Kinetic and Mechanistic Studies of Prolyl Oligopeptidase from the Hyperthermophile Pyrococcus furiosus

Journal of Biological Chemistry

Volumn 276, Issue 22, 2001, Pages 19310-19317

  Harris, Michael N ^a   Madura, Jeffry D ^b   Ming, Li June ^a   Harwood, Valerie J ^a  

^a UNIVERSITY OF SOUTH FLORIDA   (United States)

^b DUQUESNE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CRYSTAL STRUCTURE; ENTHALPY; ENTROPY; HIGH TEMPERATURE EFFECTS; HYDROGEN BONDS; IONIZATION; NEUROLOGY; PH EFFECTS; REACTION KINETICS; THERMODYNAMIC STABILITY;

PHYLOGENETIC DOMAINS;

ENZYMES;

PROLYL ENDOPEPTIDASE; WATER; DEUTERIUM OXIDE; HYDROGEN; SERINE PROTEINASE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; ENTHALPY; ENTROPY; ENZYME ISOLATION; ENZYME KINETICS; ENZYME LOCALIZATION; ENZYME MECHANISM; ENZYME STABILITY; ENZYME STRUCTURE; HIGH TEMPERATURE; HYDROGEN BOND; NONHUMAN; PH; PHYLOGENY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PROCESSING; PYROCOCCUS FURIOSUS; SEQUENCE ALIGNMENT; TEMPERATURE DEPENDENCE; THERMOSTABILITY; AMINO ACID SEQUENCE; ANIMAL; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME SPECIFICITY; ENZYMOLOGY; HYDROLYSIS; KINETICS; METABOLISM; MOLECULAR EVOLUTION; MOLECULAR GENETICS; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; SWINE; TEMPERATURE;

ARCHAEA; BACTERIA (MICROORGANISMS); MAMMALIA; PYROCOCCUS; PYROCOCCUS FURIOSUS; SUIDAE;

AMINO ACID SEQUENCE; ANIMALS; CATALYSIS; DEUTERIUM OXIDE; EVOLUTION, MOLECULAR; HYDROGEN; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KINETICS; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PYROCOCCUS FURIOSUS; SEQUENCE HOMOLOGY, AMINO ACID; SERINE ENDOPEPTIDASES; SUBSTRATE SPECIFICITY; SWINE; TEMPERATURE; WATER;

EID: 0035379671     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M010489200     Document Type: Article

References (44)

1. Bauer, M. W., and Kelly, R. M. (1998) Biochemistry 37, 1710-1718
2. Kaper, T., Lebbink, J. H. G., Pouwels, J., Kopp, J., Schulz, G. E., van der Oost, J., and de Vos, W. M. (2000) Biochemistry 39, 4963-4970
3. Britton, K. L., Baker, P. J., Borges, K. M., Engel, P. C., Pasquo, A., Rice, D. W., Robb, F. T., Scandurra, R., Stillman, T. J., and Yip, K. S. (1995) Eur. J. Biochem. 229, 688-695
4. Vetriani, C., Maeder, D., Tolliday, N., Yip, K. S., Stillman, T. J., Britton, K. L., Rice, D. W., Klump, H. H., and Robb, T. T. (1998) Proc. Natl. Acad. Sci. U. S. A. 95, 12300-12305
5. Harwood, V. J., Denson, J. D., Robinson-Bidle, K. A., and Schreier, H. J. (1997) J. Bacteriol. 179, 3613-3618
6. Koida, M., and Walter, R. (1976) J. Biol. Chem. 251, 7593-7599
7. Robinson, K. A., Bartley, D. A., Robb, F. T., and Schreier, H. J. (1995) Gene 152, 103-106
8. Rennex, D., Hemmings, B. A., Hofsteenge, J., and Stone, S. R. (1991) Biochemistry 30, 2195-2203
9. Rawlings, N. D., and Barrett, A. J. (1994) Methods Enzymol. 244, 19-61
10. Walter, R., Shlank, H., Glass, J. D., Schwartz, I. L., and Kerenyi, T. D. (1971) Science 173, 827-829
11. Yoshimoto, T., Nishimura, T., Kita, T., and Tsuru, D. (1983) J. Biochem. 94, 1179-1190
12. Yoshimoto, T., Simmons, W. H., Kita, T., and Tsuru, D. (1981) J. Biochem. 90, 325-334
13. Sattar, A. K. M. A., Yoshimoto, T., Yamamoto, N., and Tsuru, D. (1990) J. Biochem. 107, 256-261
14. Yoshimoto, T., Sattar, A. K. M. A., Hirose, W., and Tsuru, D. (1988) J. Biochem. 104, 622-627
15. Kantani, A., Yoshimoto, T., Kitazono, A., Kokubo, T., and Tsuru, D. (1993) J. Biochem. 113, 790-796
16. Chevallier, S. P., Goeltz, P. T., Banville, D., and Gagnon J. (1992) J. Biol. Chem. 267, 8192-8199
17. Szwajcer-Dey, E., Rasmussen, J., Meldal, M., and Breddam, K. (1992) J. Bacteriol. 174, 2454-2459
18. Blumberg, S., Teichberg, V. I., Charli, J. L., Hersh, L. B., and McKelvy, J. F. (1980) Brain Res. 192, 477-486
19. Hersh, L. B., and McKelvy, J. F. (1979) Brain Res. 168, 553-564
20. Yoshimoto, T., Kado, K., Matsubara, F., Koriyama, N., Kaneto, H., and Tsuru, D. (1987) J. Pharmacobio-Dyn. 10, 730-735
21. Fulop, V., Bocskei, Z., and Polgar, L. (1998) Cell 94, 161-170
22. Glasoe, P. K., and Long, F. A. (1960) J. Phys. Chem. 64, 188-190
23. Levitt, M. (1992) J. Mol. Biol. 266, 507-533
24. Fechteler, T., Dengler, U., and Schomburg, D. (1995) J. Mol. Biol. 253, 114-131
25. Walter, R., and Yoshimoto, T. (1978) Biochemistry 17, 4139-4144
26. Yoshimoto, T., Walter, R., and Tsuru, D. (1980) J. Biol. Chem. 255, 4786-4792
27. Venkatasubban, K. S., and Schowen, R. L. (1986) CRC Crit. Rev. Biochem. 17, 1-44
28. Bender, M. J., Clement, G. E., Kezdy, F. J., and Heek, H. D. (1964) J. Am. Chem. Soc. 86, 3680-3684
29. Polgar, L. (1991) Eur. J. Biochem. 197, 441-447
30. Polgar, L. (1992) Biochem. J. 283, 647-648
31. Polgar, L. (1992) Biochemistry 31, 7729-7735
32. Polgar, L. (1993) FEBS Lett. 322, 227-230
33. Moriyama, A., Nakanishi, M., and Sasaki, M. (1988) J. Biochem. 104, 112-117
34. Morris, A. L., MacArthur, M. W., Hutchinson, E. G., and Thorton, J. M. (1992) Proteins Struct. Funct. Genet. 12, 345-364
35. Izatt, R. M., and Christensen, J. J. (1976) in Handbook of Biochemistry and Molecular Biology (Fasman, G. D., ed) 3rd ed, Physical Chemical Data, Vol. 1, pp. 151-269, CRC Press, New York
36. Burlini, N., Magnani, P., Villa, A., Macchi, F., Tortora, P., and Guerritore, A. (1992) Biochim. Biophys. Acta 1122, 283-292
37. Cowan, D. A., and Daniel, R. M. (1982) Biochim. Biophys. Acta 705, 293-305
38. Kabashima, T., Fujii, M., Meng, Y., Ito, K., and Yoshimoto, T. (1998) Arch. Biochem. Biophys. 358, 141-148
39. Yang, J. J., Artis, D. R., and Van Wart, H. E. (1994) Biochemistry 33, 6516-6523
40. Shapiro, R., Holmquist, B., and Riordan, J. F. (1983) Biochemistry 22, 3850-3857
41. Cornish-Bowden, A. (1995) Fundamentals of Enzyme Kinetics, revised ed., pp. 112-114, Portland, London
42. Riordan, J. F. (1979) Mol. Cell. Biochem. 14, 4699-4704
43. Segal, I. H. (1975) Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and steady-State Enzyme Systems, pp. 1-950, Wiley, New York
44. Pauling, L. (1948) The Nature of the Chemical Bond, 2nd ed., p. 333, Cornell University Press, Ithaca, NY