The activity of the Arabidopsis bifunctional lysine-ketoglutarate reductase/saccharopine dehydrogenase enzyme of lysine catabolism is regulated by functional interaction between its two enzyme domains

Journal of Biological Chemistry

Volumn 277, Issue 51, 2002, Pages 49655-49661

  Zhu, Xiaohong ^a   Tang, Guiliang ^a   Galili, Gad ^a  

^a WEIZMANN INSTITUTE OF SCIENCE   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CATALYSIS; DESORPTION; MASS SPECTROMETRY; MUTAGENESIS; PLANTS (BOTANY); POLYPEPTIDES; SODIUM CHLORIDE; YEAST;

CATABOLISM;

ENZYMES;

CASEIN KINASE II; SACCHAROPINE DEHYDROGENASE; SODIUM CHLORIDE;

ARABIDOPSIS; ARTICLE; DESORPTION; ENZYME ACTIVITY; ENZYME CONFORMATION; IONIZATION; MASS SPECTROMETRY; NONHUMAN; PHOSPHORYLATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN INTERACTION; SITE DIRECTED MUTAGENESIS;

ALANINE; ARABIDOPSIS; ASPARTIC ACID; CASEIN KINASE II; CHROMATOGRAPHY, GEL; DIMERIZATION; DOSE-RESPONSE RELATIONSHIP, DRUG; EGTAZIC ACID; LYSINE; MUTAGENESIS, SITE-DIRECTED; MUTATION; PHOSPHORYLATION; PLASMIDS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTEIN-SERINE-THREONINE KINASES; RECOMBINANT PROTEINS; SACCHAROPINE DEHYDROGENASES; SERINE; SODIUM CHLORIDE; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; THREONINE;

ANIMALIA; ARABIDOPSIS;

EID: 0037147307     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M205466200     Document Type: Article

References (20)

1. Arruda, P., Kemper, E. L., Papes, F., and Leite, A. (2000) Trends Plant Sci. 5, 324-330
2. Galili, G., Tang, G., Zhu, X., and Gakiere, B. (2001) Curr. Opin. Plant Biol. 4, 261-266
3. Markovitz, P. J., Chuang, D. T., and Cox, R. P. (1984) J. Biol. Chem. 259, 11643-11646
4. Woody, N. C. (1964) Am. J. Dis. Child 108, 543
5. Papes, F., Surpili, M. J., Langone, F., Trigo, J. R., and Arruda, P. (2001) FEBS Lett. 488, 34-38
6. Galili, G. (2002) Annu. Rev. Plant Physiol. Mol. Biol. 53, 27-43
7. Karchi, H., Shaul, O., and Galili, G. (1994) Proc. Natl. Acad. Sci. U. S. A. 91, 2577-2581
8. Moulin, M., Deleu, C., and Larher, F. (2000) Plant Physiol. Biochem. 38, 577-585
9. Zhu, X., Tang, G., Granier, F., Bouchez, D., and Galili, D. (2001) Plant Physiol. 126, 1539-1545
10. Karchi, H., Miron, D., Ben-Yaacov, S., and Galili, G. (1995) Plant Cell 7, 1963-1970
11. Miron, D., Ben-Yaacov, S., Karchi, H., and Galili, G. (1997) Plant J. 12, 1453-1458
12. Gaziola, A., Teixeira, C. M. G., Lugli, J., Sodek, L., and Azevedo, R. A. (1997) Eur. J. Biochem. 247, 364-371
13. Kemper, E. L., Cord-Neto, G., Capella, A. N., Goncalves-Butruile, M., Azevedo, R. A., and Arruda, P. (1998) Eur. J. Biochem. 253, 720-729
14. Zhu, X., Tang, G., and Galili, G. (2000) Plant Physiol. 124, 1363-1372
15. Zhu, X., Tang, G., and Galili, G. (2000) Biochem. J. 351, 215-220
16. Vernet, T., Dignard, D., and Thomas, D. Y. (1987) Gene 52, 225-233
17. Miron, D., Ben-Yaacov, S., Reches, C., Schupper, A., and Galili, G. (2000) Plant Physiol. 123, 655-663
18. Kemper, E. L., Neto, G. C., Papes, F., Moraes, K. C., Leite, A., and Arruda, P. (1999) Plant Cell 11, 1981-1994
19. Tang, G., Zhu, X., Tang, X., and Galili, G. (2000) Plant J. 23, 195-203
20. Tang, G., Zhu, X., Gakiere, B., Levanony, H., Kahana, A., and Galili, G. (2002) Plant Physiol. 130, 147-154