KEGG   ENZYME: 3.4.22.50
Entry
EC 3.4.22.50                Enzyme                                 
Name
V-cath endopeptidase;
AcNPV protease;
BmNPV protease;
NPV protease;
baculovirus cathepsin;
nucleopolyhedrosis virus protease;
viral cathepsin
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Cysteine endopeptidases
Reaction(IUBMB)
Endopeptidase of broad specificity, hydrolysing substrates of both cathepsin L and cathepsin B
Comment
In peptidase family C1. Contributes to the liquefaction of the tissues of the insect host in the late stages of infection by the baculovirus.
History
EC 3.4.22.50 created 2003
Orthology
K20741  Baculoviridae V-cath endopeptidase
Reference
1  [PMID:7730794]
  Authors
Slack JM, Kuzio J, Faulkner P
  Title
Characterization of v-cath, a cathepsin L-like proteinase expressed by the baculovirus Autographa californica multiple nuclear polyhedrosis virus.
  Journal
J Gen Virol 76 ( Pt 5):1091-8 (1995)
DOI:10.1099/0022-1317-76-5-1091
  Sequence
[vg:1403960]
Reference
2  [PMID:9400597]
  Authors
Hawtin RE, Zarkowska T, Arnold K, Thomas CJ, Gooday GW, King LA, Kuzio JA, Possee RD.
  Title
Liquefaction of Autographa californica nucleopolyhedrovirus-infected insects is dependent on the integrity of virus-encoded chitinase and cathepsin genes.
  Journal
Virology 238:243-53 (1997)
DOI:10.1006/viro.1997.8816
Other DBs
ExplorEnz - The Enzyme Database: 3.4.22.50
IUBMB Enzyme Nomenclature: 3.4.22.50
ExPASy - ENZYME nomenclature database: 3.4.22.50
BRENDA, the Enzyme Database: 3.4.22.50
CAS: 316365-69-2

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Gene (74)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (73)   
Protein sequence (170)   
   UniProt (146)   
   SWISS-PROT (18)   
   RefSeq(pep) (6)   
DNA sequence (66)   
   RefSeq(nuc) (12)   
   GenBank (30)   
   EMBL (24)   
Protein domain (8)   
   InterPro (8)   
All databases (318)   

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