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Fibrolase (EC 3.4.24.72,fibrinolytic proteinase,Agkistrodon contortrix contortrix metalloproteinase,Agkistrodon contortrix contortrix venom metalloproteinase) is anenzyme.^[1]^[2]^[3]^[4]^[5] This enzymecatalyses the followingchemical reaction

Hydrolysis of -Ala¹⁴-Leu- ininsulin B chain and -Lys⁴¹³-Leu- in alpha-chain offibrinogen

This enzyme is present in the venom of the southern copperhead snake (Agkistrodon contortrix contortrix).

References

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^Retzios AD, Markland FS (December 1988). "A direct-acting fibrinolytic enzyme from the venom of Agkistrodon contortrix contortrix: effects on various components of the human blood coagulation and fibrinolysis systems".Thrombosis Research.52 (6):541–52.doi:10.1016/0049-3848(88)90127-2.PMID 3232124.
^Guan AL, Retzios AD, Henderson GN, Markland FS (September 1991). "Purification and characterization of a fibrinolytic enzyme from venom of the southern copperhead snake (Agkistrodon contortrix contortrix)".Archives of Biochemistry and Biophysics.289 (2):197–207.doi:10.1016/0003-9861(91)90462-r.PMID 1898066.
^Randolph A, Chamberlain SH, Chu HL, Retzios AD, Markland FS, Masiarz FR (May 1992)."Amino acid sequence of fibrolase, a direct-acting fibrinolytic enzyme from Agkistrodon contortrix contortrix venom".Protein Science.1 (5):590–600.doi:10.1002/pro.5560010505.PMC 2142229.PMID 1304358.
^Loayza SL, Trikha M, Markland FS, Riquelme P, Kuo J (December 1994). "Resolution of isoforms of natural and recombinant fibrolase, the fibrinolytic enzyme from Agkistrodon contortrix contortrix snake venom, and comparison of their EDTA sensitivities".Journal of Chromatography B.662 (2):227–43.doi:10.1016/0378-4347(94)00202-9.PMID 7719479.
^Retzios AD, Markland FS (May 1994). "Fibrinolytic enzymes from the venoms of Agkistrodon contortrix contortrix and Crotalus basiliscus basiliscus: cleavage site specificity towards the alpha-chain of fibrin".Thrombosis Research.74 (4):355–67.doi:10.1016/0049-3848(94)90151-1.PMID 8085237.

External links

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Fibrolase at the U.S. National Library of MedicineMedical Subject Headings (MeSH)

v t e Proteases:metalloendopeptidases (EC 3.4.24)
ADAM proteins	Alpha secretases ADAM9 ADAM10 ADAM17 ADAM19 ADAM2 ADAM7 ADAM8 ADAM11 ADAM12 ADAM15 ADAM18 ADAM22 ADAM23 ADAM28 ADAM33 ADAMTS1 ADAMTS2 ADAMTS3 ADAMTS4 ADAMTS5 ADAMTS8 ADAMTS9 ADAMTS10 ADAMTS12 ADAMTS13
Matrix metalloproteinases	Collagenases MMP1 MMP8 Gelatinases MMP2 MMP9 MMP3 MMP7 MMP10 MMP11 MMP12 MMP13 MMP14 MMP15 MMP16 MMP17 MMP19 MMP20 MMP21 MMP23A MMP23B MMP24 MMP25 MMP26 MMP27 MMP28
Other	Neprilysin Procollagen peptidase Thermolysin Pregnancy-associated plasma protein A Bone morphogenetic protein 1 Lysostaphin Insulin-degrading enzyme ZMPSTE24

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1Oxidoreductases (list) EC2Transferases (list) EC3Hydrolases (list) EC4Lyases (list) EC5Isomerases (list) EC6Ligases (list) EC7Translocases (list)

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Category:

EC 3.4.24

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