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Information on EC 3.4.24.72 - fibrolase
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3.4.24.72 fibrolaseSpecify your search results
Word Map
- 3.4.24.72
- plasmin
-
thrombolytic
- copperhead
-
fibrinogenolytic
- medicine
- neuwiedi
- alteplase
-
nonhemorrhagic
- drug development
- pharmacology
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
3-203-fibrolase[3-serine], AfeE, Agkistrodon contortrix contortrix metalloproteinase, ALF, Alfimeprase, brevilysin L6, brevithrombolase, broad bean-fibrinolytic enzyme, CFR15-protease, fibrinolytic enzyme, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Agkistrodon contortrix contortrix metalloproteinase
-
-
-
-
Alfimeprase
brevithrombolase
broad bean-fibrinolytic enzyme
CFR15-protease
fibrinolytic enzyme
fibrinolytic protease
Fibrinolytic proteinase
-
-
-
-
Non-hemorrhagic fibrinolytic metalloproteinase
-
-
-
-
Proteinase, Agkistrodon contortrix contortrix venom metallo-
-
-
-
-
VlF
-
-
-
-
Alfimeprase
-
-
-
-
Alfimeprase
-
commercial preparation. Alfimeprase is identical to fibrolase except for a two amino acid truncation at the amino-terminus and the insertion of a new amino-terminal amino acid in the truncated protein, these changes lead to a more stable enzyme for prolonged storage
fibrinolytic protease
Mucor subtilissimus UCP 1262
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of -Ala14-/-Leu- in insulin B chain and -Lys413-/-Leu- in Aalpha-chain of fibrinogen
hydrolysis of Ala14-Leu15
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
116036-70-5
-
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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
4-amino-benzene-His-Thr-Glu-Lys-leu-Val-Thr-Ser-dinitrophenol + H2O
?
-
-
-
-
?
Abz-His-Thr-Glu-Lys-Leu-Val-Thr-Ser-2,4-dinitrophenyl + H2O
Abz-His-Thr-Glu-Lys + Leu-Val-Thr-Ser-2,4-dinitrophenyl
-
-
-
-
?
alpha2-macroglobulin + H2O
fragments of alpha2-macroglobulin
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-Phe-Ser-Pro + Phe-Arg
-
-
-
-
ir
bovine serum gamma-globulin + H2O
?
-
marginal hydrolytic activity
-
-
?
bradykinin + H2O
Arg-Pro-Pro-Gly-Phe-Ser-Pro + Phe-Arg
-
-
-
-
?
D-Ile-Pro-Arg-4-nitroanilide + H2O
D-Ile-Pro-Arg + 4-nitroaniline
-
-
-
?
D-Phe-Pip-Arg-4-nitroanilide + H2O
D-Phe-Pip-Arg + 4-nitroaniline
-
-
-
?
Fibrin Aalpha-chain + H2O
?
-
human, cleavage at Lys413-Lys414, the Bbeta-chain is cleaved more slowly and the gamma-chain is minimally affected
-
-
?
fibrin clot + H2O
?
-
the enzyme induces inhibition of fibrin clot formation in a concentration-dependent manner
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
second best substrate
-
-
?
Nalpha-benzoyl-DL-arginine-4-nitroanilide + H2O
Nalpha-benzoyl-DL-arginine + 4-nitroaniline
pyroGlu-Gly-Arg-4-nitroanilide + H2O
pyroGlu-Gly-Arg + 4-nitroaniline
-
-
-
-
?
S-2444 + H2O
pyroGlu-Gly-Arg + 4-nitroaniline
-
i.e. pyroGlu-Gly-Arg-4-nitroanilide
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide + H2O
succinyl-L-Ala-L-Ala-L-Pro-L-Phe + 4-nitroaniline
Mucor subtilissimus
-
-
-
-
?
bovine plasma fibrinogen + H2O
?
-
marginal hydrolytic activity
-
-
?
Bovine serum albumin + H2O
?
-
16.62% activity compared to human fibrin
-
-
?
Bovine serum albumin + H2O
?
Bacillus amyloliquefaciens MCC2606
-
16.62% activity compared to human fibrin
-
-
?
D-Val-Leu-Lys-4-nitroanilide + H2O
D-Val-Leu-Lys + 4-nitroaniline
-
highest activity
-
-
?
D-Val-Leu-Lys-4-nitroanilide + H2O
D-Val-Leu-Lys + 4-nitroaniline
-
-
-
?
Fibrin + H2O
?
-
fibrinolytic activity cleaving the Lys413-Leu414 bond
-
-
?
Fibrin + H2O
?
-
human substrate, fibrinolytic activity cleaving the Lys413-Leu414 bond
-
-
?
Fibrin + H2O
?
-
fibrinolase cleaves the alpha-chain more rapidly than the beta-chain of fibrin
-
-
?
Fibrin + H2O
?
-
the enzyme can catalyze fibrin clot lysis effectively
-
-
?
Fibrin + H2O
?
Bacillus amyloliquefaciens CGMCC 7380
-
the enzyme can catalyze fibrin clot lysis effectively
-
-
?
Fibrin + H2O
?
-
the enzyme degrades all the four peptide chains of fibrin rapidly
-
-
?
Fibrin + H2O
?
Bacillus subtilis BR21
-
the enzyme degrades all the four peptide chains of fibrin rapidly
-
-
?
Fibrin + H2O
?
-
the enzyme has the ability to directly degrade fibrin in vitro and effectively dissolve thrombi in vivo without activating plasminogen or influencing the activities of tissue plasminogen activator and plasminogen activator inhibitor-1
-
-
?
Fibrin + H2O
?
best substrate. The enzyme exhibits about 2fold higher activity for fibrin than fibrinogen. Fibrin can be hydrolyzed completely in about 30 min
-
-
?
Fibrinogen + H2O
?
-
fibrolase rapidly cleaves the A(alpha)-chain of fibrinogen and the B(beta)-chain at a slower rate, while it has no activity on the gamma-chain. The primary cleavage site at the alpha-chain ist he Lys-Leu bond at residues 413-414
-
-
?
Fibrinogen + H2O
?
the enzyme has a direct proteolytic activity against the A alpha-chain of fibrinogen at positions Lys413 and Leu414
-
-
?
fibrinogen + H2O
fibrin + ?
-
55.21% activity compared to human fibrin. Among the three chains of fibrinogen, Aalpha and Bbeta chains are degraded rapidly, whereas gamma-chain of fibrinogen shows significant resistance to degradation by the enzyme
-
-
?
fibrinogen + H2O
fibrin + ?
-
the highest fibrinolytic activity and a degradation of blood clot in vitro of 62% are obtained in a medium with 2% (w/v) soybean flour and 1% (w/v) D-glucose at 200 rpm after 48 h of cultivation, at pH 7.2 and 37°C
-
-
?
fibrinogen + H2O
fibrin + ?
Bacillus amyloliquefaciens MCC2606
-
55.21% activity compared to human fibrin. Among the three chains of fibrinogen, Aalpha and Bbeta chains are degraded rapidly, whereas gamma-chain of fibrinogen shows significant resistance to degradation by the enzyme
-
-
?
fibrinogen + H2O
fibrin + ?
Bacillus amyloliquefaciens UFPEDA 485
-
the highest fibrinolytic activity and a degradation of blood clot in vitro of 62% are obtained in a medium with 2% (w/v) soybean flour and 1% (w/v) D-glucose at 200 rpm after 48 h of cultivation, at pH 7.2 and 37°C
-
-
?
fibrinogen + H2O
fibrin + ?
-
the enzyme degrades only Aalpha and Bbeta chains of fibrinogen
-
-
?
fibrinogen + H2O
fibrin + ?
Bacillus subtilis BR21
-
the enzyme degrades only Aalpha and Bbeta chains of fibrinogen
-
-
?
fibrinogen + H2O
fibrin + ?
-
the alpha-chain of fibrinogen is degraded very quickly within 5 min, followed by beta-chain in 1 h whereas the gamma-chain is degraded in 2 h
-
-
?
fibrinogen + H2O
fibrin + ?
-
the alpha-chain is rapidly hydrolyzed and the beta-chain is partially digested by 10 ng of starase. With an increase in starase concentration to 120 ng, the gamma-chain is partially degraded, but all the alpha-, beta- and gamma-chains of fibrinogen are completely cleaved by 250 ng and higher concentration of starase
-
-
?
fibrinogen + H2O
fibrin + ?
fibrinogen can be hydrolyzed completely in 4-6 h
-
-
?
fibrinogen + H2O
fibrin + ?
-
the enzyme exhibits cleavage of Aalphaand Bbeta chains of fibrin(ogen) and has no effect on gamma chain
-
-
?
fibrinogen + H2O
fibrin + propeptide
bovine substrate
-
-
?
fibrinogen + H2O
fibrin + propeptide
-
fibrinogenolytic activity
-
-
?
fibrinogen + H2O
fibrin + propeptide
bovine substrate, fibrinogenolytic activity
-
-
?
fibrinogen + H2O
fibrin + propeptide
-
human substrate, fibrinogenolytic activity
-
-
?
Fibrinogen Aalpha-chain + H2O
?
-
cleavage at Lys413-Leu414 (initial cleavage)
-
-
?
Fibrinogen Aalpha-chain + H2O
?
-
cleavage specificity is not dictated by the Lys-Leu bond per se, but by the surrounding sequence
-
-
?
Fibrinogen Aalpha-chain + H2O
?
-
the Bbeta-chain is cleaved more slowly and the gamma-chain is minimally affected
-
-
?
Hemoglobin + H2O
?
-
25.09% activity compared to human fibrin
-
-
?
Hemoglobin + H2O
?
Bacillus amyloliquefaciens MCC2606
-
25.09% activity compared to human fibrin
-
-
?
His-Thr-Glu-Lys-Leu-Val-Thr-Ser + H2O
?
-
cleaving sequence residues 410-417 from fibrinogen Aalpha-chain
-
-
?
human fibrin + H2O
?
-
fibrin is the most preferred substrate (100% activity). The beta-chain of fibrin is the primary component and site susceptible for the enzyme in early action. The enzyme can completely degrade all the four chains of fibrin
-
-
?
human fibrin + H2O
?
Bacillus amyloliquefaciens MCC2606
-
fibrin is the most preferred substrate (100% activity). The beta-chain of fibrin is the primary component and site susceptible for the enzyme in early action. The enzyme can completely degrade all the four chains of fibrin
-
-
?
Insulin B-chain + H2O
?
-
cleavage between Ala14 and Leu15
-
-
?
Insulin B-chain + H2O
?
-
fibrinogenolytic activity cleaving the Leu11-Val-Glu-Ala-Leu-Tyr-Leu-Val18 peptide
-
-
?
Leu-Val-Glu-Ala-Leu-Tyr-Leu-Val + H2O
?
-
cleaving sequence residues 11-18 from insulin B-chain
-
-
?
low molecular weight kininogen + H2O
kallidin + ?
-
-
i.e. Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
?
low-molecular weight kininogen + H2O
kallidin + ?
-
-
-
-
?
low-molecular weight kininogen + H2O
kallidin + ?
-
initiates generation of bradykinin
-
-
?
Nalpha-benzoyl-DL-arginine-4-nitroanilide + H2O
Nalpha-benzoyl-DL-arginine + 4-nitroaniline
-
marginal hydrolytic activity
-
-
?
Nalpha-benzoyl-DL-arginine-4-nitroanilide + H2O
Nalpha-benzoyl-DL-arginine + 4-nitroaniline
-
marginal hydrolytic activity
-
-
?
additional information
?
-
-
no activity against a series of chromogenic 4-nitroanilide substrates
-
-
?
additional information
?
-
-
exhibits little if any hemorrhagic activity
-
-
?
additional information
?
-
-
does not activate protein C
-
-
?
additional information
?
-
-
does not activate plasminogen
-
-
?
additional information
?
-
-
does not activate plasminogen
-
-
?
additional information
?
-
-
direct fibrinolytic activity
-
-
?
additional information
?
-
fibrolase identified in multiple isoforms
-
?
additional information
?
-
-
fibrolase identified in multiple isoforms
-
?
additional information
?
-
-
thrombolysis in animals by snake venom alfimeprase, overview
-
-
?
additional information
?
-
-
alfimeprase is the recombinant truncated form of fibrolase from snake venom lacking the two N-terminal amino acids Glu and Gln
-
-
?
additional information
?
-
the enzyme is a nonhemorrhagic zinc metalloprotease
-
-
?
additional information
?
-
the enzyme is a nonhemorrhagic zinc metalloprotease
-
-
?
additional information
?
-
-
the enzyme is a nonhemorrhagic zinc metalloprotease
-
-
?
additional information
?
-
-
the enzyme is a nonhemorrhagic zinc metalloprotease, peptide substrate specificity, preference for Xaa-Leu and Xaa-Phe overview
-
-
?
additional information
?
-
chimeric Arg-Gly-Asp-fibrolase efficiently inhibits platelet aggregation in a dose-dependent manner and a prolonged incubation time obviously increased the inhibitory effect, in contrast to fibrolase
-
-
?
additional information
?
-
-
chimeric Arg-Gly-Asp-fibrolase efficiently inhibits platelet aggregation in a dose-dependent manner and a prolonged incubation time obviously increased the inhibitory effect, in contrast to fibrolase
-
-
?
additional information
?
-
-
fibrolase neither activates nor degrades plasminogen
-
-
?
additional information
?
-
-
no activity with plasminogen, N-benzoyl-Pro-Phe-Arg-4-nitroanilide, N-benzoyl-Ile-Glu-Gly-Arg-4-nitroanilide, N-(4-tosyl)-Gly-Pro-Arg-4-nitroanilide, and bovine serum albumin
-
-
?
additional information
?
-
-
no activity with plasminogen, N-benzoyl-Pro-Phe-Arg-4-nitroanilide, N-benzoyl-Ile-Glu-Gly-Arg-4-nitroanilide, N-(4-tosyl)-Gly-Pro-Arg-4-nitroanilide, and bovine serum albumin
-
-
?
additional information
?
-
Mucor subtilissimus
-
no activity with Gly-Arg-4-nitroanilide and Nalpha-benzoyl-DL-Arg-4-nitroanilide
-
-
?
additional information
?
-
Mucor subtilissimus UCP 1262
-
no activity with Gly-Arg-4-nitroanilide and Nalpha-benzoyl-DL-Arg-4-nitroanilide
-
-
?
additional information
?
-
-
the enzyme shows weak amidolytic activity for the substrates Z-D-Arg-Gly-Arg-4-nitroanilide and D-Phe-Pip-Arg-4-nitroanilide
-
-
?
additional information
?
-
-
the enzyme was devoid of hemorrhagic effect
-
-
?
additional information
?
-
-
the enzyme does not display any detectable hydrolysis of gamma chain of fibrin over a period of 180 min
-
-
?
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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
bradykinin + H2O
Arg-Pro-Pro-Gly-Phe-Ser-Pro + Phe-Arg
-
-
-
-
?
low-molecular weight kininogen + H2O
kallidin + ?
-
initiates generation of bradykinin
-
-
?
Fibrin + H2O
?
-
fibrinolase cleaves the alpha-chain more rapidly than the beta-chain of fibrin
-
-
?
Fibrin + H2O
?
-
the enzyme has the ability to directly degrade fibrin in vitro and effectively dissolve thrombi in vivo without activating plasminogen or influencing the activities of tissue plasminogen activator and plasminogen activator inhibitor-1
-
-
?
Fibrinogen + H2O
?
-
fibrolase rapidly cleaves the A(alpha)-chain of fibrinogen and the B(beta)-chain at a slower rate, while it has no activity on the gamma-chain. The primary cleavage site at the alpha-chain ist he Lys-Leu bond at residues 413-414
-
-
?
Fibrinogen + H2O
?
the enzyme has a direct proteolytic activity against the A alpha-chain of fibrinogen at positions Lys413 and Leu414
-
-
?
fibrinogen + H2O
fibrin + ?
-
the alpha-chain of fibrinogen is degraded very quickly within 5 min, followed by beta-chain in 1 h whereas the gamma-chain is degraded in 2 h
-
-
?
fibrinogen + H2O
fibrin + ?
-
the alpha-chain is rapidly hydrolyzed and the beta-chain is partially digested by 10 ng of starase. With an increase in starase concentration to 120 ng, the gamma-chain is partially degraded, but all the alpha-, beta- and gamma-chains of fibrinogen are completely cleaved by 250 ng and higher concentration of starase
-
-
?
fibrinogen + H2O
fibrin + ?
-
the enzyme exhibits cleavage of Aalphaand Bbeta chains of fibrin(ogen) and has no effect on gamma chain
-
-
?
fibrinogen + H2O
fibrin + propeptide
bovine substrate
-
-
?
fibrinogen + H2O
fibrin + propeptide
-
fibrinogenolytic activity
-
-
?
low molecular weight kininogen + H2O
kallidin + ?
-
-
i.e. Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
?
additional information
?
-
-
thrombolysis in animals by snake venom alfimeprase, overview
-
-
?
additional information
?
-
chimeric Arg-Gly-Asp-fibrolase efficiently inhibits platelet aggregation in a dose-dependent manner and a prolonged incubation time obviously increased the inhibitory effect, in contrast to fibrolase
-
-
?
additional information
?
-
-
chimeric Arg-Gly-Asp-fibrolase efficiently inhibits platelet aggregation in a dose-dependent manner and a prolonged incubation time obviously increased the inhibitory effect, in contrast to fibrolase
-
-
?
additional information
?
-
-
fibrolase neither activates nor degrades plasminogen
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Cu2+
Fe2+
K+
Mg2+
Mn2+
Na+
Zinc
Zn2+
additional information
Mn2+
-
the activity of the enzyme is enhanced to 111.21% in the presence of 10 mM Mn2+
Na+
Streptomyces sp. DPUA1576
-
the activity of protease is slightly enhanced (to 106%) by the presence of Na+ ions
Zinc
-
effect of zinc binding on the structure and stability of fibrolase
Zn2+
-
1 mol per mol of enzyme, fibrolase is a zinc metalloprotease with the zinc binding motif HEXXHXXGXXH
Zn2+
-
a zinc metalloproteinase containing one mole of zinc
additional information
-
the enzyme activity is not influenced by Mn2+, Cu2+, Ca2+, Mg2+, Co2+, Zn2+, and Fe2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N-4-tosyl-phenylalanyl chloromethyl ketone
-
16.5% residual activity at 0.1 mM
Nalpha-tosyl-L-lysine chloromethylketone
-
51.5% residual activity at 0.1 mM
tosyl-L-lysine chloromethyl ketone
21.3% residual activity at 0.1 mM
tosyl-L-phenylalanine chloromethyl ketone
37.2% residual activity at 0.1 mM
alpha2-Macroglobulin
-
the 720 kDa tetrameric inhibitor causes rapid and irreversible inhibition by sterical hindrance, the PEG-bound enzyme is less sensitive
-
alpha2-Macroglobulin
-
rapid, irreversible inhibition by physical entrapment
-
EDTA
-
EDTA sensitivity of the isoforms of the natural and of the recombinant enzyme
phenylmethylsulfonyl fluoride
18.5% residual activity at 1 mM
Tetraethylenepentamine
-
complete and rapid inhibition
tosyl-phenylalanine chloromethyl ketone
-
76.2% residual activity at 5 mM
additional information
-
not inhibited by any serine protease inhibitor
-
additional information
-
not: DFP, soybean trypsin inhibitor, trasylol, PCMB
-
additional information
-
polyethylene glycol addition to the enzyme modifies the enzyme size and reduces its activity
-
additional information
Mucor subtilissimus
-
not inhibited by EDTA, iodoacetic acid, and 2-mercaptoethanol
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
the enzyme does not require plasminogen or any other bloodborne intermediate for activity
-
additional information
-
the enzyme does not require plasminogen or any other bloodborne intermediate for activity
-
additional information
-
the enzyme is a direct-acting thrombolytic agent and does not rely on plasminogen for clot dissolution
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Arthritis
Plasminogen is a joint-specific positive- or negative-determinant of arthritis pathogenesis.
Carotid Artery Thrombosis
Thrombolytic effects of recombinant fibrolase or APSAC in a canine model of carotid artery thrombosis.
Cockayne Syndrome
Involvement of antipain-sensitive protease activity in the interferon-beta-induced UV-refractoriness of Cockayne syndrome fibroblasts.
Infections
Toxoplasma gondii: effects of neuwiedase, a metalloproteinase from Bothrops neuwiedi snake venom, on the invasion and replication of human fibroblasts in vitro.
Lung Injury
Adenovirally mediated gene transfer of functional human tissue-type plasminogen activator to murine lungs.
Myocardial Infarction
Defibrase, a purified fibrinolytic protease from snake venom in acute myocardial infarction.
Myocardial Infarction
Effect of thrombolysis on myocardial injury: recombinant tissue plasminogen activator vs. alfimeprase.
Myocardial Infarction
[Alterations of peripheral blood endothelial progenitor cells from patients with ST elevation myocardial infarction after snake venom fibrinolytic enzyme therapy.]
Myotoxicity
Pathological alterations induced by neuwiedase, a metalloproteinase isolated from Bothrops neuwiedi snake venom.
Neoplasms
The fibrinolysis inhibitor ?2-antiplasmin restricts lymphatic remodelling and metastasis in a mouse model of cancer.
Osteoporosis
Fibrin accumulation secondary to loss of plasmin-mediated fibrinolysis drives inflammatory osteoporosis.
Pulmonary Embolism
Starase: A bi-functional fibrinolytic protease from hepatic caeca of Asterina pectinifera displays antithrombotic potential.
Reperfusion Injury
Effect of thrombolysis on myocardial injury: recombinant tissue plasminogen activator vs. alfimeprase.
ST Elevation Myocardial Infarction
[Alterations of peripheral blood endothelial progenitor cells from patients with ST elevation myocardial infarction after snake venom fibrinolytic enzyme therapy.]
Thrombosis
Biological and thrombolytic properties of fibrolase--a new fibrinolytic protease from snake venom.
Thrombosis
Chimeric derivative of fibrolase, a fibrinolytic enzyme from southern copperhead venom, possesses inhibitory activity on platelet aggregation.
Thrombosis
Clinical utility of novel agents in the treatment of central venous catheter occlusion.
Thrombosis
Effect of thrombolysis on myocardial injury: recombinant tissue plasminogen activator vs. alfimeprase.
Thrombosis
Extracellular Production of a Potent and Chemically Resistant Nattokinase in Immobilized Escherichia coli Using Response Surface Methodology.
Thrombosis
Feedback regulation of endothelial cell surface plasmin generation by PKC dependent phosphorylation of annexin A2.
Thrombosis
In Vivo Anticoagulant and Thrombolytic Activities of a Fibrinolytic Serine Protease (Brevithrombolase) With the k-Carrageenan-Induced Rat Tail Thrombosis Model.
Thrombosis
Preparation and toxicity evaluation of a novel nattokinase-tauroursodeoxycholate complex.
Thrombosis
Starase: A bi-functional fibrinolytic protease from hepatic caeca of Asterina pectinifera displays antithrombotic potential.
Thrombosis
Thrombolytic effects of recombinant fibrolase or APSAC in a canine model of carotid artery thrombosis.
Thrombosis
Thrombolytic Potential of Novel Thiol-Dependent Fibrinolytic Protease from Bacillus cereus RSA1.
Venous Thrombosis
Fibrolase, an active thrombolytic enzyme in arterial and venous thrombosis model systems.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
analysis of kinetic and equilibrium binding parameters of streptokinase-plasmin catalytic complex formation and its regulation by effectors 6-AHA and benzamidine
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
native and PEG-bound enzyme, rapid interaction kinetics with inhibitor alpha2-macroglobulin
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
blood clot lysis in vitro model, overview
additional information
-
the enzyme shows specific activity of 5.2 units/mg (cell free crude extract) and 64.9 units/mg (after 12.4 fold purification). One unit is defined as microgram of L-tyrosine equivalent liberated per ml per min after 30 min incubation at 37°C
additional information
-
specific activity of 9.22 units/mg after 8.37fold purification. One unit is defined as the amount of the enzyme producing acid-soluble material from azocasein to cause an increase in absorbance of 0.001 at 660 nm per min
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
-
considerable activity is observed at pH 10.0 (84.4%). The enzyme exhibits poorer activity in the acidic pH 5.0-6.0 (53-64%)
5 - 9
-
more than 60% activity between pH 5.0 and 9.0, about 40% activity at pH 10.0, no activity at pH 4.0
6 - 12
the enzyme shows more than 60% activity at pH values ranging from 6.0 to 12.0
7 - 8
Streptomyces sp. DPUA1576
-
the enzyme activity decreases rapidly at levels below pH 7.0 and above pH 8.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
40
45
50
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 60
Mucor subtilissimus
-
the enzyme shows more than 80% activity between 10 and 60°C. The enzyme is completely denatured at temperatures above 80°C
25 - 55
-
about 75% activity 25°C, about 80% activity 30°C, 100% activity at 35°C, about 80% activity 40°C, about 60% activity 45°C, about 50% activity 50°C, about 45% activity 55°C. At 60°C, the activity of the enzyme is completely lost
25 - 75
Streptomyces sp. DPUA1576
-
highest protease activity between 35 and 55°C. The relative activities at 25°C and 75°C are 59% and 49%, respectively
37 - 60
the enzyme maintains up to 80% of its maximum activity at a temperature range of 37-60°C
40 - 60
-
considerable activity is observed at 60°C (88.6%) and at 40°C (68.6%)
50 - 60
Serratia sp. KG-2-1
-
maximum enzyme activity at 40°C (100%) then decreases gradually with relative activity of 69.28 and 67.75% at 50 and 60°C, respectively
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subspecies Agkistrodon contortrix contortrix, southern copperhead snake
-
-
brenda
-
-
-
brenda
southern copperhead, isoforms of natural and recombinant enzyme
-
-
brenda
southern copperhead, isoforms of natural and recombinant enzyme (resolution by high performance capillary electrophoresis)
-
-
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
-
the enzyme inhibits fibrin polymer formation (anticoagulant effect)
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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). VM1F_AGKCO
203
0
22908
Swiss-Prot
Mitochondrion (Reliability: 5)
VM1F_MACLB
202
0
22851
Swiss-Prot
other Location (Reliability: 3)
B7Q4I3_IXOSC
395
0
44715
TrEMBL
other Location (Reliability: 1)
B7QM90_IXOSC
437
0
50200
TrEMBL
Secretory Pathway (Reliability: 1)
B7PTJ6_IXOSC
225
0
25108
TrEMBL
other Location (Reliability: 4)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22540
-
Agkistrodon contortrix, calculation from amino acid sequence
22710
22750
-
Agkistrodon contortrix, isoform fib2, calculation from amino acid sequence
22880
-
Agkistrodon contortrix, isoform fib1, calculation from amino acid sequence
23000
23800
x * 23800, recombinant His-tagged alfimeprase, SDS-PAGE
42000
-
x * 42000, the enzyme exists in three isoforms of 42000, 48000 and 60000 Da, SDS-PAGE
48000
60000
23000
-
x * 23000, native enzyme, x * 60000, PEG-bound enzyme
48000
-
x * 48000, the enzyme exists in three isoforms of 42000, 48000 and 60000 Da, SDS-PAGE
60000
-
x * 23000, native enzyme, x * 60000, PEG-bound enzyme
60000
-
x * 60000, the enzyme exists in three isoforms of 42000, 48000 and 60000 Da, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
-
x * 23000-24000, Agkistrodon contortrix, SDS-PAGE under reducing and nonreducing condition
?
x * 23800, recombinant His-tagged alfimeprase, SDS-PAGE
?
-
x * 42000, the enzyme exists in three isoforms of 42000, 48000 and 60000 Da, SDS-PAGE
?
-
x * 48000, the enzyme exists in three isoforms of 42000, 48000 and 60000 Da, SDS-PAGE
?
-
x * 60000, the enzyme exists in three isoforms of 42000, 48000 and 60000 Da, SDS-PAGE
?
-
x * 42000, the enzyme exists in three isoforms of 42000, 48000 and 60000 Da, SDS-PAGE
-
?
-
x * 48000, the enzyme exists in three isoforms of 42000, 48000 and 60000 Da, SDS-PAGE
-
?
-
x * 60000, the enzyme exists in three isoforms of 42000, 48000 and 60000 Da, SDS-PAGE
-
?
Mucor subtilissimus UCP 1262
-
x * 97000, SDS-PAGE
-
additional information
-
alfimeprase is the recombinant truncated form of fibrolase from snake venom lacking the two N-terminal amino acids Glu and Gln, fibrolase N-terminus: SFPQR, alfimeprase N-terminus: EQRFPQR
additional information
-
the protein is composed of 5 alpha-helical regions, 4 parallel and 1 antiparallel beta-sheet, stablized by 3 disulfide bonds
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
-
adduction of polyethylene glycol to reduce the rate of clearance from the circulation, and coupling to an Arg-Gly-Asp (RGD) like peptide imparting inhibitory activity on platelet aggregation and thrombus formation while maintaining full fibrinolytic activity
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
construction of a heterobifunctional chimeric derivative of fibrolase through linking covalently with a RGD-like peptide via a surface residue distant from the active site, structure, overview, the chimera shows fibrolase and platelet-binding ability, the chimeric enzyme exhibits an IC50 of 105 nM in inhibition of platelet aggregation, overview
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 12
-
pre-incubation of fibrinolytic protease for 1 h at pH 4.0-12.0 causes substantial activity loss
733238
5 - 11
-
the enzyme remains stable for 2 h at pH 5.0-11.0, retaining more than 80% activity
754441
5.8 - 9.2
Streptomyces sp. DPUA1576
-
protease and fibrinolytic activities are stable during 6 h, at a pH ranging from 6.8 to 8.4 and 5.8 to 9.2, respectively
752378
6 - 12
7
-
after incubation for 12 h, the enzyme retains 82.89% of its activity at pH 7.0, 66.03% at pH 8.0, and 50% at pH 6.0 and 9.0 after 8 h of incubation, respectively
754580
7 - 10
-
after 60 min incubation the enzyme possesses remarkable stability at pH 7.0-10.0 (98.5-100%). In the acidic pH (5.0-6.0), the enzyme retains 77 and 85% activity, respectively
733596
6 - 12
Serratia sp. KG-2-1
-
the purified enzyme shows higher stability between pH 6.0-8.0 retaining more than 90% of its activity while it retains 87.22 and 74.23% of its activity at pH 5.0 and 9.0, respectively. With further increase in pH 18% residual activity is observed at pH 12.0
752343
6 - 12
the enzyme activity remains stable after 60 min at pH 6.0-12.0
753870
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 30
Serratia sp. KG-2-1
-
the enzyme shows relatively high stability between 10-30°C retaining 94.87, 94.83 and 99.79% of activity at respective temperatures while at higher temperature activity decreases
20 - 70
the enzyme activity remains stable for 60 min at 20-30°C and loses about 50% activity after 60 min at 50°C. After 60 min at 60°C, the enzyme completely loses its activity
20 - 80
-
fibrinolytic protease loses about 40-60% of its activity after 1 h incubation at 20-80°C
23 - 60
-
the enzyme is highly thermostable up to 52°C retaining more than 40% of its initial activity when incubated at 23-60°C for 1 h and 2 h
25 - 75
Streptomyces sp. DPUA1576
-
the enzyme is stable during 120 min at 25 and 35°C and shows 98, 100, and 59% residual activity at 25, 35 and 45°C, respectively. The enzyme in the crude extract loses its activity after 60 min between 55 and 75°C
30 - 50
-
the enzyme is quite stable at 30-50°C for 60 min, but at 60°C and above activity decreases drastically
30 - 60
-
the enzyme remains stable between 30 and 60°C when incubated for 40 min
37
additional information
-
effect of temperature on conformation
37
-
about 50% loss of activity after 2 days, complete loss of activity after 10 days
37
-
after 12 h of incubation, the enzyme remains stable at 4, 25 and 37°C, maintaining activities of 96.04, 95.88, and 98.26%, respectively, and maintains 58.84% of its activity at 40°C
37
Mucor subtilissimus
-
at 37°C, the enzyme residual activity is 94 and 68% of the initial one after 120 and 150 min of incubation, respectively
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Effect of zinc binding on the structure and stability of fibrolase
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C or -20°C, stable for 6 months, 20-30% loss of activity after 1 year
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation and DEAE-Sephadex gel filtration
ammonium sulfate precipitation and Poros-HQ ion-exchange column chromatography and Sephadex G100 gel filtration
-
ammonium sulfate precipitation, DEAE-cellulose ion-exchange column chromatography and Sephadex G-75 gel filtration
-
ammonium sulfate precipitation, dialysis and DEAE-cellulose column chromatography
-
ammonium sulfate precipitation, Hi Prep phenyl column chromatography, and Superdex 75 gel filtration
-
ammonium sulfate precipitation, HPD-100 macroporous resin column chromatography, 201 × 7 ion-exchange resin column chromatography, and Superdex 200 gel filtration
ammonium sulfate precipitation, octyl Sepharose column chromatography, SP Sepharose column chromatography, Sephadex G-25 gel filtration, and Superdex 75 gel filtration
-
aqueous two-phase system with 30% (w/v) polyethylene glycol 6000 and 13.2% (w/v) sodium sulfate
Mucor subtilissimus
-
DEAE Sepharose column chromatography and Q Sepharose column chromatography
-
DEAE-Sepharose CL6B column chromatography, Sepharose CL4B column chromatography, and Mono Q HR column chromatography
-
high performance liquid chromatography, hydroxyapatite high performance liquid chromatography and cation exchange high performance liquid chromatography
-
HiTrap Q-Sepharose column chromatography, gel filtration
hydrophobic interaction high performance liquid chromatography, hydroxyapatite high performance liquid chromatography and cation exchange high performance liquid chromatography
-
hydrophobic interaction HPLC, hydroxyapatite HPLC and cation exchange HPLC
-
native enzyme by hydrophobic interaction and hydroxyapatite chromatography
-
Q-Sepharose column chromatography, Sephacryl S-100 gel filtration, and Sephadex G-50 gel filtration
-
recombinant soluble His-tagged enzyme from Escherichia coli by nickel affinity and hydrophobic interaction chromatography to 95.6% purity
secreted recombinant His-tagged alfimeprase from Pichia pastoris strains of GS115 and KM71 cell culture medium by immunoaffinity chromatography to 96% purity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
chimeric Arg-Gly-Asp-fibrolase is expressed in Escherichia coli BL21(DE3) cells
co-expression of the active signal-less His-tagged enzyme with chaperone DsbC in Escherichia coli cytoplasm, over 90% of the recombinant enzyme is soluble due to DsbC, while the chaperones FkpA and Skp do not have an effect on fibrolase solubility
expression of the wild-type fibrolase and a truncated enzyme form, alfimeprase
-
gene alf, high level expression of His-tagged alfimeprase in Pichia pastoris strains of GS115 and KM71 by methanol induction, secretion of the recombinant enzyme to the cell culture medium
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cotton cake as nitrogen source enhances fibrinolytic protease production substantially (71%) as compared to control
soybean meal supports maximum protease production, followed by malt extract, cotton cake, gelatin and beef extract
the optimal conditions to obtain high protease production are 1.26% soybean flour and 1.23% glucose concentration
cotton cake as nitrogen source enhances fibrinolytic protease production substantially (71%) as compared to control
-
cotton cake as nitrogen source enhances fibrinolytic protease production substantially (71%) as compared to control
-
-
soybean meal supports maximum protease production, followed by malt extract, cotton cake, gelatin and beef extract
-
soybean meal supports maximum protease production, followed by malt extract, cotton cake, gelatin and beef extract
-
-
the optimal conditions to obtain high protease production are 1.26% soybean flour and 1.23% glucose concentration
-
the optimal conditions to obtain high protease production are 1.26% soybean flour and 1.23% glucose concentration
-
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
using 50 mM Tris-HCl, 0.5 M L-arginine, 1 M NaCl, 0.5 mM ZnCl2, 1 mM oxidized glutathione, 2 mM reduced glutathione, and 2 M urea at pH 7.0. After the protein is added, the pH is adjusted to 7.5, and the protein is left to refold at 4°C for approximately 24 h
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
-
summary of results (including adverse events and pharmacodynamics) regarding drug development of alfimeprase as a potential drug against thrombosis and vascular disorders
medicine
pharmacology
-
alfimeprase is a potential therapeutic agents in thrombosis therapy, clinical indications and studies, overview
medicine
development of more effective therapeutic approaches for treating occlusive thrombotic diseases, potential clinical interest in fibrolase for pharmacologic dissolution of an established thrombus
medicine
-
the enzyme effectively protects against acute pulmonary thromboembolism via degradation of thrombi with less activation of plasminogen
medicine
-
the use of the recombinant fibrolase alfimeprase results in rapid restoration of arterial patency in less than 4 h in most peripheral arterial occlusion patients
medicine
-
starase has the potential to be a potent thrombolytic agent due to its bi-functional properties (containing both direct-acting and plasminogen-activating activities) and lack of hemorrhagic activity
medicine
-
the enzyme has therapeutic potential in peptide-based cardiovascular drug development
medicine
the enzyme is a candidate for antithrombotic drug development
medicine
-
the enzyme is useful for reducing or preventing thrombotic challenge
medicine
-
the enzyme has therapeutic potential in peptide-based cardiovascular drug development
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Guan, A.L.; Retzios, A.D.; Henderson, G.N.; Markland, F.S.
Purification and characterization of a fibrinolytic enzyme from venom of the southern copperhead snake (Agkistrodon contortrix contortrix)
Arch. Biochem. Biophys.
289
197-207
1991
Agkistrodon contortrix contortrix
brenda
Retzios, A.D.; Markland, F.S.
A direct-acting fibrinolytic enzyme from the venom of Agkistrodon contortrix contortrix: effects on various components of the human blood coagulation and fibrinolysis systems
Thromb. Res.
52
541-552
1988
Agkistrodon contortrix contortrix
brenda
Randolph, A.; Chamberlain, S.H.; Chu, H.L.C.; Retzios, A.D.; Markland, F.S.; Masiarz, F.R.
Amino acid sequence of fibrolase, a direct-acting fibrinolytic enzyme from Agkistrodon contortrix contortrix venom
Protein Sci.
1
590-600
1992
Agkistrodon contortrix contortrix
brenda
Loayza, S.L.; Trikha, M.; Markland, F.S.; Riquelme, P.; Kuo, J.
Resolution of isoforms of natural and recombinant fibrolase, the fibrinolytic enzyme from Agkistrodon contortrix contortrix snake venom, and comparison of their EDTA sensitivities
J. Chromatogr.
662
227-243
1994
Agkistrodon contortrix contortrix
brenda
Retzios, A.D.; Markland, F.S.
Fibrinolytic enzymes from the venoms of Agkistrodon contortrix contortrix and Crotalus basiliscus basiliscus: cleavage site specificity towards the alpha-chain of fibrin
Thromb. Res.
74
355-367
1994
Agkistrodon contortrix contortrix
brenda
Manning, M.C.
Sequence analysis of fibrolase, a fibrinolytic metalloproteinase from Agkistrodon contortrix contortrix
Toxicon
33
1189-1200
1995
Agkistrodon contortrix contortrix
brenda
Trikha, M.; Schmitmeier, S.; Markland, F.S.
Purification and characterization of fibrolase isoforms from venom of individual southern copperhead (Agkistrodon contortrix Contortrix) snakes
Toxicon
32
1521-1531
1994
Agkistrodon contortrix contortrix
brenda
Patton, L.M.; Pretzer, D.; Schulteis, B.S.; Saggart, B.S.; Tennant, K.D.; Ahmed, N.K.
Activity assays for characterizing the thrombolytic protein fibrolase
J. Biochem. Biophys. Methods
27
11-23
1993
Agkistrodon contortrix contortrix
brenda
Markland, F.S.; Morris, S.; Deschamps, J.R.; Ward, K.B.
Resolution of isoforms of natural and recombinant fibrinolytic snake venom enzyme using high performance capillary electrophoresis
J. Liq. Chromatogr.
16
2189-2201
1993
Agkistrodon contortrix contortrix
-
brenda
Pretzer, D.; Schulteis, B.; Vander Velde, D.G.; Smith, C.D.; Mitchell, J.W.; Manning, M.C.
Effect of zinc binding on the structure and stability of fibrolase, a fibrinolytic protein from snake venom
Pharm. Res.
9
870-877
1992
Agkistrodon contortrix contortrix
brenda
Pretzer, D.; Schulteis, B.S.; Smith, C.D.; Vander Velde, D.G.; Mitchell, J.W.; Manning, M.C.
Stability of the thrombolytic protein fibrolase: effect of temperature and pH on activity and conformation
Pharm. Res.
8
1103-1112
1991
Agkistrodon contortrix contortrix
brenda
Chen, H.M.; Guan, A.L.; Markland, F.S.
Immunological properties of the fibrinolytic enzyme (fibrolase) from southern copperhead (Agkistrodon contortrix contortrix) venom and its purification by immunoaffinity chromatography
Toxicon
29
683-694
1991
Agkistrodon contortrix contortrix
brenda
Guan, A.L.; Markland, F.S.
Isoelectric focusing in immobilized pH gradients of a snake venom fibrinolytic enzyme
J. Biochem. Biophys. Methods
16
215-226
1988
Agkistrodon contortrix contortrix
brenda
Bolger, M.B.; Swenson, S.; Markland, F.S., Jr.
Three-dimensional structure of fibrolase, the fibrinolytic enzyme from southern copperhead venom, modeled from the X-ray structure of adamalysin II and atrolysin C
AAPS Pharmsci.
3
E16
2001
Agkistrodon contortrix contortrix (P28891), Agkistrodon contortrix contortrix
brenda
Swenson, S.; Toombs, C.F.; Pena, L.; Johansson, J.; Markland, F.S.
alpha-Fibrinogenases
Curr. Drug Targets Cardiovasc. Haematol. Disord.
4
417-435
2004
Agkistrodon contortrix
brenda
Swenson, S.; Markland, F.S.; Toombs, C.
Fibrolase
Handbook of Proteolytic Enzymes (Barrett,A. J. ;Rawlings,N. D. ,Woessner)
1
640-643
2004
Agkistrodon contortrix
-
brenda
Swenson, S.; Markland, F.S.
Snake venom fibrin(ogen)olytic enzymes
Toxicon
45
1021-1039
2005
Gloydius halys, Bothrops neuwiedi, Agkistrodon contortrix
brenda
Shi, J.; Zhang, S.T.; Zhang, X.J.; Xu, H.; Guo, A.G.
Expression, purification, and activity identification of alfimeprase in Pichia pastoris
Protein Expr. Purif.
54
240-246
2007
Agkistrodon contortrix contortrix (P28891)
brenda
Zhang, S.T.; Shi, J.; Zhao, J.; Qi, Y.F.; Guo, A.G.
Expression of soluble and functional snake venom fibrinolytic enzyme fibrolase via the co-expression of DsbC in Escherichia coli
Protein Pept. Lett.
13
559-563
2006
Agkistrodon contortrix contortrix (P28891), Agkistrodon contortrix contortrix
brenda
Swenson, S.; Markland, F.S.
Fibrolase
Toxin Rev.
25
351-378
2006
Agkistrodon contortrix contortrix
-
brenda
Toombs, C.F.; Deitcher, S.R.
Nonclinical and clinical characterization of a novel acting thrombolytic: alfimeprase
Toxin Rev.
25
379-392
2006
Agkistrodon contortrix contortrix
-
brenda
No authors listed
Alfimeprase
Drugs R. D.
9
185-190
2008
Agkistrodon contortrix contortrix
brenda
Verhamme, I.M.; Bock, P.E.
Rapid-reaction kinetic characterization of the pathway of streptokinase-plasmin catalytic complex formation
J. Biol. Chem.
283
26137-26147
2008
Homo sapiens
brenda
Lin, X.; Liang, X.; Tang, J.; Chen, J.; Qiu, P.; Yan, G.
The effect of the fibrinolytic enzyme FIIa from Agkistrodon acutus venom on acute pulmonary thromboembolism
Acta Pharmacol. Sin.
32
239-244
2011
Deinagkistrodon acutus
brenda
Fang, H.M.; Zhao, L.; Lu, P.; Chen, S.J.; Bao, Z.X.; Qin, Y.F.; Zhu, Z.Y.; Zhao, J.M.; Mai, J.; Zhang, S.T.
Modular design, expression and characterization of novel bifunctional mutants of fibrolase with combined platelet aggregation-inhibition and fibrinolytic activity
Protein J.
30
247-252
2011
Agkistrodon contortrix contortrix (P28891), Agkistrodon contortrix contortrix
brenda
Markland, F.S.; Swenson, S.
Fibrolase: trials and tribulations
Toxins
2
793-808
2010
Agkistrodon contortrix contortrix
brenda
Bajaj, B.; Sharma, N.; Singh, S.
Enhanced production of fibrinolytic protease from Bacillus cereus NS-2 using cotton seed cake as nitrogen source
Biocatal. Agricult. Biotechnol.
2
204-209
2013
Bacillus cereus, Bacillus cereus NS-2
-
brenda
Majumdar, S.; Sarmah, B.; Gogoi, D.; Banerjee, S.; Ghosh, S.; Banarjee, S.; Chattopadhyay, P.; Mukherjee, A.
Characterization, mechanism of anticoagulant action, and assessment of therapeutic potential of a fibrinolytic serine protease (Brevithrombolase) purified from Brevibacillus brevis strain FF02B
Biochimie
103
50-60
2014
Brevibacillus brevis, Brevibacillus brevis FF02B
brenda
Choi, J.; Sapkota, K.; Kim, S.; Kim, S.
Starase: A bi-functional fibrinolytic protease from hepatic caeca of Asterina pectinifera displays antithrombotic potential
Biochimie
105
45-57
2014
Patiria pectinifera
brenda
Bi, Q.; Han, B.; Liu, W.; Feng, Y.; Jiang, Z.
UFEIII, a fibrinolytic protease from the marine invertebrate, Urechis unicinctus
Biotechnol. Lett.
35
1115-1120
2013
Urechis unicinctus
brenda
Bajaj, B.; Singh, S.; Khullar, M.; Singh, K.; Bhardwaj, S.
Optimization of fibrinolytic protease production from Bacillus subtilis I-2 using agro-residues
Braz. Arch. Biol. Technol.
57
653-662
2014
Bacillus subtilis, Bacillus subtilis I-2
-
brenda
Silva, G.; Bezerra, R.; Teixeira, J.; Porto, T.; Lima-Filho, J.; Porto, A.
Fibrinolytic protease production by new Streptomyces sp. DPUA 1576 from Amazon lichens
Electron. J. Biotechnol.
18
16-19
2015
Streptomyces sp., Streptomyces sp. DPUA 1576
-
brenda
Bagchi, S.; Sondhia, S.; Agrawal, M.; Banerjee, S.
An angiotensin-converting enzyme-inhibitory metabolite with partial structure of microginin in a cyanobacterium Anabaena fertilissima CCC597, producing fibrinolytic protease
J. Appl. Phycol.
28
177-180
2016
Trichormus fertilissimus, Trichormus fertilissimus CCC597
-
brenda
Taneja, K.; Bajaj, B.; Kumar, S.; Dilbaghi, N.
Production, purification and characterization of fibrinolytic enzyme from Serratia sp. KG-2-1 using optimized media
3 Biotech
7
184
2017
Serratia sp. KG-2-1
brenda
Silva, G.; Bezerra, R.; Teixeira, J.; Silva, F.; Correia, J.; Porto, T.; Lima-Filho, J.; Porto, A.
Screening, production and biochemical characterization of a new fibrinolytic enzyme produced by Streptomyces sp. (Streptomycetaceae) isolated from Amazonian lichens
Acta Amaz.
46
301-310
2016
Streptomyces sp. DPUA1576
-
brenda
Xiao, P.; Yao, S.; Liu, J.; Miao, Y.; Wang, Y.
Enhanced production of fibrinolytic enzyme from Bacillus amyloliquefaciens CGMCC 7380 using broad bean (Vicia faba L.) as substrate
Adv. J. Food Sci. Technol.
9
832-839
2015
Bacillus amyloliquefaciens, Bacillus amyloliquefaciens CGMCC 7380
-
brenda
Meshram, V.; Saxena, S.; Paul, K.; Gupta, M.; Kapoor, N.
Production, purification and characterisation of a potential fibrinolytic protease from endophytic Xylaria curta by solid substrate fermentation
Appl. Biochem. Biotechnol.
181
1496-1512
2017
Xylaria curta
brenda
Choi, J.; Lee, H.; Kim, S.
Purification and antithrombotic activity of wulfase, a fibrinolytic enzyme from the fruit bodies of the edible and medicinal mushroom Sparassis crispa Wulf. ex. Fr
Appl. Biochem. Microbiol.
52
608-614
2016
Sparassis crispa
-
brenda
Verma, P.; Chatterjee, S.; Keziah, M.S.; Devi, S.C.
Fibrinolytic protease from marine Streptomyces rubiginosus VITPSS1
Cardiovasc. Hematol. Agents Med. Chem.
16
44-55
2018
Streptomyces rubiginosus, Streptomyces rubiginosus VITPSS1
brenda
Yogesh, D.; Halami, P.
Evidence that multiple proteases of Bacillus subtilis can degrade fibrin and fibrinogen
Int. Food Res. J.
22
1662-1667
2015
Bacillus subtilis, Bacillus subtilis BR21
-
brenda
Sun, Z.; Liu, P.; Cheng, G.; Zhang, B.; Dong, W.; Su, X.; Huang, Y.; Cui, Z.; Kong, Y.
A fibrinolytic protease AfeE from Streptomyces sp. CC5, with potent thrombolytic activity in a mouse model
Int. J. Biol. Macromol.
85
346-354
2016
Streptomyces sp. CC5 (A0A0A7W604)
brenda
Nascimento, T.; Sales, A.; Porto, C.; Brandao, R.; de Campos-Takaki, G.; Teixeira, J.; Porto, T.; Porto, A.; Converti, A.
Purification of a fibrinolytic protease from Mucor subtilissimus UCP 1262 by aqueous two-phase systems (PEG/sulfate)
J. Chromatogr. B Analyt. Technol. Biomed. Life Sci.
1025
16-24
2016
Mucor subtilissimus, Mucor subtilissimus UCP 1262
brenda
Khobragade, C.; Gophane, S.; Motwani, R.
Purification and characterization of extracellular protease from soil isolate Stenotrophomonas maltophilia as novel target for fibrinolysis
J. Microbiol. Biotechnol. Food Sci.
7
496-502
2018
Stenotrophomonas maltophilia, Stenotrophomonas maltophilia CNK-7R
-
brenda
Liu, X.; Kopparapu, N.; Zheng, H.; Katrolia, P.; Deng, Y.; Zheng, X.
Purification and characterization of a fibrinolytic enzyme from the food-grade fungus, Neurospora sitophila
J. Mol. Catal. B
134
98-104
2016
Neurospora sitophila
-
brenda
de Souza, F.; Sales, A.; Costa e Silva, P.; Bezerra, R.; de Medeiros e Silva, G.; de Araújo, J.; de Campos Takaki, G.; Porto, T.; Teixeira, J.; Porto, A.
Optimization of production, biochemical characterization and in vitro evaluation of the therapeutic potential of fibrinolytic enzymes from a new Bacillus amyloliquefaciens
Macromol. Res.
24
587-595
2016
Bacillus amyloliquefaciens, Bacillus amyloliquefaciens UFPEDA 485
-
brenda
D, D.; S, J.N.; S, M.K.; C, S.D.
Novel fibrinolytic protease producing Streptomyces radiopugnans VITSD8 from marine sponges
Mar. Drugs
17
164
2019
Streptomyces radiopugnans, Streptomyces radiopugnans VITSD8
brenda
Devaraj, Y.; Rajender, S.K.; Halami, P.M.
Purification and characterization of fibrinolytic protease from Bacillus amyloliquefaciens MCC2606 and analysis of fibrin degradation product by MS/MS
Prep. Biochem. Biotechnol.
48
172-180
2018
Bacillus amyloliquefaciens, Bacillus amyloliquefaciens MCC2606
brenda
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