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3.4.24.58: russellysin

This is an abbreviated version!
For detailed information about russellysin, go to the full flat file.

Word Map on EC 3.4.24.58

Reaction

Specifically activates several components of the blood clotting system, including coagulation factor X, coagulation factor IX and protein C by cleavage of -Arg-/- bonds. Has no action on insulin B chain =

Synonyms

Blood-coagulation factor X activating enzyme, EC 3.4.21.23, Metalloproteinase RVV-x, Proteinase, Vipera russelli, Russell's viper blood coagulation factor X activator, Russell's Viper venom factor X activator, Russell's viper venom factor X activator, RVV-X, Russell`s viper venom coagulation factor X-activating enzyme, Russell’s viper venom factor X activator, RVV-X, snake venom protease

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.58 russellysin

Inhibitors

Inhibitors on EC 3.4.24.58 - russellysin

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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyroGlu-Arg-Trp
Q7LZ61; Q4PRD1; Q4PRD2
the synthetic tripeptide shows complete inhibition of the gelatinolytic activity of RVV-X at 5 mM
pyroGlu-Glu-Trp
Q7LZ61; Q4PRD1; Q4PRD2
the synthetic tripeptide shows complete inhibition of the gelatinolytic activity of RVV-X at 5 mM
pyroGlu-Lys-Trp
Q7LZ61; Q4PRD1; Q4PRD2
the synthetic tripeptide shows complete inhibition of the gelatinolytic activity of RVV-X at 5 mM
RNA132
-
an allosteric RNA aptamer, secondary structure folding, overview, causes 87% inhibition of the enzyme in the RVV-X-SPZXa assay, using a chromogenic substrate for the activated factor X, releasing the chromophore, 4-nitroanilide acetate, the snake venom protease competes with the human or murine vascular endothelial growth factor, VEGF165, for binding to RNA132 and reverses the inhibitory activity of RNA132 on RVV-X and restores its enzymatic activity, the VEGF165 of zebrafish functions partially, mapping of binding sites, overview
-
Snake venom factor IX/factor X-binding protein
-
with a C-type lectin structure, inhibits factor X activation
-