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Enzyme Nomenclature
Information on EC 3.4.24.72 - fibrolase
for references in articles please use BRENDA:EC3.4.24.72
Word Map on EC 3.4.24.72
- 3.4.24.72
- plasmin
-
thrombolytic
- copperhead
-
fibrinogenolytic
- alteplase
- medicine
-
nonhemorrhagic
- neuwiedi
- drug development
- pharmacology
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
3.4.24.72
-
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RECOMMENDED NAME
GeneOntology No.
fibrolase
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subspecies Agkistrodon contortrix contortrix, southern copperhead snake
-
-
-
-
-
southern copperhead, isoforms of natural and recombinant enzyme
-
-
southern copperhead, isoforms of natural and recombinant enzyme (resolution by high performance capillary electrophoresis)
-
-
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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-Val-Leu-Lys-4-nitroanilide + H2O
D-Val-Leu-Lys + 4-nitroaniline
-
highest activity
-
-
?
Fibrin Aalpha-chain + H2O
?
-
human, cleavage at Lys413-Lys414, the Bbeta-chain is cleaved more slowly and the gamma-chain is minimally affected
-
-
-
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
-
-
?
bovine plasma fibrinogen + H2O
?
-
marginal hydrolytic activity
-
-
?
Fibrin + H2O
?
-
fibrinolytic activity
-
-
?
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 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 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 + 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
-
-
-
His-Thr-Glu-Lys-Leu-Val-Thr-Ser + H2O
?
-
cleaving sequence residues 410-417 from fibrinogen Aalpha-chain
-
-
?
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
?
-
-
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, 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
?
-
-
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
?
-
-
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
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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 + ?
-
-
i.e. Lys-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
?
P28891
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 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 + propeptide
-
bovine substrate
-
-
?
fibrinogen + H2O
fibrin + propeptide
-
fibrinogenolytic activity
-
-
?
additional information
?
-
-
thrombolysis in animals by snake venom alfimeprase, overview
-
-
-
additional information
?
-
P28891
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+
Mg2+
Mn2+
Zinc
Zn2+
additional information
Zinc
-
enzyme contains 1 mol of zinc per mol of protein; zinc metalloproteinase
Zinc
-
identification of the zinc binding site; zinc metalloproteinase
Zinc
-
effect of zinc binding on the structure and stability of fibrolase; zinc metalloproteinase
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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INHIBITORS
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
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
Tetraethylenepentamine
-
complete and rapid inhibition
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
-
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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 is a direct-acting thrombolytic agent and does not rely on plasminogen for clot dissolution
-
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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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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
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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%)
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
50
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 60
-
considerable activity is observed at 60°C (88.6%) and at 40°C (68.6%)
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8
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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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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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SUBUNITS
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
-
additional information
-
the protein is composed of 5 alpha-helical regions, 4 parallel and 1 antiparallel beta-sheet, stablized by 3 disulfide bonds
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
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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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
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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 80
-
fibrinolytic protease loses about 40-60% of its activity after 1 h incubation at 20-80°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
-
about 50% loss of activity after 2 days, complete loss of activity after 10 days
additional information
-
effect of temperature on conformation
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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, Hi Prep phenyl column chromatography, and Superdex 75 gel filtration
-
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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ENGINEERING
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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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
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summary of results (including adverse events and pharmacodynamics) regarding drug development of alfimeprase as a potential drug against thrombosis and vascular disorders
medicine
pharmacology
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alfimeprase is a potential therapeutic agents in thrombosis therapy, clinical indications and studies, overview
medicine
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development of more effective therapeutic approaches for treating occlusive thrombotic diseases, potential clinical interest in fibrolase for pharmacologic dissolution of an established thrombus
medicine
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the enzyme effectively protects against acute pulmonary thromboembolism via degradation of thrombi with less activation of plasminogen
medicine
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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
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the enzyme has therapeutic potential in peptide-based cardiovascular drug development
medicine
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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
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LINKS TO OTHER DATABASES (specific for EC-Number 3.4.24.72)
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