Horrilysin | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC no. | 3.4.24.47 | ||||||||
CAS no. | 84056-81-5 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
|
Horrilysin (EC 3.4.24.47, Crotalus horridus metalloendopeptidase, hemorrhagic proteinase IV, Crotalus horridus horridus venom hemorrhagic proteinase) is an enzyme. This enzyme catalyses the following chemical reaction
- Cleavage of only the single bond Ala-Leu in the insulin B chain, Ser-Leu in the A chain, and Ile-Gly, Pro-Ala, and Ser-Trp in melittin
This endopeptidase is present in the venom of the timber rattlesnake (Crotalus horridus horridus)
References
- Civello DJ, Duong HL, Geren CR (February 1983). "Isolation and characterization of a hemorrhagic proteinase from timber rattlesnake venom". Biochemistry. 22 (4): 749–55. doi:10.1021/bi00273a007. PMID 6340728.
- Civello DJ, Moran JB, Geren CR (February 1983). "Substrate specificity of a hemorrhagic proteinase from timber rattlesnake venom". Biochemistry. 22 (4): 755–62. doi:10.1021/bi00273a008. PMID 6340729.
External links
- Horrilysin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
Proteases: metalloendopeptidases (EC 3.4.24) | |
---|---|
ADAM proteins | |
Matrix metalloproteinases | |
Other |
Enzymes | |
---|---|
Activity | |
Regulation | |
Classification | |
Kinetics | |
Types |
|