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- PA: Serine (S) Peptidases
- S1: Chymotrypsin
S1: Chymotrypsin C
Unless otherwise stated all data on this page refer to the human proteins. Gene information is provided for human (Hs), mouse (Mm) and rat (Rn).
Enzymes
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acrosin
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cathepsin G
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chymase 1
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chymotrypsin C
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chymotrypsin like
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chymotrypsin like elastase 1
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complement C1r
C
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complement C1s
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complement factor B
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coagulation factor II, thrombin
C
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coagulation factor VII
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coagulation factor IX
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coagulation factor X
C
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coagulation factor XI
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coagulation factor XII
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elastase, neutrophil expressed
C
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granzyme A
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granzyme B
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granzyme K
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kallikrein B1
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kallikrein 1
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kallikrein related peptidase 2
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kallikrein related peptidase 3
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kallikrein related peptidase 4
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kallikrein related peptidase 5
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kallikrein related peptidase 6
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kallikrein related peptidase 7
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kallikrein related peptidase 8
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kallikrein related peptidase 14
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plasminogen
C
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plasminogen activator, tissue type
C
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plasminogen activator, urokinase
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serine protease 1
C
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serine protease 2
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serine protease 3
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serine protease 8
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protein C, inactivator of coagulation factors Va and VIIIa
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proteinase 3
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suppression of tumorigenicity 14
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transmembrane serine protease 2
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transmembrane serine protease 6
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transmembrane serine protease 11D
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tryptase alpha/beta 1
C
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tryptase gamma 1
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References
1. AstraZeneca. AZ12971554. Accessed on 12/09/2014. Modified on 12/09/2014. astrazeneca.com, http://openinnovation.astrazeneca.com/what-we-offer/compound/az12971554/
2. Cheng L, Pettersen D, Ohlsson B, Schell P, Karle M, Evertsson E, Pahlen S, Jonforsen M, Plowright AT, Bostrom J et al.. (2014) Discovery of the Fibrinolysis Inhibitor AZD6564, Acting via Interference of a Protein-Protein Interaction. ACS Med Chem Lett, 5 (5): 538-543. [PMID:24900876]
3. Crocetti L, Giovannoni MP, Schepetkin IA, Quinn MT, Khlebnikov AI, Cilibrizzi A, Piaz VD, Graziano A, Vergelli C. (2011) Design, synthesis and evaluation of N-benzoylindazole derivatives and analogues as inhibitors of human neutrophil elastase. Bioorg. Med. Chem., 19 (15): 4460-72. [PMID:21741848]
4. Deinum J, Mattsson C, Inghardt T, Elg M. (2009) Biochemical and pharmacological effects of the direct thrombin inhibitor AR-H067637. Thromb. Haemost., 101 (6): 1051-9. [PMID:19492147]
5. Erba F, Fiorucci L, Pascarella S, Menegatti E, Ascenzi P, Ascoli F. (2001) Selective inhibition of human mast cell tryptase by gabexate mesylate, an antiproteinase drug. Biochem. Pharmacol., 61 (3): 271-6. [PMID:11172730]
6. Galemmo RA Jr., Fevig JM, Carini DJ, Cacciola J, Wells BL, Hillyer GL, Buriak J Jr., Rossi KA, Stouten PFW, Alexander RS et al.. (1996) (N-acyl-N-alkyl)glycyl borolysine analogs: A new class of potent thrombin inhibitors. Bioorganic & Medicinal Chemistry Letters, 6 (24): 2913–2918.
7. Gustafsson D, Antonsson T, Bylund R, Eriksson U, Gyzander E, Nilsson I, Elg M, Mattsson C, Deinum J, Pehrsson S et al.. (1998) Effects of melagatran, a new low-molecular-weight thrombin inhibitor, on thrombin and fibrinolytic enzymes. Thromb. Haemost., 79 (1): 110-8. [PMID:9459334]
8. Hauel NH, Nar H, Priepke H, Ries U, Stassen JM, Wienen W. (2002) Structure-based design of novel potent nonpeptide thrombin inhibitors. J. Med. Chem., 45 (9): 1757-66. [PMID:11960487]
9. Hays SJ, Caprathe BW, Gilmore JL, Amin N, Emmerling MR, Michael W, Nadimpalli R, Nath R, Raser KJ, Stafford D et al.. (1998) 2-amino-4H-3,1-benzoxazin-4-ones as inhibitors of C1r serine protease. J. Med. Chem., 41 (7): 1060-7. [PMID:9544206]
10. Imiya M, Matsuo T. (1997) Inhibition of collagen-induced platelet aggregation by argatroban in patients with acute cerebral infarction. Thromb. Res., 88 (2): 245-50. [PMID:9361377]
11. Johnson PH, Sze P, Winant RC, Hudson D, Underhill P, Lazar JB, Olsen C, Almquist R. (1991) Structure-function and refolding studies of the thrombin-specific inhibitor hirudin. Haemostasis, 21 Suppl 1: 41-8. [PMID:1894196]
12. Liverton NJ, Carroll SS, Dimuzio J, Fandozzi C, Graham DJ, Hazuda D, Holloway MK, Ludmerer SW, McCauley JA, McIntyre CJ et al.. (2010) MK-7009, a potent and selective inhibitor of hepatitis C virus NS3/4A protease. Antimicrob. Agents Chemother., 54 (1): 305-11. [PMID:19841155]
13. Mori S, Itoh Y, Shinohata R, Sendo T, Oishi R, Nishibori M. (2003) Nafamostat mesilate is an extremely potent inhibitor of human tryptase. J. Pharmacol. Sci., 92 (4): 420-3. [PMID:12939527]
14. Pakkala M, Hekim C, Soininen P, Leinonen J, Koistinen H, Weisell J, Stenman UH, Vepsäläinen J, Närvänen A. (2007) Activity and stability of human kallikrein-2-specific linear and cyclic peptide inhibitors. J. Pept. Sci., 13 (5): 348-53. [PMID:17436344]
15. Perzborn E, Roehrig S, Straub A, Kubitza D, Mueck W, Laux V. (2010) Rivaroxaban: a new oral factor Xa inhibitor. Arterioscler. Thromb. Vasc. Biol., 30 (3): 376-81. [PMID:20139357]
16. Pinto DJ, Smallheer JM, Cheney DL, Knabb RM, Wexler RR. (2010) Factor Xa inhibitors: next-generation antithrombotic agents. J. Med. Chem., 53 (17): 6243-74. [PMID:20503967]
17. Sperzel M, Huetter J. (2007) Evaluation of aprotinin and tranexamic acid in different in vitro and in vivo models of fibrinolysis, coagulation and thrombus formation. J. Thromb. Haemost., 5 (10): 2113-8. [PMID:17666018]
18. Stevens T, Ekholm K, Gränse M, Lindahl M, Kozma V, Jungar C, Ottosson T, Falk-Håkansson H, Churg A, Wright JL et al.. (2011) AZD9668: pharmacological characterization of a novel oral inhibitor of neutrophil elastase. J. Pharmacol. Exp. Ther., 339 (1): 313-20. [PMID:21791628]
19. Tan X, Soualmia F, Furio L, Renard JF, Kempen I, Qin L, Pagano M, Pirotte B, El Amri C, Hovnanian A et al.. (2015) Toward the first class of suicide inhibitors of kallikreins involved in skin diseases. J. Med. Chem., 58 (2): 598-612. [PMID:25489658]
20. Tully DC, Vidal A, Chatterjee AK, Williams JA, Roberts MJ, Petrassi HM, Spraggon G, Bursulaya B, Pacoma R, Shipway A et al.. (2008) Discovery of inhibitors of the channel-activating protease prostasin (CAP1/PRSS8) utilizing structure-based design. Bioorg. Med. Chem. Lett., 18 (22): 5895-9. [PMID:18752942]
21. Warkentin TE, Greinacher A, Craven S, Dewar L, Sheppard JA, Ofosu FA. (2005) Differences in the clinically effective molar concentrations of four direct thrombin inhibitors explain their variable prothrombin time prolongation. Thromb. Haemost., 94 (5): 958-64. [PMID:16363236]
22. Witting JI, Bourdon P, Brezniak DV, Maraganore JM, Fenton 2nd JW. (1992) Thrombin-specific inhibition by and slow cleavage of hirulog-1. Biochem. J., 283 ( Pt 3): 737-43. [PMID:1290488]
23. Wong PC, Crain EJ, Xin B, Wexler RR, Lam PY, Pinto DJ, Luettgen JM, Knabb RM. (2008) Apixaban, an oral, direct and highly selective factor Xa inhibitor: in vitro, antithrombotic and antihemostatic studies. J. Thromb. Haemost., 6 (5): 820-9. [PMID:18315548]
24. Young WB, Rai R, Shrader WD, Burgess-Henry J, Hu H, Elrod KC, Sprengeler PA, Katz BA, Sukbuntherng J, Mordenti J. (2006) Small molecule inhibitors of plasma kallikrein. Bioorg. Med. Chem. Lett., 16 (7): 2034-6. [PMID:16413183]
How to cite this family page
Database page citation:
S1: Chymotrypsin. Accessed on 17/07/2019. IUPHAR/BPS Guide to PHARMACOLOGY, http://www.guidetopharmacology.org/GRAC/FamilyDisplayForward?familyId=751.
Concise Guide to PHARMACOLOGY citation:
Alexander SPH, Fabbro D, Kelly E, Marrion NV, Peters JA, Faccenda E, Harding SD, Pawson AJ, Sharman JL, Southan C, Davies JA; CGTP Collaborators. (2017) The Concise Guide to PHARMACOLOGY 2017/18: Enzymes. Br J Pharmacol. 174 Suppl 1: S272-S359.
