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Literature summary extracted from

  • Markland, F.S.; Swenson, S.
    Fibrolase: trials and tribulations (2010), Toxins, 2, 793-808.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.24.72 additional information the enzyme is a direct-acting thrombolytic agent and does not rely on plasminogen for clot dissolution Agkistrodon contortrix contortrix

Application

EC Number Application Comment Organism
3.4.24.72 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 Agkistrodon contortrix contortrix

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.24.72 expressed in Pichia pastoris Agkistrodon contortrix contortrix

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.72 alpha2-Macroglobulin
-
 Agkistrodon contortrix contortrix
3.4.24.72 EDTA
-
 Agkistrodon contortrix contortrix

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.72 Zn2+ a zinc metalloproteinase containing one mole of zinc Agkistrodon contortrix contortrix

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.24.72 23000
-
 x * 23000 Agkistrodon contortrix contortrix

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.24.72 bradykinin + H2O Agkistrodon contortrix contortrix
-
 Arg-Pro-Pro-Gly-Phe-Ser-Pro + Phe-Arg
-
 ?
3.4.24.72 Fibrin + H2O Agkistrodon contortrix contortrix fibrinolase cleaves the alpha-chain more rapidly than the beta-chain of fibrin ?
-
 ?
3.4.24.72 Fibrinogen + H2O Agkistrodon contortrix contortrix 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 ?
-
 ?
3.4.24.72 low molecular weight kininogen + H2O Agkistrodon contortrix contortrix
-
 kallidin + ? i.e. Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg ?
3.4.24.72 additional information Agkistrodon contortrix contortrix fibrolase neither activates nor degrades plasminogen ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.72 Agkistrodon contortrix contortrix
-
 southern copperhead snake
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.24.72 hydrophobic interaction HPLC, hydroxyapatite HPLC and cation exchange HPLC Agkistrodon contortrix contortrix

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.24.72 venom
-
 Agkistrodon contortrix contortrix
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.72 bradykinin + H2O
-
 Agkistrodon contortrix contortrix Arg-Pro-Pro-Gly-Phe-Ser-Pro + Phe-Arg
-
 ?
3.4.24.72 Fibrin + H2O fibrinolase cleaves the alpha-chain more rapidly than the beta-chain of fibrin Agkistrodon contortrix contortrix ?
-
 ?
3.4.24.72 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 Agkistrodon contortrix contortrix ?
-
 ?
3.4.24.72 low molecular weight kininogen + H2O
-
 Agkistrodon contortrix contortrix kallidin + ? i.e. Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg ?
3.4.24.72 additional information fibrolase neither activates nor degrades plasminogen Agkistrodon contortrix contortrix ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.24.72 ? x * 23000 Agkistrodon contortrix contortrix

Synonyms

EC Number Synonyms Comment Organism
3.4.24.72 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 Agkistrodon contortrix contortrix