Information on EC 3.4.22.50 - V-cath endopeptidase

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The expected taxonomic range for this enzyme is: Baculoviridae

SplaateEC_Number,Commentary
EC NUMBER
COMMENTARY
3.4.22.50
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SplaateRecommended_Name,GO_Number
RECOMMENDED NAME
GeneOntology No.
V-cath endopeptidase
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SplaateReaction,Reaction_id,Commentary,IF(Commentary != '',Organism,'') ,IF(Commentary != '',Literature,'')
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
endopeptidase of broad specificity, hydrolyzing substrates of both cathepsin L and cathepsin B
show the reaction diagram
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-
-
-
SplaateReaction_Type,Organism,Commentary,Literature
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
SplaatePathway,BRENDA_Link,KEGG_Link,MetaCyc_Link,Source_Database
SplaateSystematic_Name,Commentary_IUBMB
SplaateSynonyms,Organism,Commentary,Literature
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
AcNPV protease
-
-
-
-
baculovirus cathepsin
-
-
-
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BmNPV protease
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-
-
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cathepsin
Cydia pomonella granulovirus CpGV-M1
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-
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NPV protease
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-
-
-
nucleopolyhedrosis virus protease
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-
-
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V-cath
Cydia pomonella granulovirus CpGV-M1
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-
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viral cathepsin
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-
-
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viral cysteine protease
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-
viral cysteine protease
Cydia pomonella granulovirus CpGV-M1
-
-
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SplaateCAS_Registry_Number,Commentary
CAS REGISTRY NUMBER
COMMENTARY
316365-69-2
-
9001-92-7
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SplaateOrganism, Commentary,Literature, Sequence_Code,Sequence_db,Textmining
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
in conjunction with chitinase, the enzyme promotes liquefaction of the host in the latter stages of infection
SwissProt
Manually annotated by BRENDA team
baculovirus, enzyme may aid in the degradation of host proteins as a source of amino acids for viral protein production
SwissProt
Manually annotated by BRENDA team
Cydia pomonella granulovirus CpGV-M1
CpGV-M1
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-
Manually annotated by BRENDA team
SplaateGeneral_Information, Organism, Commentary, Literature
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
the absence of v-cathepsin results in poor melanization and liquefaction of Cydia pomonella larvae
physiological function
-
v-cathepsin is involved in the degradation of larval tissues of Cydia pomonella
SplaateSubstrates,Products,id,Organism_Substrates,Commentary_Substrates, Literature_Substrates, Commentary_Products, Literature_Products,Reversibility
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Azocoll + H2O
?
show the reaction diagram
Cydia pomonella granulovirus, Cydia pomonella granulovirus CpGV-M1
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-
-
-
?
N-benzyloxycarbonyl-Arg-Arg-7-amino-4-methylcoumarin + H2O
?
show the reaction diagram
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-
-
?
N-benzyloxycarbonyl-Leu-Arg-7-amino-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
N-benzyloxycarbonyl-Phe-Arg-7-amino-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
N-benzyloxycarbonyl-Val-Arg-7-amino-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
N-benzyloxycarbonyl-Val-Val-Arg-7-amino-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
SplaateNatural_Substrates,Natural_Products,id,Organism_Substrates,Commentary_Substrates,Literature_Substrates,Commentary_Products,Literature_Products,Reversibility
SplaateCofactor,Organism,Commentary,Literature,Filename
SplaateMetals_Ions,Organism,Commentary, Literature
SplaateInhibitors, Organism, Commentary, Literature,Filename
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
antipain
0.00005 mM, complete inhibition
chicken cystatin
0.0001 mM, complete inhibition
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E64
cysteine protease specific inhibitor
E64
0.0001 mM, complete inhibition
iodoacetate
0.05 mM, 80% inhibition
Leupeptin
0.00005 mM, complete inhibition
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
-
10 microM
SplaateActivating_Compound, Organism, Commentary, Literature,Filename
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Autographa californica multiple nucleopolyhedrovirus chitinase
-
a proposed folding chaperone for the progenitor of V-CATH
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SplaateKM_Value,KM_Value_Maximum, Substrate,Organism, Commentary, Literature, Filename
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.003
Z-Arg-Arg-7-amido-4-methylcoumarin
-
0.022
Z-Leu-Arg-7-amino-4-methylcoumarin
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0.039
Z-Phe-Arg-7-amino-4-methylcoumarin
-
0.043
Z-Val-Arg-7-amino-4-methylcoumarin
-
0.058
Z-Val-Val-Arg-7-amino-4-methylcoumarin
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SplaateTurnover_Number, Turnover_Number_Maximum, Substrate,Organism,Commentary, Literature, Filename
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.73
Z-Arg-Arg-7-amido-4-methylcoumarin
Autographa californica nucleopolyhedrovirus
P25783
-
0.73
Z-Leu-Arg-7-amino-4-methylcoumarin
Autographa californica nucleopolyhedrovirus
P25783
-
0.95
Z-Phe-Arg-7-amino-4-methylcoumarin
Autographa californica nucleopolyhedrovirus
P25783
-
0.94
Z-Val-Arg-7-amino-4-methylcoumarin
Autographa californica nucleopolyhedrovirus
P25783
-
0.51
Z-Val-Val-Arg-7-amino-4-methylcoumarin
Autographa californica nucleopolyhedrovirus
P25783
-
SplaateKCat_KM_Value,KCat_KM_Value_Maximum, Substrate,Organism, Commentary, Literature, Filename
SplaateKI_Value,KI_Value_Maximum, Inhibitor,Organism, Commentary, Literature, Filename
SplaateIC50_Value,IC50_Value_Maximum, Inhibitor,Organism, Commentary, Literature, Filename
SplaateSpecific_Activity, Specific_Activity_Maximum, Organism ,Commentary, Literature
SplaatepH_Optimum, pH_Optimum_Maximum, Organism, Commentary, Literature
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 5.5
bell-shaped profile, hydrolysis of Z-Phe-Arg-7-amino-4-methylcoumarin and Z-Arg-Arg-7-amino-4-methylcoumarin
SplaatepH_Range,pH_Range_Maximum, Organism,Commentary, Literature
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 7.5
hydrolysis of Z-Phe-Arg-7-amino-4-methylcoumarin
4 - 7.5
hydrolysis of Z-Arg-Arg-7-amino-4-methylcoumarin
SplaateTemperature_Optimum, Temperature_Optimum_Maximum, Organism, Commentary, Literature
SplaateTemperature_Range, Temperature_Range_Maximum, Organism, Commentary, Literature
SplaatepI_Value,pI_Value_Maximum, Organism,Commentary, Literature
SplaateSource_Tissue, Organism, Commentary, Literature, Textmining
SplaateLocalization, Organism, Commentary, id_go, Literature, Textmining
SplaatePDB,PDB,PDB,Organism,Uniprot_ID
SplaateMolecular_Weight, Molecular_Weight_Maximum, Organism, Commentary, Literature
SplaateSubunits, Organism, Commentary, Literature
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 27500, 35500 Da and 32000 Da species are probaly precursors of the mature enzyme, immunoblot; x * 37000, deduced from nucleotide sequence
?
x * 27500, mature enzyme, calculated from amino acid sequence
SplaatePosttranslational_Modification, Organism, Commentary, Literature
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
N-glycosylation may occur at Asn158
SplaateCommentary, Organism, Literature
SplaatepH_Stability,pH_Stability_Maximum, Organism, Commentary, Literature
SplaateTemperature_Stability,Temperature_Stability_Maximum, Organism, Commentary, Literature
SplaateGeneral_Stability, Organism, Literature
SplaateOrganic_Solvent, Organism, Commentary, Literature
SplaateOxidation_Stability,Organism,Literature
SplaateStorage_Stability, Organism, Literature
SplaateCommentary, Organism, Literature
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
SplaateCommentary, Organism, Literature
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Anticarsia gemmatalis multiple nucleopolyhedrovirus isolate 2D
expression in Escherichia coli
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SplaateCommentary, Organism, Literature
SplaateEngineering, Organism, Commentary, Literature
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
in this study a cysteine protease-deleted Bombyx mori multiple nucleopolyhedrovirus (CPD-BmMNPV) bacmid using the lambda recombination system is constructed. The protease activities of Bombyx mori cells and silkworm larvae infected with this CPD-BmMNPV bacmid are reduced by 94% and 85%, respectively. By using this system, a GFP(uv)-beta1,3-N-acetylglucosaminyltransferase 2 (GFP(uv)-beta3GnT2) fusion protein is successfully expressed in silkworm larvae with less protein degradation and without larvae liquefaction
additional information
-
v-cath-deletion mutant, chloramphenicol acetyl transferase gene replaced the cathepsin gene
additional information
Cydia pomonella granulovirus CpGV-M1
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v-cath-deletion mutant, chloramphenicol acetyl transferase gene replaced the cathepsin gene
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SplaateCommentary, Organism, Literature
SplaateApplication,Organism,Commentary,Literature
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
this CPD-BmMNPV bacmid system provides rapid protein production in silkworms and can be used for the production of recombinant eukaryotic proteins without proteolytic degradation
agriculture
the introduction of the v-cath gene into the genome of Anticarsia gemmatalis multiple nucleopolyhedrovirus improves its insecticidal activity against Anticarsia gemmatalis larvae