EC Number   |
General Information |
Reference |
|---|
   3.4.21.95 | evolution |
the amino acid sequence of VLFVA shows significant homology with snake venom and mammalian serine proteinases. The other sequences (VLP2, VLP3 and VLP4) are homologous to VLFVA, but have two principal discrepancies in the translated protein sequence in comparison with snake venom serine protease structures: in the active site triad Ser195 is replaced by Asn195 and His57 by Arg57. Sequences of VLP3 and VLP4 represent combinations of VLFVA and VLP2 clones |
755604 |
| 3.4.21.95 | malfunction |
clopidogrel P2Y12 adenosine diphosphate (ADP) receptor inhibitor reduces markedly the aggregating effect induced by VLCII indicating the involvement of ADP signaling pathway |
754034 |
| 3.4.21.95 | metabolism |
proteases of venoms from subspecies of Macrovipera lebetina affecting blood coagulation cascade, overview |
755604 |
| 3.4.21.95 | physiological function |
binding kinetic study of RVV-V with two designed peptides corresponding to the regions from site I (Gln699-Asn713) and site II (1008Lys-Pro1022), respectively, of substrate blood coagulation factor V. Peptide II shows a lower binding affinity with KD of 2.775 mM while the Peptide I shows none. The peptide binding results in global conformational changes in the native fold of RVV-V, whereas the similar studies for thrombin fail to make major changes in the native fold |
755149 |
| 3.4.21.95 | physiological function |
in addition to its proteolytic activity, enzyme VLCII presents coagulant activity on human plasma. The isolated VLCII displays proaggregating effect on human platelets in a concentration-dependent manner with an absence of lag time. Purified VLCII is able to clot human plasma |
754034 |
| 3.4.21.95 | physiological function |
small peptides derived from factor V activator destabilize the beta-amyloid aggregate. Factor V activator-mediated proteolysis is not involved. Peptide CTNIF and a mixture of six peptides are most potent in converting the aggregates to the monomeric state and thus, preventing cytotoxicity in SH-SY5Y human neuroblastoma cells |
732117 |
| 3.4.21.95 | physiological function |
the enzyme VLFVA has the ability to activate factor V |
755604 |
