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Information on EC 3.4.22.B1 - vignain and Organism(s) Ricinus communis and UniProt Accession O65039

for references in articles please use BRENDA:EC3.4.22.B1
preliminary BRENDA-supplied EC number
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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.B1 vignain
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This record set is specific for:
Ricinus communis
UNIPROT: O65039
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Word Map
The taxonomic range for the selected organisms is: Ricinus communis
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hydrolysis of proteins, such as azocasein. Preferential cleavage: Asn-/-Xaa in small molecule substrates such as Boc-Asn-/-OPHNO2
Synonyms
sh-ep, cyp15a, cysep, vmpe-1, cpph1, sulfhydryl-endopeptidase, vignain, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cysteine endopeptidase
-
Bean endopeptidase
-
-
-
-
C01.010
-
-
-
-
cysteine proteinase
-
-
-
-
SH-EP
-
-
-
-
sulfhydryl-endopeptidase
-
-
-
-
VmPE-1
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
149371-19-7
-
229473-96-5
-
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
-
-
-
?
beta-casein + H2O
?
show the reaction diagram
-
-
-
?
CBZ-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
H-D-Val-Leu-Lys-chloromethylketone
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
present in the seed coat during the final stages of sclerification but absent from the caruncle
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
upon collapse of the nucellar cells, the content of the ricinosomes is released into the cytoplasm
Manually annotated by BRENDA team
additional information
-
in ricinosomes, deriving from the endoplasmic reticulum, both pro CysEp and mature CysEp are present in protein extracts of the nucellar tissues during seed development
-
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CYSEP_RICCO
360
0
40111
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24930
LC-MS experiments, purified enzyme including the inhibitor H-D-Val-Leu-Lys-chloromethylketone
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
to homogeneity, gel filtration
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Than, M.E.; Helm, M.; Simpson, D.J.; Lottspeich, F.; Huber, R.; Gietl, C.
The 2.0 A crystal structure and substrate specificity of the KDEL-tailed cysteine endopeptidase functioning in programmed cell death of Ricinus communis endosperm
J. Mol. Biol.
336
1103-1116
2004
Ricinus communis (O65039), Ricinus communis
Manually annotated by BRENDA team
Greenwood, J.S.; Helm, M.; Gietl, C.
Ricinosomes and endosperm transfer cell structure in programmed cell death of the nucellus during Ricinus seed development
Proc. Natl. Acad. Sci. USA
102
2238-2243
2005
Ricinus communis
Manually annotated by BRENDA team