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Literature summary for 3.1.1.4 extracted from

  • Osipov, A.V.; Filkin, S.Y.; Makarova, Y.V.; Tsetlin, V.I.; Utkin, Y.N.
    A new type of thrombin inhibitor, noncytotoxic phospholipase A2, from the Naja haje cobra venom (2010), Toxicon, 55, 186-194.
    View publication on PubMed
Search for more literature for 3.1.1.4

Inhibitors

Inhibitors Comment Organism Structure
4-bromophenacyl bromide selectively and irreversibly modifies the His48 residue in the active site Naja kaouthia
additional information 4-bromophenacyl bromide does not modify the enzyme, no incorporation of the 4-bromophenacyl group into the enzyme Naja haje

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
14340
-
 mass spectrometry Naja haje
15840
-
 ethylpyridylation after total reduction of the enzyme, mass spectrometry Naja haje

Organism

Organism UniProt Comment Textmining
Naja haje
-
-
-
Naja kaouthia P00596
-
-

Purification (Commentary)

Purification (Comment) Organism
by gel filtration and ammonium acetate precipitation Naja haje

Source Tissue

Source Tissue Comment Organism Textmining
venom
-
 Naja haje
-
venom
-
 Naja kaouthia
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information does not hydrolyze either fibrinogen or thrombin Naja haje ?
-
 ?

Synonyms

Synonyms Comment Organism
Group IB phospholipase A2
-
 Naja haje
phospholipase A2
-
 Naja kaouthia
PLA2
-
 Naja haje
PLA2 CM2
-
 Naja kaouthia
thrombin inhibitor from Naja haje
-
 Naja haje
TI-Nh
-
 Naja haje

General Information

General Information Comment Organism
physiological function does not impair the adhesion of PC12 cells to plates. Is at least 2 orders of magnitude more cytotoxic than thrombin inhibitor from Naja haje Naja kaouthia
physiological function is a mixed-type inhibitor of thrombin and effectively inhibits thrombin-induced platelet aggregation. Does not require a plasma cofactor, the inhibition is direct. Strongly prolongs the thrombin clotting time (25fold at 0.0000475 mM) with whole human blood plasma. Possesses relatively weak enzymatic activity and is nontoxic to PC12 cells at concentrations up to 0.015 mM, but evokes neurite outgrowth in these cells at a concentration of approximately 0.001 mM, does not impair the adhesion of PC12 cells to plates. At concentrations up to approximately 0.00005 mM, at which the thrombin-clotting time is substantially prolonged, the enzyme exerts no detectable effects on both the intrinsic and extrinsic pathways of the coagulation cascade, thus is a selective thrombin inhibitor. Is at least 2 orders of magnitude less cytotoxic than PLA2 CM2 from Naja kaouthia Naja haje