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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
-
nonhemorrhagic
- neuwiedi
- alteplase
- pharmacology
- drug development
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
fibrolase, alfimeprase, fibrinolytic protease, neuwiedase, brevithrombolase, starase, fibrinolytic proteinase, ufeiii, snake venom fibrinolytic enzyme, cfr15-protease, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Agkistrodon contortrix contortrix metalloproteinase
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-
-
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Alfimeprase
brevithrombolase
broad bean-fibrinolytic enzyme
CFR15-protease
fibrinolytic enzyme
fibrinolytic protease
Fibrinolytic proteinase
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-
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Non-hemorrhagic fibrinolytic metalloproteinase
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-
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Proteinase, Agkistrodon contortrix contortrix venom metallo-
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-
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VlF
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-
-
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Alfimeprase
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Alfimeprase
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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
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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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-
-
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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
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
?
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human, cleavage at Lys413-Lys414, the Bbeta-chain is cleaved more slowly and the gamma-chain is minimally affected
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-
?
fibrin clot + H2O
?
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the enzyme induces inhibition of fibrin clot formation in a concentration-dependent manner
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-
?
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
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i.e. pyroGlu-Gly-Arg-4-nitroanilide
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-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-4-nitroanilide + H2O
succinyl-L-Ala-L-Ala-L-Pro-L-Phe + 4-nitroaniline
-
-
-
-
?
bovine plasma fibrinogen + H2O
?
-
marginal hydrolytic activity
-
-
?
Bovine serum albumin + H2O
?
-
16.62% activity compared to human fibrin
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-
?
Bovine serum albumin + H2O
?
Bacillus amyloliquefaciens MCC2606
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16.62% activity compared to human fibrin
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-
?
D-Val-Leu-Lys-4-nitroanilide + H2O
D-Val-Leu-Lys + 4-nitroaniline
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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
?
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fibrinolase cleaves the alpha-chain more rapidly than the beta-chain of fibrin
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-
?
Fibrin + H2O
?
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the enzyme can catalyze fibrin clot lysis effectively
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-
?
Fibrin + H2O
?
Bacillus amyloliquefaciens CGMCC 7380
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the enzyme can catalyze fibrin clot lysis effectively
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?
Fibrin + H2O
?
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the enzyme degrades all the four peptide chains of fibrin rapidly
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?
Fibrin + H2O
?
Bacillus subtilis BR21
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the enzyme degrades all the four peptide chains of fibrin rapidly
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?
Fibrin + H2O
?
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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
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?
Fibrin + H2O
?
best substrate. The enzyme exhibits about 2fold higher activity for fibrin than fibrinogen. Fibrin can be hydrolyzed completely in about 30 min
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-
?
Fibrinogen + H2O
?
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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
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?
Fibrinogen + H2O
?
the enzyme has a direct proteolytic activity against the A alpha-chain of fibrinogen at positions Lys413 and Leu414
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?
fibrinogen + H2O
fibrin + ?
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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
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?
fibrinogen + H2O
fibrin + ?
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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
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?
fibrinogen + H2O
fibrin + ?
Bacillus amyloliquefaciens MCC2606
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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
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?
fibrinogen + H2O
fibrin + ?
Bacillus amyloliquefaciens UFPEDA 485
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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
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?
fibrinogen + H2O
fibrin + ?
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the enzyme degrades only Aalpha and Bbeta chains of fibrinogen
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?
fibrinogen + H2O
fibrin + ?
Bacillus subtilis BR21
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the enzyme degrades only Aalpha and Bbeta chains of fibrinogen
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?
fibrinogen + H2O
fibrin + ?
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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
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?
fibrinogen + H2O
fibrin + ?
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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
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?
fibrinogen + H2O
fibrin + ?
fibrinogen can be hydrolyzed completely in 4-6 h
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?
fibrinogen + H2O
fibrin + ?
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the enzyme exhibits cleavage of Aalphaand Bbeta chains of fibrin(ogen) and has no effect on gamma chain
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?
fibrinogen + H2O
fibrin + propeptide
bovine substrate
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?
fibrinogen + H2O
fibrin + propeptide
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fibrinogenolytic activity
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?
fibrinogen + H2O
fibrin + propeptide
bovine substrate, fibrinogenolytic activity
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?
fibrinogen + H2O
fibrin + propeptide
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human substrate, fibrinogenolytic activity
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?
Fibrinogen Aalpha-chain + H2O
?
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cleavage at Lys413-Leu414 (initial cleavage)
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?
Fibrinogen Aalpha-chain + H2O
?
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cleavage specificity is not dictated by the Lys-Leu bond per se, but by the surrounding sequence
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?
Fibrinogen Aalpha-chain + H2O
?
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the Bbeta-chain is cleaved more slowly and the gamma-chain is minimally affected
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?
Hemoglobin + H2O
?
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25.09% activity compared to human fibrin
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-
?
Hemoglobin + H2O
?
Bacillus amyloliquefaciens MCC2606
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25.09% activity compared to human fibrin
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?
His-Thr-Glu-Lys-Leu-Val-Thr-Ser + H2O
?
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cleaving sequence residues 410-417 from fibrinogen Aalpha-chain
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?
human fibrin + H2O
?
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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
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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
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-
?
Insulin B-chain + H2O
?
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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 + ?
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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
?
-
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exhibits little if any hemorrhagic activity
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-
?
additional information
?
-
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does not activate protein C
-
-
?
additional information
?
-
-
does not activate plasminogen
-
-
?
additional information
?
-
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does not activate plasminogen
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-
?
additional information
?
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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
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-
?
additional information
?
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alfimeprase is the recombinant truncated form of fibrolase from snake venom lacking the two N-terminal amino acids Glu and Gln
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?
additional information
?
-
the enzyme is a nonhemorrhagic zinc metalloprotease
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?
additional information
?
-
the enzyme is a nonhemorrhagic zinc metalloprotease
-
-
?