The role of the flap residue, threonine 77, in the activation and catalytic activity of pepsin A

Protein Engineering

Volumn 12, Issue 1, 1999, Pages 55-61

  Okoniewska, M ^a   Tanaka, T ^a   Yada, R Y ^a  

^a UNIVERSITY OF GUELPH   (Canada)

Author keywords

Aspartic proteinases; Flap loop; Pepsin; Pepsinogen; Zymogen activation

Indexed keywords

AMINO ACID; MUTANT PROTEIN; PEPSIN A; PEPSINOGEN; THREONINE;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME STRUCTURE; HYDROGEN BOND; PRIORITY JOURNAL; PROTEIN DEGRADATION; STRUCTURE ACTIVITY RELATION;

EID: 0032972250     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/12.1.55     Document Type: Article

References (35)

1. Abad-Zapatero, C., Rydel, T.J. and Erickson, J. (1990) Proteins, 8, 62-81.
2. Al-Janabi., Hartsuck, J.A. and Tang, J. (1972) J. Biol. Chem., 241, 4628-4632.
3. Andreeva, N., Bochkarev, A. and Pechik, I. (1995) In Takahashi, K. (ed.), Aspartic Proteinases. Plenum Press, New York, pp. 19-32.
4. Bailey, D., Cooper, J.B., Veerapandian, B., Blundell, T.L., Atrash, B., Jones, D.M. and Szelke, M. (1993) Biochem. J., 289, 363-371.
5. Chang, C.T., Wu, C.-S.C. and Yang, J.T. (1978) Anal. Biochem., 91, 13-31.
6. Chen, L., Erickson, J.W., Rydel, T.J., Park, C.H., Neidhart, D., Luly, J. and Abad-Zapatero, C. (1992) Acta Crystallogr., B48, 476-488.
7. Cooper, J. and Newman, M.P. (1991) Adv. Exp. Biol. Med., 306, 47-61.
8. Cooper, J., Khan, G., Taylor, G., Tickle, I.J. and Blundell, T.L. (1990) J. Mol. Biol., 214, 199-222.
9. Dunn, B.M., Jimenez, M., Parten, B.F., Veller, M.J., Rolph, C.E. and Kay, J. (1986) Biochem. J., 237, 899-906.
10. Faust, P.L., Kornfeld, S. and Chirgwin, J.M. (1985) Proc. Natl Acad. Sci. USA. 82, 4910-4914.
11. Fruton, J.S. (1976) Adv. Enzymol., 44, 401-443.
12. Fujinaga, M., Chernaia, M.M., Tarasova, N.I., Mosimann, S.C. and James, M.N.G. (1995) Protein Sci., 4, 960-972.
13. Glick, M.D., Auer, H.E., Rich, D.H., Kawai, M. and Kamath, A. (1986) Biochemistry, 25, 1858-1864.
14. Glick, M.D., Shalitin, Y. and Hilt, C.R. (1989) Biochemistry, 28, 2626-2630.
15. Glick, M.D., Hilt, C.R. and Mende-Mueller, L. (1991) Int. J. Pept. Protein Res., 37, 230-235.
16. Guggenheim, E.A. (1926) Philos. Mag., 2, 538-543.
17. Hartsuck, J.A., Koelsch, G. and Remington, J.S. (1992) Proteins, 13, 1-25.
18. Hayano, T., Sogawa, K., Ichihara, Y., Fuji-Kuriyama, Y. and Takahashi, K. (1988) J. Biol. Chem., 263, 1382-1385.
19. James, M.N.G. and Sielecki, A.R. (1985) Biochemistry, 24, 3701-3713.
20. Kempner, E.S. (1993) FEBS Lett., 326, 4-10.
21. Kunkel, T.A. (1985) Proc. Natl Acad. Sci. USA, 82, 488-492.
22. Laemmli, U.K. (1970) Nature. 227, 680-685.
23. Lin, X.-L., Wong, R.N.S. and Tang, J. (1989) J. Biol. Chem., 264, 4482-4489.
24. Lin, Y., Fusek, M., Lin, X., Hartsuck, J.A., Kezdy, F.J. and Tang, J. (1992) J. Biol. Chem., 267, 18413-18418.
25. Lin, X.-I., Loy, J.A., Sussman, F. and Tang, J. (1993) Protein Sci., 2, 1383-1390.
26. Navia, M.A., Fitzgerald, P.M.D., McKeever, B.M., Leu, C.-T., Heimbach, J.C., Herber, W.K., Sigal, I.S., Darke, P.L. and Springer, J.P. (1989) Nature, 337, 615-620.
27. McPhie, P. (1976) Anal. Biochem., 73, 258-261.
28. Miller, M., Jaskolski, M., Rao, J.M.K., Leis, J. and Wlodawer, A. (1989) Nature, 337, 576-579.
29. Pearl, L.H. (1987) FEBS Lett., 214, 8-12.
30. Sakoda, M. and Hiromi, K. (1976) J. Biochem., 80, 547-555.
31. Shintani, T. Nomura, K. and Ichishima, E. (1997) J. Biol. Chem., 272, 18855-18861.
32. Sielecki, A.R., Fujinaga, M., Read, R.J. and James, M.N.G. (1990) J. Mol. Biol., 214, 143-170.
33. Sielecki, A.R., Fujinaga, M., Read, R.J. and James, M.N.G. (1991) J. Mol. Biol., 219, 671-692.
34. Tanaka, T. and Yada, R.Y. (1996) Biochem. J., 315, 443-446.
35. Tanaka, T. and Yada, R.Y. (1997) Arch. Biochem. Biophys., 340, 355-358.