Calicivirin
Calicivirin (EC 3.4.22.66, Camberwell virus processing peptidase, Chiba virus processing peptidase, Norwalk virus processing peptidase, Southampton virus processing peptidase, norovirus virus processing peptidase, calicivirus trypsin-like cysteine protease, calicivirus TCP, calicivirus 3C-like protease, calicivirus endopeptidase, rabbit hemorrhagic disease virus 3C endopeptidase) is an enzyme.[1][2][3][4][5] This enzyme catalyses the following chemical reaction
- Endopeptidase with a preference for cleavage when the P1 position is occupied by Glu- and the P1- position is occupied by Gly-
Viruses that are members of the Norovirus genus (Caliciviridae family) are a major cause of epidemic acute viral gastroenteritis.
References
- ↑ Meyers, G., Rossi, C. and Thiel, H.J. (2004). "Calicivirus endopeptidases". In Barrett, A.J., Rawlings, N.D. and Woessner, J.F. Handbook of Proteolytic Enzymes (2nd ed.). London: Elsevier. pp. 1380–1382.
- ↑ Wirblich, C., Sibilia, M., Boniotti, M.B., Rossi, C., Thiel, H.J. and Meyers, G. (1995). "3C-like protease of rabbit hemorrhagic disease virus: identification of cleavage sites in the ORF1 polyprotein and analysis of cleavage specificity". J. Virol. 69: 7159–7168. PMID 7474137.
- ↑ Martín Alonso, J.M., Casais, R., Boga, J.A. and Parra, F. (1996). "Processing of rabbit hemorrhagic disease virus polyprotein". J. Virol. 70: 1261–1265. PMID 8551592.
- ↑ Liu, B., Clarke, I.N. and Lambden, P.R. (1996). "Polyprotein processing in Southampton virus: identification of 3C-like protease cleavage sites by in vitro mutagenesis". J. Virol. 70: 2605–2610. PMID 8642693.
- ↑ Liu, B.L., Viljoen, G.J., Clarke, I.N. and Lambden, P.R. (1999). "Identification of further proteolytic cleavage sites in the Southampton calicivirus polyprotein by expression of the viral protease in E. coli". J. Gen. Virol. 80: 291–296. PMID 10073687.
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