| EC |
3.4.21.95 |
| Accepted name: |
snake venom factor V activator |
| Reaction: |
Fully activates human clotting factor V by a single cleavage at the Trp-Tyr-Leu-Arg1545┼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 |
| Comments: |
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, MetaCyc, MEROPS, PDB, CAS registry number: 471269-12-2, 123757-15-3, 123757-16-4, 123757-17-5, 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] |
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| [EC 3.4.21.95 created 1997] |
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