KEGG   ENZYME: 3.4.21.95Help
Entry
EC 3.4.21.95                Enzyme                                 

Name
snake venom factor V activator
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Serine endopeptidases
BRITE hierarchy
Reaction(IUBMB)
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
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].
History
EC 3.4.21.95 created 1997
Reference
1  [PMID:7043192]
  Authors
Kisiel W, Canfield WM.
  Title
Snake venom proteases that activate blood-coagulation factor V.
  Journal
Methods. Enzymol. 80 Pt C (1981) 275-85.
Reference
2  [PMID:3053712]
  Authors
Tokunaga F, Nagasawa K, Tamura S, Miyata T, Iwanaga S, Kisiel W.
  Title
The factor V-activating enzyme (RVV-V) from Russell's viper venom. Identification of isoproteins RVV-V alpha, -V beta, and -V gamma and their complete amino acid sequences.
  Journal
J. Biol. Chem. 263 (1988) 17471-81.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
471269-12-2 123757-15-3 123757-16-4 123757-17-5 123757-18-6

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