Hepacivirin

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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
PMC
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PMC	articles
PubMed	articles
NCBI	proteins

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.

^ 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.

[1] 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.

[2] 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.

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