Carboxy-monopeptidase substrate specificity of human cathepsin X

Biochemical and Biophysical Research Communications

Volumn 329, Issue 2, 2005, Pages 445-452

  Devanathan, Gopal ^a,b   Turnbull, Joanne L ^b   Ziomek, Edmund ^a   Purisima, Enrico O ^a   Ménard, Robert ^a   Sulea, Traian ^a  

^a NATIONAL RESEARCH COUNCIL CANADA   (Canada)

^b Gina Cody School of Engineering and Computer Science   (Canada)

Author keywords

Binding profile; Carboxypeptidase; Cathepsin X; Functional redundancy; Kinetics; Subsite specificity

Indexed keywords

AMINO ACID; ASPARAGINE; ASPARTIC ACID; CATHEPSIN; CATHEPSIN X; GLUTAMINE; GLYCINE; HISTIDINE; PEPTIDASE; PROLINE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CONTROLLED STUDY; ENZYME LOCALIZATION; ENZYME SPECIFICITY; ENZYME SUBSTRATE; KINETICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION;

EID: 14644411088     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.01.150     Document Type: Article

References (33)

1. D. Turk, and G. Guncar Lysosomal cysteine proteases (cathepsins): promising drug targets Acta Cryst. D 59 2003 203 213
2. H.A. Chapman, R.J. Riese, and G.P. Shi Emerging roles for cysteine proteases in human biology Annu. Rev. Physiol. 59 1997 63 88
3. D.P. Dickinson Cysteine peptidases of mammals: their biological roles and potential effects in the oral cavity and other tissues in health and disease Crit. Rev. Oral Biol. Med. 13 2002 238 275
4. F. Lecaille, J. Kaleta, and D. Bromme Human and parasitic papain-like cysteine proteases: their role in physiology and pathology and recent developments in inhibitor design Chem. Rev. 102 2002 4459 4488
5. V. Turk, B. Turk, G. Guncar, D. Turk, and J. Kos Lysosomal cathepsins: structure, role in antigen processing and presentation, and cancer Adv. Enzyme Regul. 42 2002 285 303
6. D.K. Nagler, and R. Menard Family C1 cysteine proteases: biological diversity or redundancy? Biol. Chem. 384 2003 837 843
7. R. Menard, T. Sulea, Cathepsin X, in: A.J. Barrett, N.D. Rawlings, J.F. Woessner (Eds.), Handbook of Proteolytic Enzymes, second ed., Elsevier, London, 2004, pp. 1113-1116
8. D.K. Nagler, and R. Menard Human cathepsin X: a novel cysteine protease of the papain family with a very short pro-region and unique insertions FEBS Lett. 434 1998 135 139
9. I. Santamaria, G. Velasco, A.M. Pendas, A. Fueyo, and C. Lopez-Otin Cathepsin Z, a novel human cysteine proteinase with a short propeptide domain and a unique chromosomal location J. Biol. Chem. 273 1998 16816 16823
10. J. Deussing, I. von Olshausen, and C. Peters Murine and human cathepsin Z: cDNA-cloning, characterization of the genes and chromosomal localization Biochim. Biophys. Acta 1491 2000 93 106
11. S. Hashmi, J. Zhang, Y. Oksov, and S. Lustigman The Caenorhabditis elegans cathepsin Z-like cysteine protease, Ce-CPZ-1, has a multifunctional role during the worms' development J. Biol. Chem. 279 2003 6035 6045
12. G. Rumpler, B. Becker, C. Hafner, M. McClelland, W. Stolz, M. Landthaler, R. Schmitt, A. Bosserhoff, and T. Vogt Identification of differentially expressed genes in models of melanoma progression by cDNA array analysis: SPARC, MIF and a novel cathepsin protease characterize aggressive phenotypes Exp. Dermatol. 12 2003 761 771
13. D.K. Nagler, S. Kruger, A. Kellner, E. Ziomek, R. Menard, P. Buhtz, M. Krams, A. Roessner, and U. Kellner Up-regulation of cathepsin X in prostate cancer and prostatic intraepithelial neoplasia Prostate 60 2004 109 119
14. D.K. Nagler, R. Zhang, W. Tam, T. Sulea, E.O. Purisima, and R. Menard Human cathepsin X: a cysteine protease with unique carboxypeptidase activity Biochemistry 38 1999 12648 12654
15. I. Klemencic, A.K. Carmona, M.H. Cezari, M.A. Juliano, L. Juliano, G. Guncar, D. Turk, I. Krizaj, V. Turk, and B. Turk Biochemical characterization of human cathepsin X revealed that the enzyme is an exopeptidase, acting as carboxy-monopeptidase or carboxy-dipeptidase Eur. J. Biochem. 267 2000 5404 5412
16. C. Therrien, P. Lachance, T. Sulea, E.O. Purisima, H. Qi, E. Ziomek, A. Alvarez-Hernandez, W.R. Roush, and R. Menard Cathepsins X and B can be differentiated through their respective mono- and dipeptidyl carboxypeptidase activities Biochemistry 40 2001 2702 2711
17. D.K. Nagler, W. Tam, A.C. Storer, J.C. Krupa, J.S. Mort, and R. Menard Interdependency of sequence and positional specificities for cysteine proteases of the papain family Biochemistry 38 1999 4868 4874
18. J. Sivaraman, D.K. Nagler, R. Zhang, R. Menard, and M. Cygler Crystal structure of human procathepsin X: a cysteine protease with the pro-region covalently linked to the active site cysteine J. Mol. Biol. 295 2000 939 951
19. G. Guncar, I. Klemencic, B. Turk, V. Turk, A. Karaoglanovic-Carmona, L. Juliano, and D. Turk Crystal structure of cathepsin X: a flip-flop of the ring of His23 allows carboxy-monopeptidase and carboxy-dipeptidase activity of the protease Structure Fold Des. 8 2000 305 313
20. A.J. Barrett, A.A. Kembhavi, M.A. Brown, H. Kirschke, C.G. Knight, M. Tamai, and K. Hanada l-Trans-epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L Biochem. J. 201 1982 189 198
21. W.D. Cornell, P. Cieplak, C.I. Bayly, I.R. Gould, K.M. Merz, D.M. Ferguson, D.C. Spellmeyer, T. Fox, J.W. Caldwell, and P.A. Kollman A second generation force field for the simulation of proteins, nucleic acids, and organic molecules J. Am. Chem. Soc. 117 1995 5179 5197
22. S.J. Weiner, P.A. Kollman, D.A. Case, U.C. Singh, C. Ghio, G. Alagona, S. Profeta Jr., and P. Weiner A new force field for molecular mechanical simulation of nucleic acids and proteins J. Am. Chem. Soc. 106 1984 765 784
23. T. Sulea, and E.O. Purisima Optimizing ligand charges for maximum binding affinity. A solvated interaction energy approach J. Phys. Chem. B 105 2001 889 899
24. L.T. Chong, S.E. Dempster, Z.S. Hendsch, L.-P. Lee, and B. Tidor Computation of electrostatic complements to proteins: a case of charge stabilizing binding Protein Sci. 7 1998 206 210
25. L.-P. Lee, and B. Tidor Barstar is electrostatically optimized for tight binding to barnase Nat. Struct. Biol. 8 2001 73 76
26. T. Sulea, and E.O. Purisima Profiling charge complementarity and selectivity for binding at the protein surface Biophys. J. 84 2003 2883 2896
27. E.O. Purisima Fast summation boundary element method for calculating solvation free energies of macromolecules J. Comput. Chem. 19 1998 1494 1504
28. E.O. Purisima, and S.H. Nilar A simple yet accurate boundary element method for continuum dielectric calculations J. Comput. Chem. 16 1995 681 689
29. S.-L. Chan, and E.O. Purisima Molecular surface generation using marching tetrahedra J. Comput. Chem. 19 1998 1268 1277
30. M.H.S. Cezari, L. Puzer, M.A. Juliano, A.K. Carmona, and L. Juliano Cathepsin B carboxypeptidase specificity analysis using internally quenched fluorescent peptides Biochem. J. 368 2002 365 369
31. M.F.M. Alves, L. Puzer, S.S. Cotrin, M.A. Juliano, L. Juliano, D. Bromme, and A.K. Carmona S3 to S3′ subsite specificity of recombinant human cathepsin K and development of selective internally quenched fluorescent substrates Biochem. J. 373 2003 981 986
32. L. Puzer, S.S. Cotrin, M.F. Alves, T. Egborge, M.S. Araujo, M.A. Juliano, L. Juliano, D. Bromme, and A.K. Carmona Comparative substrate specificity analysis of recombinant human cathepsin V and cathepsin L Arch. Biochem. Biophys. 430 2004 274 283
33. R. Menard, C. Therrien, P. Lachance, T. Sulea, H. Qi, A. Alvarez-Hernandez, and W.R. Roush Cathepsins X and B display distinct activity profiles that can be exploited for inhibitor design Biol. Chem. 382 2001 839 845