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 genus Norovirus (family Caliciviridae) are a major cause of epidemic acute viral gastroenteritis.

References

^ Meyers G, Rossi C, Thiel HJ (2004). "Calicivirus endopeptidases". In Barrett AJ, Rawlings ND, Woessner JF (eds.). Handbook of Proteolytic Enzymes (2nd ed.). London: Elsevier. pp. 1380–1382.
^ Wirblich C, Sibilia M, Boniotti MB, Rossi C, Thiel HJ, Meyers G (November 1995). "3C-like protease of rabbit hemorrhagic disease virus: identification of cleavage sites in the ORF1 polyprotein and analysis of cleavage specificity". Journal of Virology. 69 (11): 7159–68. PMC 189637. PMID 7474137.
^ Martín Alonso JM, Casais R, Boga JA, Parra F (February 1996). "Processing of rabbit hemorrhagic disease virus polyprotein". Journal of Virology. 70 (2): 1261–5. PMC 189940. PMID 8551592.
^ Liu B, Clarke IN, Lambden PR (April 1996). "Polyprotein processing in Southampton virus: identification of 3C-like protease cleavage sites by in vitro mutagenesis". Journal of Virology. 70 (4): 2605–10. PMC 190109. PMID 8642693.
^ Liu BL, Viljoen GJ, Clarke IN, Lambden PR (February 1999). "Identification of further proteolytic cleavage sites in the Southampton calicivirus polyprotein by expression of the viral protease in E. coli". The Journal of General Virology. 80 ( Pt 2) (2): 291–6. doi:10.1099/0022-1317-80-2-291. PMID 10073687.

External links

Calicivirin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

v t e Proteases: cysteine proteases (EC 3.4.22)
Caspase	Caspase 1 Caspase 2 Caspase 3 Caspase 4 Caspase 5 Caspase 6 Caspase 7 Caspase 8 Caspase 9 Caspase 10 Caspase 12 Caspase 13 Caspase 14
Fruit-derived	Papain Ficain Bromelain Actinidain
Calpain	CAPN1 CAPN2 CAPN3 CAPN5 CAPN6 CAPN7 CAPN8 CAPN9 CAPN10 CAPN11 CAPN12 CAPN13 CAPN14 CAPNS1 CAPNS2
Cathepsin	B C F H K L1/L2 O S W Z
Other	Clostripain Cancer procoagulant Separase Autophagin Cruzipain 3C-like protease Gingipain R Gingipain K

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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