KEGG   ENZYME: 3.4.22.50Help
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
BRITE hierarchy
Reaction(IUBMB)
Endopeptidase of broad specificity, hydrolyzing 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
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) (1995) 1091-8.
  Sequence
[up:P25783]
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 (1997) 243-53.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
316365-69-2

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