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Information on EC 3.4.21.60 - Scutelarin
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3.4.21.60 ScutelarinSpecify your search results
Word Map
- 3.4.21.60
- clot
-
anticoagulant
- coagulation
- venom
- thromboplastin
- snake
-
chromogenic
- dabigatran
-
bleeding
- thrombocytopenia
-
procoagulant
- carinatus
-
heparin-induced
- meizothrombin
-
etexilate
- viper
- argatroban
- echis
-
r-hirudin
- lepirudin
- prothrombinase
- rivaroxaban
- textilis
- pseudonaja
- lonomia
-
anti-factor
-
anti-xa
-
doacs
- apixaban
-
idarucizumab
-
hemoclot
- bivalirudin
-
elapid
-
prothrombinase-induced
- obliqua
- prethrombin-2
-
tropidechis
- melagatran
- medicine
- edoxaban
-
saw-scaled
-
peg-hirudin
The enzyme appears in viruses and cellular organisms
Synonyms
ecarin, prothrombin activator, lopap, pseutarin c, cotiaractivase, cotiarinase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 3.4.99.28
-
-
formerly
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Proteinase, Oxyuranus scutellatus prothrombin-activating
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-
-
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prothrombin activator
Taipan activator
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
selective cleavage of Arg-/-Thr and Arg-/-Ile in prothrombin to form thrombin and two inactive fragments
From the venom of the Taipan snake (Oxyuranus scutellatus). Converts prothrombin to thrombin. Specificity is similar to that of Factor Xa (EC 3.4.21.6). However, unlike Factor Xa this enzyme can cleave its target in the absence of coagulation Factor Va. Activity is potentiated by phospholipid and Ca2+ which binds via gamma-carboxyglutamic acid residues. Similar enzymes are known from the venom of other Australian elapid snakes, including Pseudonaja textilis textilis, Oxyuranus microlepidotus and Demansia nuchalis affinis.
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
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CAS REGISTRY NUMBER
COMMENTARY
93389-45-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
benzoyl-Ile-Glu-Gly-Arg 4-nitroanilide + H2O
benzoyl-Ile-Glu-Gly-Arg + 4-nitroaniline
-
-
-
-
?
prothrombin + H2O
active thrombin + thrombin fragment 1 + prothrombin 1
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cotiarinase is a snake venom serine proteinase that generated thrombin upon incubation with prothrombin, limited proteolysis of this protein to release prothrombin 1, fragment 1 and thrombin
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-
?
prothrombin + H2O
alpha-thrombin + ?
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cleavage at positions Arg271-Thr272 and Arg320-Ile321
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-
?
prothrombin + H2O
thrombin + inactive prothrombin fragments
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-
-
?
prothrombin + H2O
?
ecarin converts prothrombin to thrombin also if the prothrombin is not gamma-carboxylated
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-
?
prothrombin + H2O
thrombin + ?
intermediate products are fragments similar to prethrombin-2 and fragment 1.2
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-
?
prothrombin + H2O
thrombin + meizothrombin
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conversion in absence of coagulation factor Va
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?
prothrombin + H2O
thrombin + meizothrombin
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cleavage of Arg274-Thr275 and Arg323-Ile324
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?
additional information
?
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the enzyme does not show fibrinogen-clotting, platelet-aggregating, fibrinogenolytic and factor X activating activities. Very low amidolytic activity as detected by the hydrolysis of the chromogenic substrates D-Phe-Pip-Arg-4-naphthyl amide and D-Val-Leu-Lys-4-naphthylamide
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-
?
additional information
?
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enzyme acts on cell survival, regulating the expression of molecules as NO and avoiding cell death. Enzyme triggers release of interleukin 8, inhibits platelet activation and chemotaxis and causes uncoagulable blood by fibrinogen depletion
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?
additional information
?
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no hydrolysis of: benzoyl-Phe-Arg 4-nitroanilide, D-Val-Leu-Lys 4-nitroanilide
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
prothrombin + H2O
active thrombin + thrombin fragment 1 + prothrombin 1
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cotiarinase is a snake venom serine proteinase that generated thrombin upon incubation with prothrombin, limited proteolysis of this protein to release prothrombin 1, fragment 1 and thrombin
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-
?
prothrombin + H2O
?
ecarin converts prothrombin to thrombin also if the prothrombin is not gamma-carboxylated
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-
?
additional information
?
-
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the enzyme does not show fibrinogen-clotting, platelet-aggregating, fibrinogenolytic and factor X activating activities. Very low amidolytic activity as detected by the hydrolysis of the chromogenic substrates D-Phe-Pip-Arg-4-naphthyl amide and D-Val-Leu-Lys-4-naphthylamide
-
-
?
additional information
?
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enzyme acts on cell survival, regulating the expression of molecules as NO and avoiding cell death. Enzyme triggers release of interleukin 8, inhibits platelet activation and chemotaxis and causes uncoagulable blood by fibrinogen depletion
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-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the enzyme from Bothrops cotiara venom activates prothrombin in the absence of the typical co-factors required for the specific cleavage of prothrombin
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
benzamidine
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inhibits hydrolysis of benzoyl-Ile-Glu-Gly-Arg 4-nitroanilide
Bovine pancreas trypsin inhibitor
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inhibits hydrolysis of benzoyl-Ile-Glu-Gly-Arg 4-nitroanilide
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Inhibitor present in the venom of Oxyuranus scutellatus
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inhibits hydrolysis of benzoyl-Ile-Glu-Gly-Arg 4-nitroanilide
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NaCl
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inhibits activation of prethrombin 2, no effect on reaction with meizothrombin
Nalpha-p-toluenesulfonyl-L-Arg methyl ester
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inhibits hydrolysis of benzoyl-Ile-Glu-Gly-Arg 4-nitroanilide
NaSCN
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bovine factor Va restores activity; reduces ability to activate prothrombin but has no effect on amidolytic activity
Soybean trypsin inhibitor
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inhibits hydrolysis of benzoyl-Ile-Glu-Gly-Arg 4-nitroanilide
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additional information
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hydrolysis of benzoyl-Ile-Glu-Gly-Arg 4nitroanilide is insensitive to: diisopropyl fluorophosphate, antithrombin III, chicken ovomucoid trypsin inhibitor, EDTA, 1,10-phenanthroline, activated protein C
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Phospholipid
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stimulates activation of both prothrombin and prethrombin 2, activation of prethrombin 1 is insensitive
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acute Kidney Injury
Fibrinogenolytic and procoagulant activities in the hemorrhagic syndrome caused by Lonomia obliqua caterpillars.
Antiphospholipid Syndrome
Management of lepirudin therapy for a patient with antiphospholipid antibody syndrome using the whole blood ecarin clot time and activated partial thromboplastin time.
Disseminated Intravascular Coagulation
Cloning of a prothrombin activator-like metalloproteinase from the West African saw-scaled viper, Echis ocellatus.
Disseminated Intravascular Coagulation
Disseminated intravascular coagulation following Echis carinatus venom in dogs: effects of a synthetic thrombin inhibitor.
Disseminated Intravascular Coagulation
Ecarin test in diagnosis of dicoumarol therapy, liver diseases and DIC.
Disseminated Intravascular Coagulation
Effects of lopap on human endothelial cells and platelets.
Disseminated Intravascular Coagulation
Fibrinogenolytic and procoagulant activities in the hemorrhagic syndrome caused by Lonomia obliqua caterpillars.
Disseminated Intravascular Coagulation
In vivo characterization of Lopap, a prothrombin activator serine protease from the Lonomia obliqua caterpillar venom.
Disseminated Intravascular Coagulation
The cardiovascular and haematological effects of purified prothrombin activator from the common brown snake (Pseudonaja textilis) and their antagonism with heparin.
Infections
Vibrio vulnificus secretes a broad-specificity metalloprotease capable of interfering with blood homeostasis through prothrombin activation and fibrinolysis.
Liver Diseases
Determination of plasma prothrombin levels by a novel Ca2+-dependent prothrombin activator (CA-1) in patients with chronic liver diseases.
Spinal Cord Injuries
Deficiency within the extrinsic prothrombin activator system in patients with acute spinal cord injury.
Thrombocytopenia
A quick assay for monitoring recombinant hirudin during cardiopulmonary bypass in patients with heparin-induced thrombocytopenia type II : adaptation of the ecarin clotting time to the act II device.
Thrombocytopenia
Hirudin monitoring using the TAS ecarin clotting time in patients with heparin-induced thrombocytopenia type II.
Thrombocytopenia
Successful use of recombinant hirudin and its monitoring by ecarin clotting time in patients with heparin-induced thrombocytopenia undergoing off-pump coronary artery revascularization.
Thrombocytopenia
The use of ecarin chromogenic assay and prothrombinase induced clotting time in the monitoring of lepirudin for the treatment of heparin-induced thrombocytopenia.
Thrombocytopenia
Use of ecarin clotting time (ECT) with lepirudin therapy in heparin-induced thrombocytopenia and cardiopulmonary bypass.
Thrombocytopenia
[Use of ecarin clotting time in whole blood for monitoring recombinant hirudine treatment during cardiopulmonary bypass in patients with heparin-induced thrombocytopenia]
Thrombosis
Comparative proteomic analysis of the venom of the taipan snake, Oxyuranus scutellatus, from Papua New Guinea and Australia: Role of neurotoxic and procoagulant effects in venom toxicity.
Thrombosis
Ecarin Clotting Time: a predictive coagulation assay for the antithrombotic activity of argatroban in the rat.
Thrombosis
In vivo characterization of Lopap, a prothrombin activator serine protease from the Lonomia obliqua caterpillar venom.
Thrombosis
Properties of biological and biochemical effects of the Iranian saw-scaled viper (Echis carinatus) venom.
Venous Thrombosis
Ecarin Clotting Time: a predictive coagulation assay for the antithrombotic activity of argatroban in the rat.
Venous Thrombosis
Inhibition of experimental arterial and venous thrombosis by ecarin, a defibrinating enzyme.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
additional information
similar enzymes from: Pseudonaja textilis textilis, Oxyuranus microlepidotus, Demansia nuchalis affinis
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-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
apart from the natural activation pathway, human prothrombin can also be activated by prothrombin activators in snake venoms. Ecarin is not dependent on any cofactors, but generates meizothrombin
physiological function
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thrombin is generated from prothrombin through cleavage at two sites by the prothrombinase complex. Prothrombinase is composed of a protease, factor Xa, and a cofactor, factor Va, which interact on negatively charged phospholipid surfaces and cleave prothrombin into thrombin 300000times faster than factor Xa alone The enzyme is responsible for the balance between bleeding and thrombosis
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
110000
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x * 110000 + x * 80000 + 2 disulfide-linked polypeptides of MW 30000 (one or both of these contain the active site), Oxyuranus scutellatus, SDS-PAGE after reduction with 2-mercaptoethanol
220000
80000
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x * 110000 + x * 80000 + 2 disulfide-linked polypeptides of MW 30000 (one or both of these contain the active site), Oxyuranus scutellatus, SDS-PAGE after reduction with 2-mercaptoethanol
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
-
x * 110000 + x * 80000 + 2 disulfide-linked polypeptides of MW 30000 (one or both of these contain the active site), Oxyuranus scutellatus, SDS-PAGE after reduction with 2-mercaptoethanol
additional information
catalytic subunit consists of a 22-residue signal peptide, 18-residue propetide, and a mature protein of 409 amino acids
additional information
-
catalytic subunit consists of a 22-residue signal peptide, 18-residue propetide, and a mature protein of 409 amino acids
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
Ser52 and Asn45 of the light and heavy chains are glycosylated in pseutarin catalytic subunit
proteolytic modification
sequence contains an 16-amino acid N-terminal signal peptide that is cleaved during secretion
additional information
additional information
gamma-carboxylation of glutamic acid residues of enzyme light chain
additional information
-
gamma-carboxylation of glutamic acid residues of enzyme light chain
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure homology modelling using the crystal structure of Pseutarin C, structure analysis
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from venom by gel filtration and cation exchange chromatography to homogeneity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
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the enzyme has potential therapeutic application in pathological conditions where the controlled activation of prothrombin is desirable
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Speijer, H.; Govers-Riemslag, J.W.P.; Zwaal, R.F.A.; Rosing, J.
Prothrombin activation by an activator from the venom of Oxyuranus scutellatus (Taipan snake)
J. Biol. Chem.
261
13258-13267
1986
More, Oxyuranus scutellatus
brenda
Walker, F.J.; Owen, W.G.; Esmon, C.T.
Characterization of the prothrombin activator from the venom of Oxyuranus scutellatus scutellatus (taipan venom)
Biochemistry
19
1020-1023
1980
Oxyuranus scutellatus
brenda
Monteiro, R.Q.; Zingali, R.B.
Inhibition of prothrombin activation by bothrojaracin, a C-type lectin from Bothrops jararaca venom
Arch. Biochem. Biophys.
382
123-128
2000
Oxyuranus scutellatus
brenda
Doorty, K.B.; Bevan, S.; Wadsworth, J.D.; Strong, P.N.
A novel small conductance Ca2+-activated K+ channel blocker from Oxyuranus scutellatus taipan venom. Re-evaluation of taicatoxin as a selective Ca2+ channel probe
J. Biol. Chem.
272
19925-19930
1997
Oxyuranus scutellatus
brenda
Chen, L.; Rezaie, A.R.
Proexosite-1-dependent recognition and activation of prothrombin by taipan venom
J. Biol. Chem.
279
17869-17874
2004
Oxyuranus scutellatus
brenda
Fritzen, M.; Flores, M.P.; Reis, C.V.; Chudzinski-Tavassi, A.M.
A prothrombin activator (Lopap) modulating inflammation, coagulation and cell survival mechanisms
Biochem. Biophys. Res. Commun.
333
517-523
2005
Lonomia obliqua
brenda
Reis, C.V.; Andrade, S.A.; Ramos, O.H.; Ramos, C.R.; Ho, P.L.; Batista, I.D.; Chudzinski-Tavassi, A.M.
Lopap, a prothrombin activator from Lonomia obliqua belonging to the lipocalin family: recombinant production, biochemical characterization and structure-function insights
Biochem. J.
398
295-302
2006
Lonomia obliqua (Q5ECE3), Lonomia obliqua
brenda
Senis, Y.A.; Kim, P.Y.; Fuller, G.L.; Garcia, A.; Prabhakar, S.; Wilkinson, M.C.; Brittan, H.; Zitzmann, N.; Wait, R.; Warrell, D.A.; Watson, S.P.; Kamiguti, A.S.; Theakston, R.D.; Nesheim, M.E.; Laing, G.D.
Isolation and characterization of cotiaractivase, a novel low molecular weight prothrombin activator from the venom of Bothrops cotiara
Biochim. Biophys. Acta
1764
863-871
2006
Bothrops cotiara
brenda
Filippovich, I.; Sorokina, N.; St Pierre, L.; Flight, S.; de Jersey, J.; Perry, N.; Masci, P.P.; Lavin, M.F.
Cloning and functional expression of venom prothrombin activator protease from Pseudonaja textilis with whole blood procoagulant activity
Br. J. Haematol.
131
237-246
2005
Pseudonaja textilis (Q56VR3), Pseudonaja textilis
brenda
Rao, V.S.; Swarup, S.; Manjunatha Kini, R.
The catalytic subunit of pseutarin C, a group C prothrombin activator from the venom of Pseudonaja textilis, is structurally similar to mammalian blood coagulation factor Xa
Thromb. Haemost.
92
509-521
2004
Pseudonaja textilis (Q56VR3), Pseudonaja textilis
brenda
Kitano, E.S.; Garcia, T.C.; Menezes, M.C.; Tashima, A.K.; Zelanis, A.; Serrano, S.M.
Cotiarinase is a novel prothrombin activator from the venom of Bothrops cotiara
Biochimie
95
1655-1659
2013
Bothrops cotiara
brenda
Loevgren, A.
Recombinant snake venom prothrombin activators
Bioengineered
4
153-157
2013
Echis carinatus (Q90495), Echis carinatus
brenda
Pomowski, A.; Ustok, F.I.; Huntington, J.A.
Homology model of human prothrombinase based on the crystal structure of Pseutarin C
Biol. Chem.
395
1233-1241
2014
Homo sapiens
brenda
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