Catalytic properties of the caspases

Cell Death and Differentiation

Volumn 6, Issue 11, 1999, Pages 1054-1059

  Stennicke, H R ^a   Salvesen, G S ^a  

^a BURNHAM INSTITUTE   (United States)

Author keywords

Caspase; Catalytic mechanism; Protease; Proteolysis

Indexed keywords

ASPARTIC ACID; CASPASE; ENZYME PRECURSOR; GRANZYME B; INTERLEUKIN 1BETA CONVERTING ENZYME;

APOPTOSIS; BINDING SITE; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; HYDROLYSIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; REVIEW; STRUCTURE ACTIVITY RELATION;

MAMMALIA;

EID: 0032762563     PISSN: 13509047     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.cdd.4400599     Document Type: Review

References (60)

1. Alnemri ES, Livingston DJ, Nicholson DW, Salvesen G, Thornberry NA, Wong WW and Yuan J (1996) Human ICE/CED-3 protease nomenclature. Cell 87: 171
2. Lewis ER, Johnson FA and Shafer JA (1981) Effect of cystein-25 on th ionization of histidine-159 in papain as determined by proton nuclear magnetic resonance spectroscopy. Evidence for a His-159-Cys-25 ion pair and its possible role in catalysis. Biochemistry 20: 48-51
3. Vernet T, Tessier DC, Chatellier J, Plouffe C, Lee TS, Thomas DY, Storer AC and Menard R (1995) Structural and functional roles of asparagine 175 in the cysteine protease papain. J. Biol. Chem. 270: 16645-16652
4. Wilson KP, Black JA, Thomson JA, Kim EE, Griffith JP, Navia MA, Murcko MA, Chambers SP, Aldape RA, Raybuck SA and Livingston DJ (1994) Structure and mechanism of interleukin-1 beta converting enzyme. Nature 370: 270-275
5. Rotonda J, Nicholson DW, Fazil KM, Gallant M, Gareau Y, Labelle M, Peterson EP, Rasper DM, Tuel R, Vaillancourt JP, Thornberry NA and Becher JW (1996) The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis. Nature Struct. Biol. 3: 619-625
6. Bateman A, Birney E, Durbin R, Eddy SR, Finn RD and Sonnhammer EL (1999) Pfam 3.1: 1313 multiple alignments and profile HMMs match the majority of proteins. Nucleic Acids Res. 27: 260-262
7. Stennicke HR and Salvesen GS (1997) Biochemical characteristics of caspases-3, -6, -7, and -8. J. Biol. Chem. 272: 25719-25723
8. Garcia-Calvo M, Peterson EP, Rasper DM, Vaillancourt JP, Zamboni R, Nicholson DW and Thornberry NA (1999) Purification and catalytic properties of human caspase family members. Cell Death Diff. 6: 362-369
9. Menard R, Carriere J, Laflamme P, Plouffe C, Khouri HE, Vernet T, Tessier DC, Thomas DY and Storer AC (1991) Contribution of the glutamine 19 side chain to transition-state stabilization in the oxyanion hole of papain. Biochemistry 30: 8924-8928
10. Schroder E, Phillips C, Garman E, Harlos K and Crawford C (1993) X-ray crystallographic structure of a papain-leupeptin complex. FEBS Lett. 315: 38-42
11. Thornberry NA, Bull HG, Calaycay JR, Chapman KT, Howard AD, Kostura MJ, Miller DK, Molineaux SM, Weidner JR, Aunins J, Elliston KO, Ayala JM, Casano FJ, Chin J, Ding GJF, Egger LA, Gaffney EP, Limjuco G, Palyha OC, Raju SM, Rolando AM, Salley JP, Yamin TT and Tocci MJ (1992) A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes. Nature 356: 768-774
12. Shaw E (1990) Cysteinyl proteinases and their selective inactivation. Adv. Enzymol. Relat. Areas Mol. Biol. 63: 271-347
13. Berger A and Schechter I (1970) Mapping the active site of papain with the aid of peptide substrates and inhibitors. Philos. Trans. R. Soc. London. [Biol.]. 257: 249-264
14. Stennicke HR, Birktoft JJ and Breddam K (1996) Characterization of the S1 binding site of the glutamic acid-specific protease from Streptomyces griseus. Protein Sci. 5: 2266-2275
15. Breddam K and Meldal M (1992) Substrate preferences of glutamic-acid-specific endopeptidases assessed by synthetic peptide substrates based on intramolecular fluorescence quenching. Eur. J. Biochem. 206: 103-107
16. Frigerio F, Coda A, Pugliese L, Lionetti C, Menegatti E, Amiconi G, Schnebli HP, Ascenzi P and Bolognesi M (1992) Crystal and molecular structure of the bovine alpha-chymotrypsin-eglinccomplexat2.0 Å resolution. J. Mol. Biol. 225: 107-123
17. Heinz DW, Priestle JP, Rahuel J, Wilson KS and Grütter MG (1991) Refined crystal structures of subtilisin novo in complex with wild-type and two mutant eglins. Comparison with other serine proteinase inhibitor complexes. J. Mol. Biol. 217: 353-371
18. Drenth J, KaIlk KH and Swen HM (1976) Binding of chloromethyl ketone substrate analogues to crystalline papain. Biochemistry 15: 3731-3738
19. Thornberry NA, Rano TA, Peterson EP, Rasper DM, Timkey T, Garcia-Calvo M, Houtzager VM, Nordstrom PA, Roy S, Vaillancourt JP, Chapman KT and Nlcholson DW (1997) A combinatorial approach defines specificities of members of the caspase family and granzyme B. J. Biol. Chem. 272: 17907-17911
20. Talanian RV, Quinlan C, Trautz S, Hackett MC, Mankovich JA, Banach D, Ghayur T, Brady KD and Wong WW (1997) Substrate specificities of caspase family proteases. J. Biol. Chem. 272: 9677-9682
21. Gron H, Meldal M and Breddam K (1992) Extensive comparison of the substrate preference of two subtilisins as determined with peptide substrates which are based on the principle of intramolecular quenching. Biochemistry 31: 6011-6018
22. Takahashi A, Alnemri ES, Lazebnik YA, Fernandes-Alnemri T, Litwack G, Moir RD, Goldman RD, Poirier GG, Kaufmann SH and Earnshaw WC (1996) Cleavage of lamin A by Mch2 alpha but no CPP32: multiple interleukin 1 beta-converting enzyme-related proteases with distinct substrate recognition properties are active in apoptosis. Proc. Natl. Acad. Sci. U.S.A. 93: 8395-8400
23. Perry DK, Smyth MJ, Stennicke HR, Salvesen GS, Duriez P, Poirier GG and Hannum YA (1997) Zinc is a potent inhibitor of the apoptotic protease, caspase-3. A novel target for zinc in the inhibition of apoptosis. J. Biol. Chem. 272: 18530-18533
24. Bian X, Hughes Jr FM, Huang Y, Cidlowski JA and Putney Jr JW (1997) Roles of cytoplasmic Ca2+ and intracellular Ca2+ stores in induction and suppression of apoptosis in S49 cells. Am. J. Physiol. 272: C1241-C1249
25. Cygler M, Sivaraman J, Grochulski P, Coulombe R, Storer AC and Mort JS (1996) Structure of rat procathepsin B: model for inhibition of cysteine protease activity by the proregion. Structure 4: 405-416
26. Coulombe R, Grochulski P, Sivaraman J, Menard R, Mort JS and Cygler M (1996) Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment. EMBO J. 15: 5492-5503
27. Gallagher T, Gilliland G, Wang L and Bryan P (1995) The prosegment-subtilisin BPN' complex: crystal structure of a specific 'foldase'. Structure 3: 907-914
28. Jain SC, Shinde U, Li Y, Inouye M and Berman HM (1998) The crystal structure of an autoprocessed Ser221Cys-subtilisin E-propeptide complex at 2.0 A resolution. J. Mol. Biol. 284: 137-144
29. Peters RJ, Shiau AK, Sohl JL, Anderson DE, Tang G, Silen JL and Agard DA (1998) Pro region C-terminus:protease active site interactions are critical in catalyzing the folding of alpha-lytic protease. Biochemistry 37: 12058-12067
30. Sauter NK, Mau T, Rader SD and Agard DA (1998) Structure of alpha-lytic protease complexes with its pro region. Nat. Struct. Biol. 5: 945-950
31. Hu Z, Haghjoo K and Jordan F (1996) Further evidence for the structure of the subtilisin propeptide and for its interactions with mature subtilisin. J. Biol. Chem. 271: 3375-3384
32. Markaryan A, Lee JD, Sirakova TD and Kolattukudy PE (1996) Specific inhibition of mature fungal serine proteinases and metalloproteinases by their propeptides. J. Bacteriol. 178: 2211-2215
33. Cygler M and Mort JS (1997) Proregion structure of members of the papain superfamily. Mode of inhibition of enzymatic activity. Biochimie 79: 645-652
34. Baker D, Silen JL and Agard DA (1992) Protease pro region required for folding is a potent inhibitor of the mature enzyme. Proteins 12: 339-344
35. Freer ST, Kraut J, Robertus JD, Wright HT and Xuong NH (1970) Chymotrypsinogen: 2.5-angstrom crystal structure, comparison with alpha-chymotrypsin, and implications for zymogen activation. Biochemistry 9: 1997- 2009
36. Fehlhammer H, Bode W and Huber R (1977) Crystal structure of bovine trypsinogen at 1-8 A resolution. II. Crystallographic refinement, refined crystal structure and comparison with bovine trypsin. J. Mol. Biol. 111: 415-438
37. Wang D, Bode W and Huber R (1985) Bovine chymotrypsinogen A X-ray crystal structure analysis and refinement of a new crystal form at 1.8 A resolution. J. Mol. Biol. 185: 595-624
38. Bode W (1979) The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding: the binding of the pancreatic trypsin inhibitor and of isoleucine-valine and of sequentially related peptides to trypsinogen and tc p-guanidinobenzoate-trypsinogen. J. Mol. Biol. 127: 357-374
39. Buckley CD, Pilling D, Henriquez NV, Parsonage G, Threlfall K, Scheel-Toellner D, Simmons DL, Akbar AN, Lord JM and Salmon M (1999) RGD peptides induce apoptosis by direct caspase-3 activation. Nature 397: 534-539
40. Yamin T-T, Ayala JM and Miller DK (1996) Activation of the native 45-kDa precursor form of interleukin-1-converting enzyme. J. Biol. Chem. 271: 13273-13282
41. Stennicke HR, Jurgensmeier JM, Shin H, Deveraux Q, Wolf BB, Yang X, Zhou Q, Ellerby HM, Ellerby LM, Bredesen D, Green DR, Reed JC, Froelich CJ and Salvesen GS (1998) Pro-caspase-3 is a major physiologic target of caspase-8. J. Biol. Chem. 273: 27084-27090
42. Li P, Nijhawan D, Budihardjo I, Srinivasula SM, Ahmad M, Alnemri ES and Wang X (1997) Cytochrome c and dATP-dependent formation of Apaf-1/Caspase-9 complex initiates an apoptotic protease cascade. Cell 91: 479-489
43. Duan H, Orth K, Chinnaiyan AM, Poirier GG, Froelich CJ, He W-Wand Dixit VM (1996) ICE-LAP6, a novel member of the ICE/Ced-3 gene family, is activated by the cytotoxíc T cell protease granzyme B. J. Biol. Chem. 271: 16720-16724
44. Srinivasula SM, Fernandes-Alnemri T, Zangrilli J, Robertson N, Armstrong RC, Wang L, Trapani JA, Tomaselli KJ, Litwack G and Alnemri ES (1996) The Cec-3/ interleukin 1 beta converting enzyme-like homolog Mch6 and the lamin-cleaving enzyme Mch2alpha are substrates for the apoptotic mediator CPP32. J. Biol. Chem. 271: 27099-27106
45. Stennicke HR, Deveraux QL, Humke EW, Reed JC, Dixit VM and Salvesen GS (1999) Caspase-9 can be activated without proteolytic processing. J. Biol. Chem. 274: 8359-8362
46. Zhou Q and Salvesen GS (1997) Activation of pro-caspase-7 by serine proteases includes a non-canonical specificity. Biochem. J. 324: 361-364
47. Muzio M, Stockwell BR, Stennicke HR, Salvesen GS and Dixit VM (1998) An induced proximity model for caspase-8 activation. J. Biol. Chem. 273: 2926-2930
48. Ware CF, Santee S and Glass A (1998) Tumor necrosis factor- related ligands and receptors. In: The Cytokine Handbook, 3rd edn, Academic Press Limited, San Deigo; 1998, pp. 549-592.
49. Martin DA, Siegel RM, Zheng L and Lenardo MJ (1998) Membrane oligomerization and cleavage activates the caspase-8 (FLICE/MACHalpha1) death signal. J. Biol. Chem. 273: 4345-4349
50. Yang X, Chang HY and Baltimore D (1998) Autoproteolytic activation of procaspase by oligomerization. Mol. Cell 1: 319-325
51. Zou H, Li Y, Liu X and Wang X (1999) An APAF-1. Cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9. J. Biol. Chem. 274: 11549-11556
52. Srinivasula SM, Ahmad M, Fernandes-Alnemri T and Alnemri ES (1998) Autoactivation of procaspase-9 by Apaf-1 -mediated oligomerization. Mol. Cell. 1: 949-957
53. Yang X, Chang HY and Baltimore D (1998) Essential role of CED-4 oligomerization in CED-3 activation and apoptosis. Science 281: 1355-1357
54. Chinnaiyan AM, Chaudhary D, O'Rourke K, Koonin EV and Dixit VM (1997) Role of CED-4 in the activation of CED-3. Nature 388: 728-729
55. Thornberry NA and Lazebnik Y (1998) Caspases: enemies within. Science 231: 1312-1316
56. Odake S, Kam CM, Narasimhan L, Poe M, Blake JT, Krahenbuhl O and Powers JC (1991) Human and murine cytotoxic T lymphocyte serine proteases: Subsite mapping with peptide thioester substrates and inhibition of enzyme activity and cytolysis by isocoumarins. Biochem. U.S.A. 30: 2217-2227
57. Chen JM, Rawlings ND, Stevens RA and Barrett AJ (1998) Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases. FEBS Lett. 441: 361-365
58. Tachias K and Madison EL (1996) Converting tissue-type plasmi nogen activator into a zymogen. J. Biol. Chem. 271: 28749-28752
59. Schechter I and Berger M (1967) On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27: 157-162
60. Gron H and Breddam K (1992) Interdependency of the binding subsites in subtilisin. Biochemistry 31: 8967-8971