. Gene 135, 137-144
25. Gilbert, W. (1978) Why genes in pieces? Nature 271, 501
26. Gilbert, W. (1987) The exon theory of genes. Cold Spring Harbor Symp. Quant. Biol. 52, 901-905
27. Blake, C.C.F. (1979) Exons encode protein functional units. Nature 277, 598
28. Kumagai, I., Takeda, S., and Miura, K. (1992) Functional conversion of the homologous proteins α-lactalbumin and lysozyme by exon change. Proc. Natl. Acad. Sci. USA 89, 5887-5891
29. Wakasugi, K., Ishimori, K., Imai, K., Wada, Y., and Morishima, I. (1994) "Module" substitution in hemoglobin subunits. Preparation and characterization of a "chimera βα-subunit.α J. Biol. Chem. 269, 18750-18756