Ser-Asn-Asn-Gly bond. Cattle, but not rabbit, factor V is cleaved, and no other proteins of the clotting system are attacked. Esterase activity is observed on Bz-Arg-OEt and Tos-Arg-OMe, and amidase activity on Phe-pipecolyl-Arg-NHPhNO2
Reaction: Fully activates human clotting factor V by a single cleavage at the Trp-Tyr-Leu-Arg1545Ser-Asn-Asn-Gly bond. Cattle, but not rabbit, factor V is cleaved, and no other proteins of the clotting system are attacked. Esterase activity is observed on Bz-Arg-OEt and Tos-Arg-OMe, and amidase activity on Phe-pipecolyl-Arg-NHPhNO2
Comment: Known from venom of Vipera russelli. Inhibited by di-isopropyl fluorophosphate, unlike the metallopeptidase russellysin (EC 3.4.24.58) that is specific for factor X [1]. In peptidase family S1 (trypsin family) [2]
Links to other databases: BRENDA, EXPASY, KEGG, MEROPS, Metacyc, PDB, CAS registry number: 471269-12-2, 123757-15-3, 123757-16-4, 123757-17-5 and 123757-18-6
References
1. Kisiel, W. and Canfield, W. M. Snake venom proteases that activate blood-coagulation factor V. Methods Enzymol. 80 (1981) 275-285. [PMID: 7043192]
2. Tokunaga, F., Nagasawa, K., Tamura, S., Miyata, T., Iwanaga, S. and Kisiel, W. The factor V-activating enzyme (RVV-V) from Russell's viper venom. Identification of isoproteins RVV-Vα, -Vβ and -Vγ and their complete amino acid sequences. J. Biol. Chem. 263 (1988) 17417-17481 [PMID: 3053712]