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Literature summary for 3.4.21.95 extracted from

  • Yadav, P.K.; Antonyraj, C.B.; Basheer Ahamed, S.I.; Srinivas, S.
    Understanding Russells viper venom factor V activators substrate specificity by surface plasmon resonance and in-silico studies (2017), PLoS ONE, 12, e0181216 .
    View publication on PubMedView publication on EuropePMC
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
factor V + H2O Daboia siamensis specifically cleaves the site III (Arg1545-Ser1546) of the factor V ?
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 ?

Organism

Organism UniProt Comment Textmining
Daboia siamensis P18964
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Daboia siamensis P18965 isoform Factor V activator RVV-V gamma
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
factor V + H2O specifically cleaves the site III (Arg1545-Ser1546) of the factor V Daboia siamensis ?
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 ?
factor V + H2O specifically cleaves the site III (Arg1545-Ser1546) of the factor V. Binding kinetic study of RVV-V with two designed peptides corresponding to the regions from site I (Gln699ÐAsn713) and site II (1008LysÐPro1022), respectively, that include 15 amino acids Daboia siamensis ?
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 ?

Synonyms

Synonyms Comment Organism
Russell's viper venom factor V activator
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 Daboia siamensis
RVV-V
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 Daboia siamensis

General Information

General Information Comment Organism
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 Daboia siamensis