Purification and characterization of dipeptidase hydrolyzing L-cysteinylglycine from radish cotyledon

Bioscience, Biotechnology and Biochemistry

Volumn 71, Issue 12, 2007, Pages 3102-3104

  Kumada, Henri Obadja ^a,b   Koizumi, Yukio ^a   Sekiya, Jiro ^a,c  

^a KYOTO UNIVERSITY   (Japan)

^b KYOTO PHARMACEUTICAL UNIVERSITY   (Japan)

^c Ukyo ku   (Japan)

Author keywords

Dipeptidase; Glutathione catabolism; L cysteinylglycine; Radish; Raphanus sativus L.

Indexed keywords

AMINO ACIDS; PLANTS (BOTANY); PROTEINS; PURIFICATION;

GLUTATHIONE CATABOLISM; HEXAMERIC METALLOENZYME;

ENZYME ACTIVITY;

CYSTEINYLGLYCINE; DIPEPTIDASE; DIPEPTIDE; VEGETABLE PROTEIN;

ARTICLE; COTYLEDON; ENZYMOLOGY; HYDROLYSIS; ISOLATION AND PURIFICATION; METABOLISM; RADISH; STEREOISOMERISM;

COTYLEDON; DIPEPTIDASES; DIPEPTIDES; HYDROLYSIS; PLANT PROTEINS; RAPHANUS; STEREOISOMERISM;

EMBRYOPHYTA; RAPHANUS SATIVUS;

EID: 37649000618     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.70443     Document Type: Article

References (19)

1. Meister, A., and Anderson, M. E., Glutathione. Annu. Rev. Biochem., 52, 711-760 (1983).
2. Meister, A., Glutathione metabolism and its selective modification. J. Biol. Chem., 263, 17205-17208 (1988).
3. Jaspers, C. J., Gigot, D., and Penninckx, M. J., Pathways of glutathione degradation in the yeast Saccharomyces cerevisiae. Phytochemistry, 24, 703-707 (1985).
4. Suzuki, H., Hashimoto, W., and Kumagai, H., Glutathione metabolism in Escherichia coli. J. Mol. Cat. B: Enzymatic, 6, 175-184 (1999).
5. Olson, C. K., and Binkley, F., Metabolism of glutathione: III. Enzymatic hydrolysis of cysteinylglycine. J. Biol. Chem., 186, 731-735 (1950).
6. Satoh, S., Keida, Y., Konta, Y., Maeda, M., Matsumoto, Y., Niwa, M., and Kohsaka, M., Purification and molecular cloning of mouse renal peptidase. Biochim. Biophys. Acta, 1163, 234-242 (1993).
7. Campbell, B. J., Forrester, L. J., Zahler, W. L., and Burks, M., β-Lactamase activity of purified and partially characterized human renal dipeptidase. J. Biol. Chem., 259, 14586-14590 (1984).
8. Adachi, H., Kubota, I., Okamura, N., Iwata, H., Tsujimoto, M., Nakazato, H., Nishihara, T., and Noguchi, T., Purification and characterization of human microsomal dipeptidase. J. Biochem., 105, 957-961 (1989).
9. Murata, K., Iba, Y., Inoue, Y., and Kimura, A., L-Leucine and its analogue: specific inhibitors for S-benzyl-L-cysteine-p- nitroanilide-hydrolyzing enzyme in Escherichia coli B. Biochem. Biophys. Res. Commun., 153, 767-772 (1988).
10. Suzuki, H., Kim, E.-S., Yamamoto, N., Hashimoto, W., Yamamoto, K., and Kumagai, H., Mapping, cloning, and DNA sequencing of pepB which encodes peptidase B of Escherichia coli K-12. J. Ferment. Bioeng., 82, 392-397 (1996).
11. Schneider, A., and Rennenberg, H., Degradation of glutathione (GSH) in heterotrophic tobacco cells. Phyton, 32, 113-117 (1992).
12. Bergmann, L., and Rennenberg, H., Glutathione metabolism in plants. In "Sulfur Nutrition and Assimilation in Higher Plants," eds. De Kok, L. J., Stulen, I., Rennenberg, H., Brunold, C., and Rauser, W. E., SPB Academic Publishing, The Hague, pp. 109-123 (1993).
13. Nakano, Y., Okawa, S., Yamauchi, T., Koizumi, Y., and Sekiya, J., Occurrence of two forms of γ-glutamyltransferases in radish plant. Plant Biotechnol., 21, 243-246 (2004).
14. Nakano, Y., Okawa, S., Prieto, R., and Sekiya, J., Subcellular localization and possible functions of γ-glutamyltransferase in the radish (Raphanus sativus L.) plant. Biosci. Biotechnol. Biochem., 70, 1790-1793 (2006).
15. Gaitonde, M. K., A spectrophotometric method for the direct determination of cysteine in the presence of other naturally occurring amino acids. Biochem. J., 104, 627-633 (1967).
16. Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-254 (1976).
17. Davis, B. J., Disc electrophoresis: II. Method and application to human serum proteins. Ann. NY Acad. Sci., 121, 404-427 (1964).
18. Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
19. Miller, C. G., and Mackinnon, K., Peptidase mutants of Salmonella typhimurium. J. Bacteriol., 120, 355-363 (1974).