# Calicivirin

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{{Short description|Enzyme}}
{{Infobox enzyme
| Name       = Calicivirin
| EC_number  = 3.4.22.66
| CAS_number =
| GO_code    = 
| image      = 
| width      = 
| caption    =  
}}
'''Calicivirin''' ({{EC number|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](/source/enzyme).<ref>{{cite book | chapter = Calicivirus endopeptidases | title = Handbook of Proteolytic Enzymes | vauthors = Meyers G, Rossi C, Thiel HJ |year = 2004 |pages = 1380–1382 | veditors = Barrett AJ, Rawlings ND, Woessner JF |edition  = 2nd |publisher = Elsevier |location = London }}</ref><ref>{{cite journal | vauthors = Wirblich C, Sibilia M, Boniotti MB, Rossi C, Thiel HJ, Meyers G | title = 3C-like protease of rabbit hemorrhagic disease virus: identification of cleavage sites in the ORF1 polyprotein and analysis of cleavage specificity | journal = Journal of Virology | volume = 69 | issue = 11 | pages = 7159–68 | date = November 1995 | doi = 10.1128/jvi.69.11.7159-7168.1995 | pmid = 7474137 | pmc = 189637 }}</ref><ref>{{cite journal | vauthors = Martín Alonso JM, Casais R, Boga JA, Parra F | title = Processing of rabbit hemorrhagic disease virus polyprotein | journal = Journal of Virology | volume = 70 | issue = 2 | pages = 1261–5 | date = February 1996 | doi = 10.1128/jvi.70.2.1261-1265.1996 | pmid = 8551592 | pmc = 189940 }}</ref><ref>{{cite journal | vauthors = Liu B, Clarke IN, Lambden PR | title = Polyprotein processing in Southampton virus: identification of 3C-like protease cleavage sites by in vitro mutagenesis | journal = Journal of Virology | volume = 70 | issue = 4 | pages = 2605–10 | date = April 1996 | doi = 10.1128/jvi.70.4.2605-2610.1996 | pmid = 8642693 | pmc = 190109 }}</ref><ref>{{cite journal | vauthors = Liu BL, Viljoen GJ, Clarke IN, Lambden PR | title = Identification of further proteolytic cleavage sites in the Southampton calicivirus polyprotein by expression of the viral protease in E. coli | journal = The Journal of General Virology | volume = 80 ( Pt 2) | issue = 2 | pages = 291–6 | date = February 1999 | pmid = 10073687 | doi = 10.1099/0022-1317-80-2-291 | doi-access = free }}</ref> This enzyme [catalyses](/source/catalysis) the following [chemical reaction](/source/chemical_reaction)

: [Endopeptidase](/source/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](/source/Norovirus) (family ''[Caliciviridae](/source/Caliciviridae)'') are a major cause of epidemic [acute viral gastroenteritis](/source/acute_viral_gastroenteritis).

== References ==
{{reflist}}

== External links ==
* {{MeshName|Calicivirin}}

{{Cysteine proteases}}
{{Enzymes}}
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Category:EC 3.4.22

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