Thioredoxin-dependent enzymatic activation of mercaptopyruvate sulfurtransferase: An intersubunit disulfide bond serves as a redox switch for activation

Journal of Biological Chemistry

Volumn 282, Issue 3, 2007, Pages 1561-1569

  Nagahara, Noriyuki ^a   Yoshii, Taro ^a   Abe, Yasuko ^a   Matsumura, Tomohiro ^a  

^a NIPPON MEDICAL SCHOOL   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYTIC SITE CYSTEINE; DISULFIDE BOND; ENZYMATIC ACTIVATION; HOMEOSTASIS; MONOMER TO DIMER RATIO; MONOMER-DIMER EQUILIBRIUM; POTASSIUM PHOSPHATE BUFFER; RAT 3-MERCAPTOPYRUVATE SULFURTRANSFERASE; THIOREDOXIN;

ACTIVATION ANALYSIS; AMINO ACIDS; CHEMICAL BONDS; ESCHERICHIA COLI; POTASSIUM COMPOUNDS; REDOX REACTIONS;

ENZYME KINETICS;

3 MERCAPTOPYRUVATE SULFURTRANSFERASE; CYSTEINE; DISULFIDE; DITHIOTHREITOL; GLUTATHIONE; PROTEIN SUBUNIT; SULFURTRANSFERASE; THIOREDOXIN; UNCLASSIFIED DRUG; 3 MERCAPTOPYRUVATE SULPHURTRANSFERASE; 3-MERCAPTOPYRUVATE SULPHURTRANSFERASE;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; DISULFIDE BOND; ENZYME ACTIVATION; ENZYME ACTIVITY; ESCHERICHIA COLI; HOMEOSTASIS; MAMMAL; MOLECULAR BIOLOGY; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FOLDING; RAT; STRUCTURE ACTIVITY RELATION; AMINO ACID SEQUENCE; ANIMAL; BINDING SITE; CHEMISTRY; METABOLISM; MOLECULAR GENETICS; PROTEIN BINDING; SEQUENCE HOMOLOGY;

ESCHERICHIA COLI; MAMMALIA; RATTUS;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CYSTEINE; DISULFIDES; DITHIOTHREITOL; ENZYME ACTIVATION; ESCHERICHIA COLI; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; PROTEIN BINDING; RATS; SEQUENCE HOMOLOGY, AMINO ACID; SULFURTRANSFERASES; THIOREDOXIN;

EID: 33847335589     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M605931200     Document Type: Article

References (45)

1. Clancey, C. J., and Gilbert, H. F. (1987) J. Biol. Chem. 262, 13545-13549
2. Hawkins, H. C., Blackburn, E. C., and Freedman, R. B. (1991) Biochem. J. 275, 349-353
3. Sasaki, Y., Kozaki, A., and Hatano, M. (1997) Proc. Natl. Acad. Sci. U. S. A. 94, 11096-11101
4. Mora-Garcia, S., Rodriguez-Suarez, R., and Wolosiuk, R. A. (1998) J. Biol. Chem. 273, 16273-16280
5. Zheng, M., Aslund, F., and Storz, G. (1998) Science 279, 1718-1721
6. Reynolds, C. M., and Poole, L. B. (2001) Biochemistry 40, 3912-3919
7. Buhrman, G., Parker, B., Sohn, J., Rudolph, J., and Mattos, C. (2005) Biochemistry 44, 5307-5316
8. Sevier, C. S., and Kaiser, C. A. (2006) Mol. Biol. Cell. 17, 2256-2266
9. Park, C., and Raines, R. T. (2001) Protein Eng. 14, 939-942
10. Suzuki, T., Suzuki, J., Mitome, N., Ueno, H., and Yoshida, M. (2000) J. Biol. Chem. 275, 37902-37906
11. Nagahara, N., and Nishino, T. (1996) J. Biol. Chem. 271, 27395-27401
12. Nagahara, N., Ito, T., and Minami, M. (1999) Histol. Histopathol. 14, 1277-1286
13. Nagahara, N., and Katayama, A. (2005) J. Biol. Chem. 280, 34569-34576
14. Taoka, S., Ohja, S., Shan, X., Kruger, W. D., and Banerjee, R. (1998) J. Biol. Chem. 273, 25179-25184
15. Mosharov, E., Cranford, M. R., and Banerjee, R. (2000) Biochemistry 39, 13005-13011
16. Chen, Z., Chakraborty, S., Shan, X., Kruger, W. D., and Banerjee, R. (1995) J. Biol. Chem. 270, 19246-19249
17. Nagahara, N., and Sawada, N. (2006) Curr. Med. Chem. 13, 1219-1230
18. Nagahara, N., Okazaki, T., and Nishino, T. (1995) J. Biol. Chem. 270, 16230-16235
19. Ploegman, J. H., Drent, G., Kalk, K. H., Hol, W. J. G., Heinrikson, R. L., Keim, P., Weng, L., and Russell, J. (1978) Nature 273, 124-129
20. Wang, Y., De Keulenaer, G. W., and Lee, R. T. (2002) J. Biol. Chem. 277, 26496-26500
21. Wollman, E. E., d'Auriol, L., Rimsky, L., Shaw, A., Jacquot, J. P., Wingfield, P., Graber, P., Dessarps, F., Robin, P., and Galibert, F. (1988) J. Biol. Chem. 263, 15506-15512
22. Powis, G., and Montfort, W. R. (2001) Annu. Rev. Pharmacol. Toxicol. 41, 261-295
23. Casagrande, S., Bonetto, V., Fratellim, M., Gianazza, E., Eberini, I., Massignan, T., Salmona, M., Chang, G., Holmgren, A., and Ghezzi, P. (2002) Proc. Natl. Acad. Sci. U. S. A. 99, 9745-9749
24. Musso, R., Di Lauro, R., Rosenberg, M., and de Crombrugghe, B. (1977) Proc. Natl. Acad. Sci. U. S. A. 74, 106-110
25. Holmgren, A. (1979) J. Biol. Chem., 254, 9627-9632
26. Park, E. M., and Thomas, J. A. (1989) Arch. Biochem. Biophys. 272, 25-31
27. Lundstrom, J., and Holmgren, A. (1990) J. Biol. Chem. 265, 9114-9120
28. Kallis, G. B., and Holmgren, A. (1980) J. Biol. Chem. 225, 10261-10265
29. Hama, H., Kayahara, T., Ogawa, W., Tsuda, M., and Tsuchiya, T. (1994) J. Biol. Chem. 115, 1135-1140
30. Papenbrock, J., and Schmidt, A. (2000) Eur. J. Biochem. 267, 145-154
31. Williams, R. A., Kelly, S. M., Mottram, J. C., and Coombs, G. H. (2003) J. Biol. Chem. 278, 1480-1486
32. Strausberg, R. L., Feingold, E. A., Grouse, L. H., Derge, J. G., Klausner, R. D., Collins, F. S., Wagner, L., Shenmen, C. M., Schuler, G. D., Altschul, S. F., Zeeberg, B., Buetow, K. H., Schaefer, C. F., Bhat, N. K., Hopkins, R. F., Jordan, H., Moore, T., Max, S. I., Wang, J., Hsieh, F., Diatchenko, L., Marusina, K., Farmer, A. A., Rubin, G. M., Hong, L., Stapleton, M., Soares, M. B., Bonaldo, M. F., Casavant, T. L., Scheetz, T. E., Brownstein, M. J., Usdin, T. B., Toshiyuki, S., Carninci, P., Prange, C., Raha, S. S., Loquellano, N. A., Peters, G. J., Abramson, R. D., Mullahy, S. J., Bosak, S. A., McEwan, P. J., McKernan, K. J., Malek, J. A., Gunaratne, P. H., Richards, S., Worley, K. C., Hale, S., Garcia, A. M., Gay, L. J., Hulyk, S. W., Villalon, D. K., Muzny, D. M., Sodergren, E. J., Lu, X., Gibbs, R. A., Fahey, J., Helton, E., Ketteman, M., Madan, A., Rodrigues, S., Sanchez, A., Whiting, M., Madan, A., Young, A. C., Shevchenko, Y., Bouffard, G. G., Blakesley, R. W., Touchman, J. W., Green, E. D., Dickson, M. C., Rodriguez, A. C., Grimwood, J., Schmutz, J., Myers, R. M., Butterfield, Y. S., Krzywinski, M. I., Skalska, U., Smailus, D. E., Schnerch, A., Schein, J. E., Jones, S. J., Marra, M. A., and Mammalian Gene Collection Program Team (2002) Proc. Natl. Acad. Sci. U. S. A. 99, 16899-16903
33. Pallini, R., Guazzi, G. C., Cannella, C., and Cacace, M. G. (1991) Biochem. Biophys. Res. Commum. 80, 887-893
34. Mikkelsen, R., Mutenda, K. E., Mant, A., Schurmann, P., and Blennow, A. (2005) Proc. Natl. Acad. Sci. U. S. A. 102, 1785-1790
35. Waksman, G., Krishna, T. S., Williams, C. H., Jr., and Kuriyan, J. (1994) J. Mol. Biol. 236, 800-816
36. Sandalova, T., Zhong, L., Lindqvist, Y., Holmgren, A., and Schneider, G. (2001) Proc. Natl. Acad. Sci. U. S. A. 98, 9533-9538
37. Kobayashi, F., Sagawa, N., Nanbu, Y., Kitaoka, Y., Mori, T., Fujii, S., Nakamura, H., Masutani, H., and Yodoi, J. (1995) Hum. Reprod. 10, 1603-1608
38. Nakamura, H., De Rosa, S., Roederer, M., Anderson, M. T., Dubs, J. G., Yodoi, J., Holmgren, A., Herzenberg, L. A., and Herzenberg, L. A. (1996) Int. Immunol. 8, 603-611
39. Kondo, N., Ishii, Y., Kwon, Y. W., Tanito, M., Horita, H., Nishinaka, Y., Nakamura, H., and Yodoi, J. (2004) J. Immunol. 172, 442-448
40. Loewy, A. G., Siekevitz, P., Menninger, J. R., and Gallant, J. (1991) Cell Structure and Function, 3rd Ed., Harcourt College Publishers, Orlando, FL
41. Guyton, A. C., and Hall, J. E. (2006) Textbook of Medical Physiology, 11th Ed., Elsevier/W. B. Saunders Co., Philadelphia
42. Nagahara, N., Ito, T., Kitamura, H., and Nishino, T. (1998). Histochem. Cell Biol. 110, 243-250
43. Larsson, A. (1973) Eur. J. Biochem. 35, 346-349
44. Martinez-Galisteo, E., Padilla, C. A., Garcia-Alfonso, C., Lopez-Barea, J., and Barcena, J. A. (1993) Biochimie (Paris) 75, 803-809
45. Gromer, S., Arscott, L. D., Williams, C. H., Jr., Schirmer, R. H., and Becker, K. (1998) J. Biol. Chem. 273, 20096-20101