Fibrolase

Last updated
Fibrolase
Identifiers
EC no. 3.4.24.72
CAS no. 116036-70-5
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

Fibrolase (EC 3.4.24.72, fibrinolytic proteinase, Agkistrodon contortrix contortrix metalloproteinase, Agkistrodon contortrix contortrix venom metalloproteinase) is an enzyme. [1] [2] [3] [4] [5] This enzyme catalyses the following chemical reaction

Hydrolysis of -Ala14-Leu- in insulin B chain and -Lys413-Leu- in alpha-chain of fibrinogen

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

Related Research Articles

<span class="mw-page-title-main">Eastern copperhead</span> Species of reptile

The eastern copperhead, also known simply as the copperhead, is a species of venomous snake, a pit viper, endemic to eastern North America; it is a member of the subfamily Crotalinae in the family Viperidae.

<i>Agkistrodon</i> Genus of snakes

Agkistrodon is a genus of venomous pit vipers commonly known as American moccasins. The genus is endemic to North America, ranging from the Southern United States to northern Costa Rica. Eight species are currently recognized, all of them monotypic and closely related. Common names include: cottonmouths, copperheads, and cantils.

<span class="mw-page-title-main">Disintegrin</span> Proteins from viper venom inhibiting platelets aggregation

Disintegrins are a family of small proteins from viper venoms that function as potent inhibitors of both platelet aggregation and integrin-dependent cell adhesion.

<i>Agkistrodon laticinctus</i> Species of snake

Agkistrodon laticinctus, commonly known as the broad-banded copperhead, is a venomous pit viper species, formerly considered a subspecies of Agkistrodon contortrix, which is found in the southern United States, from Kansas, through Oklahoma and throughout central Texas.

Adamalysin is an enzyme. This enzyme catalyses the following chemical reaction

Helge Stormorken was a Norwegian veterinarian and physician.

<span class="mw-page-title-main">Cysteine-rich secretory protein</span>

Cysteine-rich secretory proteins, often abbreviated as CRISPs, are a group of glycoproteins. They are a subgroup of the CRISP, antigen 5 and Pr-1 (CAP) protein superfamily and also contain a domain related to the ShK toxins. They are substantially implicated in the functioning of the mammalian reproductive system. CRISPs are also found in a variety of snake venoms where they inhibit both smooth muscle contraction and cyclic nucleotide-gated ion channels.

Venombin A is an enzyme. This enzyme catalyses the following chemical reaction

Snake venom factor V activator is an enzyme. This enzyme catalyses the following chemical reaction

Atrolysin A is an enzyme that is one of six hemorrhagic toxins found in the venom of western diamondback rattlesnake. This endopeptidase has a length of 419 amino acid residues. The metalloproteinase disintegrin-like domain and the cysteine-rich domain of the enzyme are responsible for the enzyme's hemorrhagic effects on organisms via inhibition of platelet aggregation.

Bothropasin is an enzyme. This enzyme catalyses the following chemical reaction

Leucolysin is an enzyme. This enzyme catalyses the following chemical reaction

Atrolysin C is an enzyme. This enzyme catalyses the following chemical reaction

Atroxase is an enzyme. This enzyme catalyses the following chemical reaction

Atrolysin E is an enzyme. This enzyme catalyses the following chemical reaction

Ruberlysin is an enzyme. This enzyme catalyses the following chemical reaction

Trimerelysin I is an enzyme. This enzyme catalyses the following chemical reaction

Trimerelysin II is an enzyme. This enzyme catalyses the following chemical reaction

Mucrolysin is an enzyme. This enzyme catalyses the following chemical reaction

Jararhagin is an enzyme. This enzyme catalyses the following chemical reaction

References

  1. 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.
  2. 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.
  3. 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.
  4. 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.
  5. 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.