Information on EC 3.4.22.50 - V-cath endopeptidase

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The enzyme appears in viruses and cellular organisms

top print hide
EC NUMBER
COMMENTARY hide
3.4.22.50
-
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RECOMMENDED NAME
GeneOntology No.
V-cath endopeptidase
-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
endopeptidase of broad specificity, hydrolyzing substrates of both cathepsin L and cathepsin B
show the reaction diagram
-
-
-
-
top print hide
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
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top print hide
CAS REGISTRY NUMBER
COMMENTARY hide
316365-69-2
-
9001-92-7
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
azocasein + H2O
?
show the reaction diagram
Azocoll + H2O
?
show the reaction diagram
N-benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
N-benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
N-benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
N-benzyloxycarbonyl-Val-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-Val-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
N-benzyloxycarbonyl-Val-Val-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-Val-Val-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
top print hide
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
antipain
0.00005 mM, complete inhibition
chicken cystatin
0.0001 mM, complete inhibition
-
iodoacetate
0.05 mM, 80% inhibition
leupeptin
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
-
10 microM
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Autographa californica multiple nucleopolyhedrovirus chitinase
-
a proposed folding chaperone for the progenitor of V-CATH
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003
Z-Arg-Arg-7-amido-4-methylcoumarin
-
0.022
Z-Leu-Arg 7-amido-4-methylcoumarin
-
0.039
Z-Phe-Arg 7-amido-4-methylcoumarin
-
0.043
Z-Val-Arg-7-amido-4-methylcoumarin
-
0.058
Z-Val-Val-Arg 7-amido-4-methylcoumarin
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.73
Z-Arg-Arg-7-amido-4-methylcoumarin
-
0.73
Z-Leu-Arg 7-amido-4-methylcoumarin
-
0.95
Z-Phe-Arg 7-amido-4-methylcoumarin
-
0.94
Z-Val-Arg-7-amido-4-methylcoumarin
-
0.51
Z-Val-Val-Arg 7-amido-4-methylcoumarin
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 5.5
bell-shaped profile, hydrolysis of Z-Phe-Arg-7-amino-4-methylcoumarin and Z-Arg-Arg-7-amino-4-methylcoumarin
top print hide
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37000
x * 37000, deduced from nucleotide sequence
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
N-glycosylation may occur at Asn158
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Anticarsia gemmatalis multiple nucleopolyhedrovirus isolate 2D
expression in Escherichia coli
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
the introduction of the v-cath gene into the genome of Anticarsia gemmatalis multiple nucleopolyhedrovirus improves its insecticidal activity against Anticarsia gemmatalis larvae
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
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LINKS TO OTHER DATABASES (specific for EC-Number 3.4.22.50)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)