A critical role for highly conserved Glu610 residue of oligopeptidase B from Trypanosoma brucei in thermal stability

Journal of Biochemistry

Volumn 147, Issue 2, 2010, Pages 201-211

  Mohd Ismail, Nor Ismaliza ^a   Yuasa, Tsuyoshi ^a   Yuasa, Keizo ^a   Nambu, Yuko ^a,c   Nisimoto, Makoto ^a   Goto, Masaki ^a   Matsuki, Hitoshi ^a   Inoue, Masahiro ^b   Nagahama, Masami ^a,d   Tsuji, Akihiko ^a  

^a UNIVERSITY OF TOKUSHIMA   (Japan)

^b KURUME UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^c KYOTO UNIVERSITY   (Japan)

^d MEIJI PHARMACEUTICAL UNIVERSITY   (Japan)

Author keywords

Oligopeptidase B; Prolyl oligopeptidase; Propeller domain; Thermal stability; Trypanosoma

Indexed keywords

ENZYME; GLUTAMIC ACID; OLIGOPEPTIDASE B; UNCLASSIFIED DRUG;

AFRICAN TRYPANOSOMIASIS; ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVE SITE; GENE MUTATION; HEAT TREATMENT; NONHUMAN; PROTEIN SECONDARY STRUCTURE; SITE DIRECTED MUTAGENESIS; THERMOSTABILITY; TRYPANOSOMA BRUCEI;

ADRENOCORTICOTROPIC HORMONE; ANIMALS; CALORIMETRY, DIFFERENTIAL SCANNING; CIRCULAR DICHROISM; ENZYME ACTIVATION; ENZYME STABILITY; GLUCAGON; GLUTAMIC ACID; HOT TEMPERATURE; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTOZOAN PROTEINS; SALTS; SERINE ENDOPEPTIDASES; TRYPANOSOMA BRUCEI BRUCEI; TRYPSIN; UREA;

TRYPANOSOMA; TRYPANOSOMA BRUCEI;

EID: 76949104934     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvp156     Document Type: Article

References (32)

1. Barrett, A.J. and Rawlings, N.D. (1995) Families and clans of serine peptiDases. Arch. Biochem. Biophys. 318, 247-250
2. Polgá r, L. (2002) The prolyl oligopeptiDase family. Cell. Mol. Life Sci. 59, 349-362
3. Fü lö p.V., Bö cskei, Z., and Polgá r, L. (1998) Prolyl oligopeptiDase: a usual beta-propeller domain regulates proteolysis. Cell 94, 161-170
4. Gé rczei, T., Kesurü , G.M., and Ná ray-Szabó , G. (2000) Construction of a 3D model of oligopeptiDase B, a potential processing enzyme in prokaryotes. J. Mol. Graph. Model 18, 7-17
5. Hiramatsu, H., Kyono, K., Higashiyama, Y., Fukushima, C., Shima, H., Sugiyama, S., Inaka, K., Yamamoto, A., and Shimizu, R. (2003) The structure and function of human dipeptidyl peptiDase IV, processing a unique eight-bladed b-propeller fold. Biochem. Biophys. Res. Commun. 302, 849-854
6. Maes, M., Goossens, F., Scharpé , S., Meltzer, H.Y., D'Hondt, P., and Cosyns, P. (1994) Lower serum prolyl endopeptiDase enzyme activity in major depression: further evidence that peptiDases play a role in the pathophysiology of depression. Biol. Psychiatry 35, 545-552
7. Wiedeman, P.E. and Trevillyan, J.M. (2003) Dipeptidyl peptiDase IV inhibitors for the treatment of impaired glucose tolerance and type 2 diabetes. Curr. Opin. Investig. Drugs 4, 412-420
8. Morty, R.E., Troeberg, L., Powers, J.C., Ono, S., LonsDale-Eccles, J.D., and Coetzer, T.H.T. (1998) A trypanosome oligopeptiDase as a target for the trypanociDal agents pentamidine, diminazene and suramin. FEBS Lett. 433, 251-256
9. Pacaud, M. and Richard, C. (1975) Protease II from Escherichia coli. Purification and characterization. J. Biol. Chem. 250, 7771-7779
10. Kanatani, A., MasuDa, T., ShimoDa, T., Misoka, F., Lin, X. S., Yoshimoto, T., and Tsuru, D. (1991) Protease II from Escherichia coli: sequencing and expression of the enzyme gene and characterization of the expressed enzyme. J. Biochem. 110, 315-320
11. Morty, R.E., Fü lö p.V., and Andrews, N.W. (2002) Substrate recognition properties of oligopeptiDase B from Salmonella enterica serovar Typhimurium. J. Bacteriol. 184, 3329-3337
12. Troeberg, L., Pike, R.N., Morty, R.E., Berry, R.K., Coetzer, T.H.T., and LonsDale-Eccles, J.D. (1996) Proteases from Trypanosoma brucei brucei. Purification, characterization and interactions with host regulatory molecules. Eur. J. Biochem. 238, 728-736
13. Morty, R.E., LonsDale-Eccles, J.D., Morehead, J., Caler, E. V., Mentele, R., Auerswald, E.A., Coetzer, T.H.T., Andrews, N.W., and Burleigh, B.A. (1999) OligopeptiDase B from Trypanosoma brucei, a new member of an emerging subgroup of serine oligopeptiDases. J. Biol. Chem. 274, 26149-26156
14. Santana, J.M., Grellier, P., Rodier, M.H., Schrevel, J., and Teixeira, A. (1992) Purification and characterization of a new 120 kDa alkaline proteinase of Trypanosoma cruzi. Biochem. Biophys. Res. Commun. 187, 1466-1473
15. Morty, R.E., Pellé , R., VaDá sz.I, Uzcanga, G.L., Seeger, W., and Bubis, J. (2005) OligopeptiDase B from Trypanosoma evansi. A parasite peptiDase that inactivates atrial natriuretic factor in the bloodstream of infected hosts. J. Biol. Chem. 280, 10925-10937
16. Guedes, H.L.M., Carneiro, M.P.D., Gomes, D.C.O., Rossi-Bergmanmn, B., and Simone, S.G. (2007) OligopeptiDase B from Leishmania amazonensis: molecular cloning, gene expression analysis and molecular model. Parasitol. Res. 101, 853-863
17. Tsuji, A., Yuasa, K., and MatsuDa, Y. (2004) Identification of oligopeptiDase B in higher plants. Purification and characterization of oligopeptiDase B from quiescent wheat embryo, Triticum aestivum. J. Biochem. 136, 673-681
18. Burleigh, B.A. and Woolsey, A.M. (2002) Cell signalling and Trypanosoma cruzi invasion. Cell. Microbiol. 4, 701-711
19. Morty, R.E., LonsDale-Eccles, J.D., Mentele, R., Auerswald, E.A., and Coetzer, T.H.T. (2001) Trypanosome-derived oligopeptiDase B is released into the plasma of infected rodents, where it persists and retains full catalytic activity. Infect. Immun. 69, 2757-2761
20. Rea, D., Hazell, C., Andrews, N.W., Morty, R.E., and Fü lö p.V. (2006) Expression, purification and preliminary crystallographic analysis of oligopeptiDase B from Trypanosoma brucei. Acta Crystallogr. Sect. F: Struct. Biol. Cryst. Commun. 62, 808-810
21. Morty, R.E., Shih, A.Y., Fü lö p.V., and Andrews, N.W. (2005) Identification of the reactive cysteine residues in oligopeptiDase B from Trypanosoma brucei. FEBS Lett. 579, 2191-2196
22. Coetzer, T.H.T., Goldring, J.P.D., and Huson, L.E.J. (2008) OligopeptiDase B: a processing peptiDase involved in pathogenesis. Biochimie 90, 336-344
23. Tsuji, A. and Kurachi, K. (1989) Isolation and characterization of a novel large protease accumulated in mammalian cells in the presence of inhibitors. J. Biol. Chem. 264, 16093-16099
24. Tsuji, A., Yoshimoto, T., Yuasa, K., and MatsuDa, Y. (2006) Protamine: a unique and potent inhibitor of oligopeptiDase B. J. Pep. Sci. 12, 65-71
25. Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
26. Laemmli, U.K. (1970) Cleavage of structure proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
27. Ellman, G.L. (1959) Tissue sulfhydryl groups. Arch. Biochem. Biophys. 82, 70-77
28. Polgá r, L. and Felfö ldi, F. (1998) OligopeptiDase B: cloning and probing stability under nonequilibrium conditions. Proteins 30, 424-434
29. Burleigh, B.A., Caler, E. V., Webster, P., and Andrews, N.W. (1997) A cytosolic serine endopeptiDase from Trypanosoma cruzi is required for the generation of Ca2 signaling in mammalian cells. J. Cell. Biol. 136, 609-620
30. Juhá sz, T., Szeltner, Z., Fü lö p.V., and Polgá r, L. (2005) Unclosed beta-propellers display stable structures: implications for substrate access to the active site of prolyl oligopeptiDase. J. Mol. Biol. 346, 907-917
31. Bastos, M. I., Grellier, P., Martins, N.F., CaDavid- Restrepo, G., de Souza-Ault, M.R., Augustyns, K., Teixeira, A.R., Schré vel, J., Maigret, B., Da Silveira, J.F., and Santana, J.M. (2005) Molecular, functional and structural properties of the prolyl oligopeptiDase of Trypanosoma cruzi (POP Tc80), which is required for parasite entry into mammalian cells. Biochem. J. 388, 29-38
32. Yang, G., Bai, A., Gao, L., Zhang, Z., Zheng, B., and Feng, Y. (2009) Glu88 in the non-catalytic domain of acylpeptide hydrolase plays dual roles: charge neutralization for enzymatic activity and formation of salt bridge for thermodynamic stability. Biochim. Biophys. Acta 1794, 94-102