KEGG   ENZYME: 3.4.22.66Help
Entry
EC 3.4.22.66                Enzyme                                 

Name
calicivirin;
Camberwell virus processing peptidase;
Chiba virus processing peptidase;
Norwalk virus processing peptidase;
Southampton virus processing peptidase;
Southampton virus;
norovirus virus processing peptidase;
calicivirus trypsin-like cysteine protease;
calicivirus TCP;
calicivirus 3C-like protease;
calicivirus endopeptidase;
rabbit hemorrhagic disease virus 3C endopeptidase
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Cysteine endopeptidases
BRITE hierarchy
Reaction(IUBMB)
Endopeptidase with a preference for cleavage when the P1 position is occupied by Glu! and the P1' position is occupied by Gly!
Comment
Viruses that are members of the Norovirus genus (Caliciviridae family) are a major cause of epidemic acute viral gastroenteritis [4]. The nonstructural proteins of these viruses are produced by proteolytic cleavage of a large precursor polyprotein, performed by a protease that is incorporated into the polyprotein [6]. Cleavage sites are apparently defined by features based on both sequence and structure since several sites in the polyprotein fulfilling the identified sequence requirements are not cleaved [1]. The presence of acidic (Asp), basic (Arg), aromatic (Tyr) or aliphatic (Leu) amino acids at the P1' position results in only minor differences in cleavage efficiency, suggesting that steric or conformational constraints may play a role in determining specificity [1]. Changes to the amino acid at the P2 position do not alter cleavage efficiency [1,2]. Belongs in peptidase family C37.
History
EC 3.4.22.66 created 2007
Reference
1
  Authors
Meyers, G., Rossi, C. and Thiel, H.J.
  Title
Calicivirus endopeptidases.
  Journal
In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.), Handbook of Proteolytic Enzymes, 2nd ed., Elsevier, London, 2004, p. 1380-1382.
Reference
2  [PMID:7474137]
  Authors
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
J. Virol. 69 (1995) 7159-68.
  Organism
Rabbit hemorrhagic disease virus
  Sequence
[up:P27410]
Reference
3  [PMID:8551592]
  Authors
Martin Alonso JM, Casais R, Boga JA, Parra F.
  Title
Processing of rabbit hemorrhagic disease virus polyprotein.
  Journal
J. Virol. 70 (1996) 1261-5.
  Organism
Rabbit hemorrhagic disease virus
  Sequence
[up:Q86119]
Reference
4  [PMID:8642693]
  Authors
Liu B, Clarke IN, Lambden PR.
  Title
Polyprotein processing in Southampton virus: identification of 3C-like protease cleavage sites by in vitro mutagenesis.
  Journal
J. Virol. 70 (1996) 2605-10.
Reference
5  [PMID:10073687]
  Authors
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
J. Gen. Virol. 80 ( Pt 2) (1999) 291-6.
  Organism
Southampton virus
  Sequence
[up:Q04544]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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