D-glyceraldehyde-3-phosphate dehydrogenase: Structural basis and functional role of the acyl transfer reactions

Biochemistry (Moscow)

Volumn 63, Issue 5, 1998, Pages 504-515

  Nagradova, N K ^a   Schmalhausen, E V ^a  

^a MOSCOW STATE UNIVERSITY   (Russian Federation)

Author keywords

Acyl transfer; Catalytic mechanism; Cysteine residues; D glyceraldehyde 3 phosphate dehydrogenase; Sulfenic acid

Indexed keywords

CYSTEINE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE;

CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVE SITE; ENZYMOLOGY; GEOBACILLUS STEAROTHERMOPHILUS; METABOLISM; OXIDATIVE PHOSPHORYLATION; PROTEIN CONFORMATION; REVIEW;

BACILLUS STEAROTHERMOPHILUS; CATALYTIC DOMAIN; CYSTEINE; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASES; MODELS, CHEMICAL; MODELS, MOLECULAR; OXIDATIVE PHOSPHORYLATION; PROTEIN CONFORMATION;

EID: 0032058850     PISSN: 00062979     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (75)

1. Harris, J. I., and Waters, M. (1976) in The Enzymes (Boyer, P. D., ed.) Vol. 13, Academic Press, New York, pp. 1-49.
2. Cerff, R. (1978) Phytochemistry, 17, 2061-2067.
3. Ferri, G., Comerio, G., Iadarola, P., Zapponi, M. C., and Speranza, M. L. (1978) Biochim. Biophys. Acta, 522, 19-31.
4. Scagliarini, S., Trost, P., Pupillo, P., and Valenti, V. (1993) Planta, 190, 313-319.
5. Iglesias, A. A., Serrano, A., Guerrero, M. G., and Losada, M. (1987) Biochim. Biophys. Acta, 925, 1-10.
6. Iglesias, A. A., and Losada, M. (1988) Arch. Biochem. Biophys., 260, 830-840.
7. Serrano, A., Mateos, M. I., and Losada, M. (1993) Biochem. Biophys. Res. Commun., 197, 1348-1356.
8. Kelly, G. J., and Gibbs, M. (1973) Plant Physiol., 52, 674-676.
9. Habenicht, A., Hellman, U., and Cerff, R. (1994) J. Mol. Biol., 237, 165-171.
10. Michels, S., Scagliarini, S., Della Seta, F., Carles, C., Riva, M., Trost, P., and Branlant, G. (1994) FEBS Lett., 339, 97-100.
11. Trentham, D. R. (1970) Biochem. J., 122, 59-69.
12. Harrigan, P. G., and Trentham, D. R. (1973) Biochem. J., 135, 695-703.
13. Krimsky, I., and Racker, E. (1955) Science, 122, 319-321.
14. Harris, I., Meriwether, B. P., and Park, J. H. (1963) Nature (Lond.), 198, 154-157.
15. Malhotra, O. P., and Bernhard, S. A. (1968) J. Biol. Chem., 243, 1243-1252.
16. Furfine, C. S., and Velick, S. F. (1965) J. Biol. Chem., 240, 844-855.
17. Hilvers, A. G., and Weenen, J. H. M. (1962) Biochim. Biophys. Acta, 58, 380-383.
18. Harrigan, P. J., and Trentham, D. R. (1974) Biochem. J., 143, 353-363.
19. Malhotra, O. P., and Bernhard, S. A. (1973) Proc. Natl. Acad. Sci. USA, 70, 2077-2081.
20. Schwendiman, B., Ingbar, D., and Bernhard, S. A. (1976) J. Mol. Biol., 108, 123-138.
21. Malhotra, O. P., and Bernhard, S. A. (1981) Biochemistry, 20, 5529-5538.
22. Malhotra, O. P., and Bernhard, S. A. (1989) Bochemistry, 28, 124-128.
23. Buehner, M., Ford, G. C., Moras, D., Olsen, K. W., and Rossmann, M. G. (1974) J. Mol. Biol., 90, 25-49.
24. Moras, D., Olsen, K. W., Sabesan, M. N., Buehner, M., Ford, G. C., and Rossmann, M. G. (1975) J. Biol. Chem., 250, 9137-9162.
25. Mercer, W. D., Winn, S. I., and Watson, H. C. (1976) J. Mol. Biol., 104, 277-283.
26. Biesecker, G., Harris, J. I., Thierry, J. C., Walker, J. E., and Wonacott, A. J. (1977) Nature (London), 266, 328-333.
27. Skarzynski, T., Moody, P. C. E., and Wonacott, A. J. (1987) J. Mol. Biol., 193, 171-187.
28. Skarzynski, T., and Wonacott, A. J. (1988) J. Mol. Biol., 203, 1097-1118.
29. Vellieux, F. M. D., Hajdu, J., Verlinde, C. L. M. J., Groendijk, H., Read, R. J., Greenhough, T. J., Campbell, J. W., Kalk, K. H., Littlechild, J. A., Watson, H. C., and Hol, W. G. J. (1993) Proc. Natl. Acad. Sci. USA, 90, 2355-2359.
30. Lin, Z.-J., Li, J., Zhang, F.-M., Song, S.-Y., Yang, J., Liang, S.-J., and Tsou, C.-L. (1993) Arch. Biochem. Biophys., 302, 161-166.
31. Korndorfer, I., Steipe, B., Huber, R., Tomschiy, A., and Jaenicke, R. (1995) J. Mol. Biol., 246, 511-521.
32. Kim, H., Feil, I. K., Verlinde, L. M. J., Petra, P. H., and Hol, W. G. J. (1995) Biochemistry, 34, 14975-14986.
33. Duee, E., Olivier-Deyris, L., Fanchon, E., Corbier, C., Branlant, G., and Dideberg, O. (1996) J. Mol. Biol., 257, 814-838.
34. Tanner, J. J., Hecht, R. M., and Krause, K. L. (1996) Biochemistry, 35, 2597-2609.
35. Hol, W. G. J., van Duijnen, P. T., and Berendsen, H. J. C. (1978) Nature, 273, 443-446.
36. Hol, W. G. J. (1985) Progr. Biophys. Mol. Biol., 45, 149-195.
37. Lodi, P. J., and Knowles, J. R. (1991) Biochemistry, 30, 6948-6956.
38. Lodi, P. J., and Knowles, J. R. (1993) Biochemistry, 32, 4338-4343.
39. Doran, J. D., and Carey, P. R. (1996) Biochemistry, 35, 12495-12502.
40. Wassarman, P. N., and Major, J. P. (1969) Biochemistry, 8, 1076-1082.
41. Polgar, L. (1974) FEBS Lett., 38, 187-190.
42. Polgar, L. (1975) Eur. J. Biochem., 51, 63-71.
43. Halasz, P., and Polgar, L. (1977) Eur. J. Biochem, 79, 491-494.
44. Vas, M., and Boross, L (1974) Eur. J. Biochem, 43, 237-244.
45. Boross, L. (1969) Acta Biochim. Acad. Sci. Hung., 4, 57-69.
46. Banas, T., Banas, B., and Wolny, M. (1976) Eur. J. Biochem., 68, 313-319.
47. Moore, J., and Fenselau, A. (1972) Biochemistry, 11, 3762-3770.
48. Garavito, R. M., Rossmann, M. G., Argos, P., and Eventoff, W. (1977) Biochemistry, 16, 5065-5071.
49. Grau, U. M. (1982) in The Pyridine Nucleotide Coenzymes (Eversee, J., Andersen, B., and Kwan-Sa You, eds.) Academic Press, New York, pp. 135-187.
50. Asryants, R. A., Kuzminskaya, E. V., and Nagradova, N. K. (1989) Biochim. Biophys. Acta, 997, 159-166.
51. Parker, D. J., and Allison, W. S. (1969) J. Biol. Chem., 244, 180-189.
52. Ehring, R., and Colowick, S. P. (1969) J. Biol. Chem., 244, 4589-4599.
53. Allison, W. S., and Connors, M. J. (1970) Arch. Biochem. Biophys., 136, 383-391.
54. Allison, W. C., and Benitez, L. V. (1972) Proc. Natl. Acad. Sci. USA, 69, 3004-3008.
55. Allison, W. S., Swain, L. C., Tracy, S. M., and Benitez, L. V. (1973) Arch. Biochem. Biophys., 155, 400-404.
56. Allison, W. S., Benitez, L. V., and Johnson, C. L. (1973) Biochem. Biophys. Res. Commun., 52, 1403-1409.
57. Benitez, L. V., and Allison, W. S. (1974) J. Biol. Chem., 249, 6234-6243.
58. You, K.-Sa, Benitez, L. V., McConachie, W. A., and Allison, W. S. (1975) Biochim. Biophys. Acta, 384, 317-330.
59. Little, C., and O'Brien, P. J. (1969) Eur. J. Biochem., 10, 533-538.
60. Kuzminskaya, E. V., Asryants, R. A., and Nagradova, N. K. (1993) FEBS Lett., 336, 208-210.
61. Schmalhausen, E. V., Muronetz, V. I., and Nagradova, N. K. (1995) FEBS Lett., 375, 18-20.
62. Schmalhausen, E. V., Muronetz, V. I., Asryants, R. A., and Nagradova, N. K. (1996) Biochemistry (Moscow), 61, 384-393 (Russ.).
63. Schmalhausen, E. V., Muronetz, V. I., and Nagradova, N. K. (1997) FEBS Lett., 414, 247-252.
64. Schmalhausen, E. V., and Muronetz, V. I. (1998) Biosci. Rep., in press.
65. Poole, L. B., and Claiborne, A. (1989) J. Biol. Chem., 264, 12330-12338.
66. Ahmed, S. A., and Claiborne, A. (1989) J. Biol. Chem., 264, 19856-19863.
67. Yeh, J. I., Claiborne, A., and Hol, W. G. (1996) Biochemistry, 35, 9951-9957.
68. Claiborne, A., Ross, R. P., and Parsonage, D. (1992) Trends Biochem. Sci., 17, 183-186.
69. Claiborne, A., Miller, H., and Parsonage, D. (1993) FASEB J., 7, 1483-1490.
70. Abate, C., Patel, L., Rausher, F. J., III, and Curran, T. (1990) Science, 249, 1157-1161.
71. Storz, G., Tartaglia, L. A., and Ames, B. N. (1990) Science, 248, 189-194.
72. Kullik, I., Toledano, M. B., Tartaglia, L. A., and Storz, G. (1995) J. Bacteriol., 177, 1275-1284.
73. McBride, A. A., Klausner, R. D., and Howley, P. M. (1992) Proc. Natl. Acad. Sci. USA, 89, 7531-7535.
74. Bandyopadhyay, S., and Gronostajski, R. M. (1994) J. Biol. Chem., 269, 29949-29955.
75. Willett, W. S., and Copley, S. D. (1996) Chemistry and Biology, 3, 851-857.