Hepacivirin
| Hepacivirin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.21.98 | ||||||||
| CAS no. | 149885-80-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Hepacivirin (EC 3.4.21.98, Cpro-2, hepatitis C virus NS3 serine proteinase, NS3-4A serine proteinase complex) is an enzyme.[1][2] This enzyme catalyses the following chemical reaction:
- Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'
This enzyme is encoded by the genome of the viruses of the hepatitis C group.
References
[edit]- ^ Kim JL, Morgenstern KA, Lin C, Fox T, Dwyer MD, Landro JA, Chambers SP, Markland W, Lepre CA, O'Malley ET, Harbeson SL, Rice CM, Murcko MA, Caron PR, Thomson JA (October 1996). "Crystal structure of the hepatitis C virus NS3 protease domain complexed with a synthetic NS4A cofactor peptide". Cell. 87 (2): 343–55. doi:10.1016/s0092-8674(00)81351-3. PMID 8861917.
- ^ Rice, C.M.; Rawlings, N.D.; Woessner, J.F. (1998). "Hepatitis C virus polyprotein peptidase". In Barrett, A.J. (ed.). Handbook of Proteolytic Enzymes. London: Academic Press. pp. 272–277.
External links
[edit]- Hepacivirin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
