Information on EC 3.4.22.B1 - vignain

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.22.B1
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
vignain
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hydrolysis of proteins, such as azocasein. Preferential cleavage: Asn-/-Xaa in small molecule substrates such as Boc-Asn-/-OPHNO2
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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-
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CAS REGISTRY NUMBER
COMMENTARY hide
149371-19-7
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229473-96-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Abz-(Xaa)n-Tyr(NO2)-Asp-OH + H2O
?
show the reaction diagram
-
-
-
?
azocasein + H2O
?
show the reaction diagram
beta-casein + H2O
?
show the reaction diagram
-
-
-
?
beta-conglycinin + H2O
?
show the reaction diagram
-
extensive hydrolysis
-
-
?
Boc-Asn-OPHNO2 + H2O
Boc-Asn + OPHNO2
show the reaction diagram
-
-
-
?
Bz-Asn-p-nitroanilide + H2O
p-nitroaniline + Bz-Asn
show the reaction diagram
Bz-Phe-Val-Arg-p-nitroanilide + H2O
p-nitroaniline + Bz-Phe-Val-Arg
show the reaction diagram
CBZ-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
phaseolin + H2O
?
show the reaction diagram
-
Cleavage of the phaseolin subunits into roughly half-sized fragments at the onset of proteolysis, only 8-10% decrease of protein
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-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
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the enzyme acts to degrade the seed storage protein in protein storage vacuoles
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
H-D-Val-Leu-Lys-chloromethylketone
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pepstatin A
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additional information
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not inhibited by EDTA
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
especially in the nitrogen fixing region
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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upon collapse of the nucellar cells, the content of the ricinosomes is released into the cytoplasm
Manually annotated by BRENDA team
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24930
LC-MS experiments, purified enzyme including the inhibitor H-D-Val-Leu-Lys-chloromethylketone
33000
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
at 2.0 A resolution and refined to a R-factor of 18.1%, vapor difussion method
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
20°C, pH 7.5, 2 hours
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
anion exchange chromatography, ultrafiltration
to homogeneity, gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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transgenic lines R108-1
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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a role of Cyp15a cysteine protease in germination and stress adaption and also in nodule organogenesis and function