Role of arginine 38 in horseradish peroxidase: A critical residue for substrate binding and catalysis

Journal of Biological Chemistry

Volumn 271, Issue 8, 1996, Pages 4023-4030

  Rodriguez Lopez, Jose Neptuno ^a   Smith, Andrew T ^b   Thorneley, Roger N F ^a  

^a JOHN INNES CENTRE   (United Kingdom)

^b UNIVERSITY OF SUSSEX   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ASCORBIC ACID; BENZOTHIAZOLE DERIVATIVE; CRESOL; FERRIC ION; GUAIACOL; HORSERADISH PEROXIDASE; HYDROPEROXIDE;

ARTICLE; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME KINETICS; ENZYME MECHANISM; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; ESCHERICHIA COLI; PRIORITY JOURNAL; SPECTROPHOTOMETRY; STEADY STATE;

AMINO ACID SEQUENCE; ARGININE; BASE SEQUENCE; BINDING SITES; CATALYSIS; CRESOLS; DNA PRIMERS; GENES, SYNTHETIC; GUAIACOL; HORSERADISH PEROXIDASE; HYDROGEN PEROXIDE; KINETICS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; POINT MUTATION; POLYMERASE CHAIN REACTION; RECOMBINANT PROTEINS; SPECTROPHOTOMETRY; SUBSTRATE SPECIFICITY; VARIATION (GENETICS);

EID: 0030068091     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.271.8.4023     Document Type: Article

References (50)

1. Dunford, H. B., and Stillman, J S. (1976) Coord. Chem 19, 187-251
2. Welinder, K G. (1985) Eur. J. Biochem. 151, 497-504
3. Welinder, K. G (1979) Eur. J Biochem. 96, 483-502
4. Shiro, Y., Kurono, M., and Morishima, I. (1986) J. Biol. Chem. 261, 9382-9390
5. Poulos, T. L., and Kraut, J. (1980) J. Biol. Chem. 255, 8199-8205
6. Baek, H. K., and Van Wart, H. E. (1989) Biochemistry 28, 5714-5719
7. Baek, H. K., and Van Wart, H. E. (1992) J. Am. Chem. Soc 114, 718-725
8. Wang, J. S., Baeck, H. K., and Van Wart, H. E (1991) Biochem. Biophys. Res. Commun. 179, 1320-1324
9. Vitello, L. B., Erman, J. E., Miller, M A, Wang, J., and Kraut, J. (1993) Biochemistry 32, 9807-9818
10. Erman, J. E., Vitello, L. B., Miller, M. A , Shaw, A., Brown, K. A , and Kraut, J (1993) Biochemistry 32, 9798-9806
11. Modi, S., Behere, D. V., and Mitra, S. (1989) J Biol. Chem. 264, 19677-19684
12. Schejter, A., Lanir, A., and Epstein, N. (1976) Arch. Biochem Biophys. 174, 36-44
13. Leigh, J. S., Maltempo, M. M., Ohlsson, P. I., and Paul, K. G. (1975) FEBS Lett 51, 304-308
14. Veitch, N. C. (1995) Biochem. Soc. Trans. 23, 232-240
15. Ortiz de Montellano, P. R. (1992) Annu. Rev. Pharmacol Toxicol. 32, 89-107
16. Harris, R. Z., Newmyer, S. L., and Ortiz de Montellano, P. R. (1993) J. Biol. Chem. 268, 1637-1645
17. Smith, A. T., Santama, N., Dacey. S , Edwards, M , Bray, E. C , Thorneley, R. N. F., and Burke, J F. (1990) J. Biol. Chem 265, 13335-13343
18. Schonbaum, G. R., and Lo, S. (1972) J. Biol. Chem. 247, 3353-3360
19. Cotton, M. L., and Dunford, H. B. (1973) Can. J. Chem. 51, 582-587
20. Smith, A T., Sanders, S. A., Thorneley, R. N. F., Burke, J. F., and Bray, R. C. (1992) Eur. J. Biochem. 207, 507-519
21. Saunders, S., and Burke, J. F. (1990) Nucleic Acids Res. 18, 494S
22. Furhop, J. H., and Smith, K. M. (1975) in Phorphyrins and Metalloproteins (Smith, K. M., ed) pp. 757-869, Elsevier, Amsterdam
23. Draper, N. R., and Smith, H. (1981) Applied Regression Analysis, 2nd Ed., Wiley, New York
24. Wilkinson, G. N. (1961) Biochem. J. 80, 324-332
25. Smulevich, G., Paoli, M., Burke, J. F., Sanders, S A , Thorneley, R. N. F., and Smith, A. T. (1994) Biochemistry 33, 7398-7407
26. Bernasconi, C F. (1976) Relaxation Kinetics, Academic Press, New York
27. Hosoya, T., Sakurada, J., Kurokawa, C., Toyoda, R., and Nakamura, S. (1989) Biochemistry 28, 2639-2644
28. Critchlow, J E., and Dunford, H. B. (1972) J. Biol. Chem. 247, 3714-3725
29. Chang, C. S, Yamazaki, I., Sinclair, R., Khalid, S., and Powers, L. (1993) Biochemistry 32, 923-928
30. Balny, C., Travers, F., Barman, T., and Douzon, P. (1987) Eur. Biophys. J. 14, 375-383
31. Erman, J. E., Vitello, L B., Miller, M. A., and Kraut, J. (1992) J. Am. Chem. Soc. 114, 6592-6593
32. Smith, A. T., Sanders, S. A., Sampson, C., Bray, R. C., Burke, J. F., and Thorneley, R N F. (1993) in Plant Peroxidases Biochemistry and Physiology, Third International Symposium Proceedings (Welinder, K G., Rasmussen, S. K., Penel, C , and Greppin, H., eds) pp. 159-168, University of Geneva, Geneva, Switzerland
33. Yonetani, T , and Schleyer, H. (1976) J. Biol. Chem. 242, 1974-1979
34. Poulos, T. L., and Finzel, B. C. (1984) in Peptide and Protein Reviews (Hearn, M. T. L., ed) pp 115-171, Marcel Dekker, New York
35. Arasasingham, R. D , Cornman, C. R., and Balch, A. L. (1989) J. Am. Chem. Soc. 111, 7800-7805
36. Burstyn, J N., Roe, J. A., Mikzstal, A. R., Shaevitz, B. A., Lang, G, and Valentine, J. S. (1988) J. Am. Chem. Soc. 110, 1382-1388
37. Yonetani, T , and Anni, H. (1987) J. Biol. Chem. 262, 9547-9554
38. Miller, M. A., Shaw, A., and Kraut, J. (1994) Nature Struct. Biol 1, 524-531
39. Veitch, N. C., and Williams, R. J. P. (1990) Eur. J. Biochem. 189, 351-362
40. Bhattacharyya, D K., Bandyopadhyay, U , and Banerjee, R. K. (1993) J. Biol. Chem. 268, 22292-22298
41. Riordan, J. F , McElvany, K. D., and Borders, C. L., Jr. (1977) Science 195, 884-885
42. George, P. (1953) Arch. Biochem. Biophys. 41, 416-424
43. Farhangrazi, Z S., Copeland, B. R., Nakayama, T , Amachi, T., Yamazaki, I., and Powers, L. S. (1994) Biochemistry 33, 5647-5652
44. Vlahos, C. J., Ghalambor, M. A., and Dekker, E. E. (1985) J. Biol Chem. 260, 5480-5485
45. Kremer, A. B., Egan, R. M , and Sable, H. Z (1980) J. Biol. Chem 255, 2405-2410
46. Goodin, D. B., Mauk, A. G., and Smith, M. (1987) J. Biol. Chem. 262, 7719-7724
47. Mauro, J. M., Fishel, L. A., Hazzard, J. T., Meyer, T. E., Tollin, G., Cusanovich, M. A., and Kraut, J. (1988) Biochemistry 27, 6256-6262
48. Meunier, B., Rodriguez-Lopez, J. N., Smith, A. T., Thorneley, R. N. F., and Rich, P. R. (1995) Biochemistry, 34, 14687-14692
49. Mims, M. P., Porras, A. G., Olson, J. S., Noble, R W., and Peterson, J. A. (1983) J Biol. Chem. 258, 14219-14232
50. Babcock, G. T., and Varotsis, C. (1993) J. Bioenerg. Biomembr. 25, 71-80