Title: Fibrolase
CAS Registry Number: 116036-70-5
Literature References: Fibrinolytic enzyme isolated from the venom of the southern copperhead snake, Agkistrodon contortrix contortix. Single chain, zinc metalloproteinase which preferentially cleaves the Aa chain of fibrinogen and fibrin. Several isoforms have been identified; the longest form has 203 amino acid residues with mol wt of 23 kDa. Isoln: N. B. Egen et al., Toxicon 25, 1189 (1987); and effect on human coagulation system: A. D. Retzios, F. S. Markland, Jr., Thromb. Res. 52, 541 (1988). Amino acid sequence: A. Randoph et al., Protein Sci. 1, 590 (1992). Resolution of isoforms: S. L. Loayza et al., J. Chromatogr. B 662, 227 (1994). Three-dimensional structure: M. B. Bolger et al., AAPS Pharmsci. 3, E16 (2001). Review and comparison with other snake venom fibrinolytic enzymes: S. Swenson, F. S. Markland, Jr., Toxicon 45, 1021-1039 (2005).
Properties: pI ~6.8.
Fibronectins Fichtelite Ficin Fidarestat Filicinic Acid

EC number
CAS number 116036-70-5
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Fibrolase (EC, 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 Aalpha-chain of fibrinogen

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