NADP-glutamate dehydrogenase isoenzymes of Saccharomyces cerevisiae: Purification, kinetic properties, and physiological roles

Journal of Biological Chemistry

Volumn 276, Issue 47, 2001, Pages 43775-43783

  DeLuna, Alexander ^a   Avendaño, Amaranta ^a   Riego, Lina ^a   González, Alicia ^a  

^a INSTITUTO DE FISIOLOGÍA CELULAR   (Mexico)

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHESIS; CATALYSIS; ENZYMES; METABOLISM; PHYSIOLOGY;

GLUTAMATE;

YEAST;

2 OXOGLUTARIC ACID; AMMONIA; CARBON; GLUTAMATE DEHYDROGENASE (NADP); GLUTAMATE DEHYDROGENASE 1; GLUTAMATE DEHYDROGENASE 2; GLUTAMIC ACID; ISOENZYME; UNCLASSIFIED DRUG; GLUTAMATE DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PRIMER DNA;

ADAPTATION; ALLOSTERISM; ANIMAL CELL; ARTICLE; BIOSYNTHESIS; BREATHING; CATALYSIS; CONTROLLED STUDY; ENZYME DEGRADATION; ENZYME MECHANISM; ENZYME PURIFICATION; ENZYME REGULATION; ENZYME SYNTHESIS; FERMENTATION; GENE OVEREXPRESSION; METABOLISM; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; SACCHAROMYCES CEREVISIAE; ENZYMOLOGY; GENE EXPRESSION REGULATION; GENETIC TRANSCRIPTION; GENETICS; ISOLATION AND PURIFICATION; KINETICS; NUCLEOTIDE SEQUENCE; POLYACRYLAMIDE GEL ELECTROPHORESIS;

ANIMALIA; SACCHAROMYCES; SACCHAROMYCES CEREVISIAE;

BASE SEQUENCE; DNA PRIMERS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GENE EXPRESSION REGULATION, ENZYMOLOGIC; GENE EXPRESSION REGULATION, FUNGAL; GLUTAMATE DEHYDROGENASE; ISOENZYMES; KINETICS; NADP; SACCHAROMYCES CEREVISIAE; TRANSCRIPTION, GENETIC;

EID: 0035941209     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M107986200     Document Type: Article

References (50)

1. Magasanik, B. (1992) in The Molecular and Cellular Biology of the Yeast Saccharomyces cerevisiae: Gene Expression (Jones, E. W., Pringle, J. R., and Broach, J. R., ed) pp. 283-317, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
2. Tempest, D. W., Meers, J. L., Brown, C. M. (1970) Biochem. J. 117, 405-407
3. Roon, R. J., Even, H. L., and Larimore, F. (1974) J. Bacteriol. 118, 89-95
4. Holzer, H., and Schneider, S. (1957) Biochem. Z. 328, 361-367
5. Benachenhou-Lahfa, N., Forterre, P., and Labendan, B. (1993) J. Mol. Evol. 36, 335-346
6. Avendaño, A., DeLuna, A., Olivera, H., Valenzuela, L., and González, A. (1997) J. Bacteriol. 179, 5594-5597
7. Smith, E. L. (1975) in The Enzymes, Vol. XI (Boyer, P. D., ed) pp. 293-367, Academic Press, Inc., New York
8. Miller, S. M., and Magasanik, B. (1990) J. Bacteriol. 172, 4927-4935
9. Drillien, R., and Lacroute, F. (1972) J. Bacteriol. 109, 203-208
10. Grenson, M., Dubois, E., Piotrowska, M., Drillien, R., and Aigle, M. (1974) Mol. Gen. Genet. 128, 73-85
11. Dang, V. D., Bohn, C., Bolotin-Fukuhara, M., and Daignan-Fornier, B. (1996) J. Bacteriol. 178, 1842-1849
12. Forsburg, S. L., and Guarente, L. (1989) Annu. Rev. Cell Biol. 5, 153-180
13. Cox, K. H., Pinchack, A. B., and Cooper, T. C. (1999) Yeast 15, 703-713
14. Janes, B. K., Pomposiello, P. J., Perez-Matos, A., Najarian, D. J., Goss, T. J., and Bender, R. A. (2001) J. Bacteriol. 183, 2709-2714
15. Ninfa, A., Jiang, P., Atkinson, M. R., and Peliska, J. A. (2000) Curr. Top. Cell Reg. 36, 31-75
16. Boy-Marcotte, E., Perrot, M., Bussereau, F., Boucherie, H., and Jacquet, M. (1998) J. Bacteriol. 180, 1044-1052
17. Wach, A., Brachat, A., Pohlmann, R., and Philippsen, P. (1994) Yeast 10, 1793-1808
18. Ito, H., Fukuda, Y., Murata, K., and Kimura, A. (1983) J. Bacteriol. 153, 163-168
19. Sambrook, J., Fritsch, E. F., and Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual, 2nd Ed., pp. 1.1-7.87, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
20. Sikorski, R. S., and Hieter, P. (1989) Genetics 122, 19-27
21. Christianson, T. W., Sikorski, R. S., Dante, M., Shero, J. H., Hieter, P. (1992) Gene (Amst.) 110, 119-122
22. Bussey, H., Kaback, D. B., Zhong, W., Vo, D. T., Clark, M. W., Fortin, N., Hall, J., Ouellette, B. F., Keng, T., Barton, A. B., Su, Y., Davies, C. J., and Storms, R. K. (1995) Proc. Natl. Acad. Sci. U. S. A. 92, 3809-3813
23. Doherty, D. (1970) Methods Enzymol. 17, 850-856
24. Cogoni, C., Valenzuela, L., González-Halphen, D., Olivera, H., Macino, G., Ballario, P., and González, A. (1995) J. Bacteriol. 177, 792-798
25. Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951) J. Biol. Chem. 193, 265-275
26. González-Halphen, D., Lindorfer, M. A., Capaldi, R. A. (1988) Biochemistry 27, 7021-7031
27. Towbin, H., Staehelin, T., Gordon, J. (1979) Bio/Technology 24, 145-149
28. Gutierrez-Cirlos, E. B., Antaramian, A., Vazquez-Acevedo, M., Coria, R., and Gonzalez-Halphen, D. (1994) J. Biol. Chem. 269, 9147-9154
29. Ellis, K. J., Morrison, J. F. (1982) Methods Enzymol. 87, 405-426
30. Kang, L., Keeler, M. L., Dunlop, P. C., and Roon, R. J. (1982) J. Bacteriol. 151, 29-35
31. Dubois, E., Grenson, M., and Wiame, J. M. (1974) Eur. J. Biochem. 48, 603-616
32. Camardella, L., Di Prisco, G., Garofano, F., and Guerrini, A. M. (1976) Biochim. Biophys. Acta 429, 324-330
33. Miñambres, B., Olivera, E. R., Jensen, R. A., and Luengo, J. M. (2000) J. Biol. Chem. 275, 39529-39542
34. Baker, P. J., Britton, K. L., Engel, P. C., Farrants, G. W., Lilley, K. S., Rice, D. W., and Stillman, T. J. (1992) Proteins 12, 75-86
35. Yip, K. S., Stillman, T. J., Britton, K. L., Artymiuk, P. J., Baker, P. J., Sedelnikova, S. E., Engel, P. C., Pasquo, A., Chiaraluce, R., Consalvi, V., Scandurra, R., and Rice, D. W. (1995) Structure 3, 1147-1158
36. Venard, R., Jallon, J. M., Fourcade, A., Iwatsubo, M. (1975) Eur. J. Biochem. 57, 371-378
37. Veronese, F. M., Boccu, E., and Conventi, L. (1975) Biochim. Biophys. Acta 377,217-228
38. Lascu, I., Barzu, T., Ty, N. G., Ngoc, L. D., Barzu, O., and Mantsch, H. H. (1977) Biochim. Biophys. Acta 482, 251-260
39. Bonete, M. J., Pérez-Pomares, F., Ferrer, J., and Camacho, M. L. (1996) Biochim. Biophys. Acta 1289, 14-24
40. Fuge, E. K., Braun E. L., Werner-Washburne, M. (1994) J. Bacteriol. 176, 5802-5813
41. Mazón, M. J., and Hemmings, B. A. (1979) J. Bacteriol. 139, 686-689
42. Valenzuela, L., Ballario, P., Aranda, C., Filetici, P., and González, A. (1998) J. Bacteriol. 180, 3533-3540
43. Coschigano, P. W., Miller, S. M., and Magasanik, B. (1991) Mol. Cell. Biol. 11, 4455-4465
44. Liu, Z., and Butow, R. A. (1999) Mol. Cell. Biol. 19, 6720-6728
45. Shamji, A., Kuruvilla, F. G., and Schreiber, S. L. (2000) Curr. Biol. 10, 1574-1581
46. Kuruvilla, F. G., Shamji, A. F., and Schreiber, S. L. (2001) Proc. Natl. Acad. Sci. U. S. A. 98, 7283-7288
47. Romero, M., Guzmán-León, S., Aranda, C., González-Halphen, D., Valenzuela, L., and González, A. (2000) Microbiology 146, 239-245
48. ter Schure, E. G., van Riel, N. A., and Verrips, T. (2000) FEMS Microbiol. Rev. 24, 67-83
49. Kwast, K. E., Burke, P. V., and Poyton, R. O. (1998) J. Exp. Biol. 201, 1177-1195
50. Piškur, J. (2001) Trends Genet. 17, 302-303