Information on EC 3.4.21.60 - Scutelarin

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.21.60
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RECOMMENDED NAME
GeneOntology No.
Scutelarin
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
selective cleavage of Arg-/-Thr and Arg-/-Ile in prothrombin to form thrombin and two inactive fragments
show the reaction diagram
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 hide
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY hide
93389-45-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
additional information
similar enzymes from: Pseudonaja textilis textilis, Oxyuranus microlepidotus, Demansia nuchalis affinis
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Benzoyl-Ile-Glu-Gly-Arg 4-nitroanilide + H2O
?
show the reaction diagram
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-
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Factor Xa-specific substrates + H2O
?
show the reaction diagram
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-
-
-
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Meizothrombin + H2O
?
show the reaction diagram
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des fragment 1
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Prethrombin 1 + H2O
?
show the reaction diagram
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-
-
-
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Prethrombin 2 + H2O
?
show the reaction diagram
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-
-
-
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prethrombin-1 + H2O
?
show the reaction diagram
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-
-
?
prothrombin + H2O
?
show the reaction diagram
prothrombin + H2O
active thrombin + thrombin fragment 1 + prothrombin 1
show the reaction diagram
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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 + ?
show the reaction diagram
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cleavage at positions Arg271-Thr272 and Arg320-Ile321
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-
?
prothrombin + H2O
thrombin + ?
show the reaction diagram
prothrombin + H2O
thrombin + inactive fragments
show the reaction diagram
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-
-
?
prothrombin + H2O
thrombin + meizothrombin
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
prothrombin + H2O
?
show the reaction diagram
prothrombin + H2O
active thrombin + thrombin fragment 1 + prothrombin 1
show the reaction diagram
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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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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
Zn-metalloprotease
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
benzamidine
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inhibits hydrolysis of benzoyl-Ile-Glu-Gly-Arg 4-nitroanilide
bothrojaracin
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inhibits prothrombin activation
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Bovine pancreas trypsin inhibitor
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inhibits hydrolysis of benzoyl-Ile-Glu-Gly-Arg 4-nitroanilide
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EDTA
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5 mM, complete inhibition
hirudin54-64(SO-3)-
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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
phenyl methyl sulfonylfluoride
complete inhibition
S2238
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noncompetitive
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Phospholipid
Prothrombin fragment 2
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stimulates activation of prethrombin 2
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0022
prethrombin-1
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pH 7.5
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0.0127 - 0.5
prothrombin
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00015 - 1200
prothrombin
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8
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hydrolysis of benzoyl-Ile-Glu-Gly-Arg 4-nitroanilide
8
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20800
x * 22500, proprotein, x * 20800, mature protein, calculated
22500
x * 22500, proprotein, x * 20800, mature protein, calculated
22931
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x * 22931, mass spectroscopy, x * 23000, SDS-PAGE
23000
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x * 22931, mass spectroscopy, x * 23000, SDS-PAGE
29000
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x * 29000, SDS-PAGE
32000
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x * 32000, heavy chain, SDS-PAGE
50000
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1 * 50000 + x * ?, catalytically active subunit, SDS-PAGE
69000
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x * 69000, SDS-PAGE
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
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
300000
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Oxyuranus scutellatus, nondenaturing PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oligomer
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1 * 50000 + x * ?, catalytically active subunit, SDS-PAGE
additional information
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catalytic subunit consists of a 22-residue signal peptide, 18-residue propetide, and a mature protein of 409 amino acids
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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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
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gamma-carboxylation of glutamic acid residues of enzyme light chain
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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the enzyme has potential therapeutic application in pathological conditions where the controlled activation of prothrombin is desirable