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Information on EC 3.2.2.22 - rRNA N-glycosylase and Organism(s) Ricinus communis and UniProt Accession P02879

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EC Tree
     3 Hydrolases
         3.2 Glycosylases
             3.2.2 Hydrolysing N-glycosyl compounds
                3.2.2.22 rRNA N-glycosylase
IUBMB Comments
Ricin A-chain and related toxins show this activity. Naked rRNA is attacked more slowly than rRNA in intact ribosomes. Naked rRNA from Escherichia coli is cleaved at a corresponding position.
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This record set is specific for:
Ricinus communis
UNIPROT: P02879
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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
Synonyms
pd-l1, ricin, shiga toxin, saporin, abrin, ricinus communis agglutinin, gelonin, ricin a chain, trichosanthin, ribosome-inactivating proteins, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cytotoxic ribosome-inactivating lectin
-
depurinating rRNA N-glycosidase
-
polynucleotide:adenosine glycosidase
-
ribosome-inactivating protein
-
ricin A chain
-
Ricinus communis agglutinin
-
type II ribosome-inactivating protein
-
gelonin
-
-
-
-
Mirabilis antiviral protein
-
-
-
-
momorcochin-S
-
-
-
-
N-glycosidase
-
-
nigrin b
-
-
-
-
ribosomal ribonucleate N-glycosidase
-
-
-
-
ribosome inactivating protein
-
-
ribosome-inactivating protein
-
-
ribosome-inactivating protein type II
-
-
ribosome-inactivating proteins
-
-
ricin
ricin A chain
-
-
ricin toxin A-chain
-
-
ricin-A-chain
-
-
ricin-like protein
-
-
Ricinus communis agglutinin II
-
-
RNA N-glycosidase
rRNA N-glycosidase
-
-
-
-
saporins
-
-
-
-
type 2 ribosome inactivating protein
-
-
type 2 RIP
-
-
type II ribosome-inactivating protein
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hydrolysis of the N-glycosylic bond at A-4324 in 28S rRNA from rat ribosomes
show the reaction diagram
catalytic mechanism
hydrolysis of the N-glycosylic bond at A-4324 in 28S rRNA from rat ribosomes
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis
hydrolysis of N-glycosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
rRNA N-glycohydrolase
Ricin A-chain and related toxins show this activity. Naked rRNA is attacked more slowly than rRNA in intact ribosomes. Naked rRNA from Escherichia coli is cleaved at a corresponding position.
CAS REGISTRY NUMBER
COMMENTARY hide
113756-12-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
23S rRNA + H2O
?
show the reaction diagram
substrate is from Escherichia coli ribosomes, the naked 23S rRNA is a good substrate, while the intact native ribosome ins no substrate
-
-
?
28S rRNA + H2O
28S rRNA fragment + ?
show the reaction diagram
depurination or 28S rRNA, removal of adenine from rRNA, inactivating ribosomal function in translation
-
-
?
28S rRNA + H2O
?
show the reaction diagram
substrate is from rat liver ribosomes, depurination of A4324 of rat 28S rRNA, generation of an R-fragment from 28S RNA, the enzyme prefers the native ribosome to the naked 28S rRNA, the toxin recognizes the sarcin-ricin domain, structure overview
-
-
?
28S rRNA within the native ribosome + H2O
?
show the reaction diagram
-
-
-
?
DNA + H2O
?
show the reaction diagram
primarily DNA substrate, polynucleotide:adenosine glycosidase activity
-
-
?
naked 28S rRNA + H2O
?
show the reaction diagram
-
-
-
?
naked rRNA + H2O
?
show the reaction diagram
primarily DNA substrate, polynucleotide:adenosine glycosidase activity
-
-
?
polyA + H2O
?
show the reaction diagram
primarily DNA substrate, polynucleotide:adenosine glycosidase activity
-
-
?
rRNA + H2O
?
show the reaction diagram
14-mer rRNA with GAGA tetraloop + H2O
14-mer rRNA with GabGA + ?
show the reaction diagram
-
substrate and product with specific DNA loop probe, fluorophore and quencher, 37°C, citrate buffer, pH 4.0, than neutralization to pH 7.6 and hybridization with DNA-probes
-
-
?
26S rRNA + H2O
?
show the reaction diagram
-
depurination of ribosomes from yeast, product determination using aniline coupling
-
-
?
28S rRNA + H2O
?
show the reaction diagram
28S rRNA + H2O
apurinic 28S rRNA + adenine
show the reaction diagram
-
depurination of a specific adenine in 28S rRNA
-
-
?
5'-dG1dC2dG3dC4dG5A6dG7dA8dG9dC10dG11dC12-3' + H2O
?
show the reaction diagram
-
GAGA stem-loop RNA-DNA hybrid substrate, analysis of activity with substrate derivative possessing variations in the tetraloop G5-A8, overview
-
-
?
5'-dG1dC2dG3dC4dG5dA6dG7A8dG9dC10dG11dC12-3' + H2O
?
show the reaction diagram
-
GAGA stem-loop RNA-DNA hybrid substrate, analysis of activity with substrate derivative possessing variations in the tetraloop G5-A8, overview
-
-
?
5'-dG1dC2dG3dC4dG5dA6G7dA8dG9dC10dG11dC12-3' + H2O
?
show the reaction diagram
-
GAGA stem-loop RNA-DNA hybrid substrate, analysis of activity with substrate derivative possessing variations in the tetraloop G5-A8, overview
-
-
?
5'-dG1dC2dG3dC4G5dA6dG7dA8dG9dC10dG11dC12-3' + H2O
?
show the reaction diagram
-
GAGA stem-loop RNA-DNA hybrid substrate, analysis of activity with substrate derivative possessing variations in the tetraloop G5-A8, overview
-
-
?
5'-G1C2G3C4dG5A6dG7A8G9C10G11C12-3' + H2O
?
show the reaction diagram
-
GAGA stem-loop RNA-DNA hybrid substrate, analysis of activity with substrate derivative possessing variations in the tetraloop G5-A8, overview
-
-
?
5'-G1C2G3C4dG5A6G7A8G9C10G11C12-3' + H2O
?
show the reaction diagram
-
GAGA stem-loop RNA-DNA hybrid substrate, analysis of activity with substrate derivative possessing variations in the tetraloop G5-A8, overview
-
-
?
5'-G1C2G3C4dG5A6G7dA8G9C10G11C12-3' + H2O
?
show the reaction diagram
-
GAGA stem-loop RNA-DNA hybrid substrate, analysis of activity with substrate derivative possessing variations in the tetraloop G5-A8, overview
-
-
?
5'-G1C2G3C4G5A6dG7A8G9C10G11C12-3' + H2O
?
show the reaction diagram
-
GAGA stem-loop RNA-DNA hybrid substrate, analysis of activity with substrate derivative possessing variations in the tetraloop G5-A8, overview
-
-
?
5'-G1C2G3C4G5A6G7A8G9C10G11C12-3' + H2O
?
show the reaction diagram
-
GAGA stem-loop RNA substrate, analysis of activity with substrate derivative possessing variations in the tetraloop G5-A8, preferred substrates to DNA stem loop derivatives, overview
-
-
?
5'-G1C2G3C4G5A6G7dA8G9C10G11C12-3' + H2O
?
show the reaction diagram
-
GAGA stem-loop RNA-DNA hybrid substrate, analysis of activity with substrate derivative possessing variations in the tetraloop G5-A8, overview
-
-
?
5'-G1C2G3C4G5A6G7mA8G9C10G11C12-3' + H2O
?
show the reaction diagram
-
RNA-2'-methoxy nucleic acid hybrid stem-loop substrate
-
-
?
5'-G1C2G3C4G5A6mG7A8G9C10G11C12-3' + H2O
?
show the reaction diagram
-
RNA-2'-methoxy nucleic acid hybrid stem-loop substrate
-
-
?
5'-G1C2G3C4G5dA6G7A8G9C10G11C12-3' + H2O
?
show the reaction diagram
-
GAGA stem-loop RNA-DNA hybrid substrate, analysis of activity with substrate derivative possessing variations in the tetraloop G5-A8, overview
-
-
?
5'-G1C2G3C4G5mA6G7A8G9C10G11C12-3' + H2O
?
show the reaction diagram
-
RNA-2'-methoxy nucleic acid hybrid stem-loop substrate
-
-
?
5'-G1C2G3C4mG5A6G7A8G9C10G11C12-3' + H2O
?
show the reaction diagram
-
RNA-2'-methoxy nucleic acid hybrid stem-loop substrate
-
-
?
5'/biotin/AGCGGGAGAGdAAAUCUCCC + H2O
5'/biotin/AGCGGGAGAG + ?
show the reaction diagram
-
RNA GdAAA substrate hybridized with ruthenylated oligodeoxynucleotide 50/Ru/TTTTTdAdCdCTdCTdCTdCdGdCTdC to give a electrochemiluminescence signal
-
-
?
5'/biotin/AGCGGGAGAGdAGAUCUCCC + H2O
5'/biotin/AGCGGGAGAG + ?
show the reaction diagram
-
RNA GdAGA substrate hybridized with ruthenylated oligodeoxynucleotide 50/Ru/TTTTTdAdCdCTdCTdCTdCdGdCTdC to give a electrochemiluminescence signal
-
-
?
5'/biotin/AGCGGGAGAGdUGAUCUCCC + H2O
5'/biotin/AGCGGGAGAG + ?
show the reaction diagram
-
RNA GdUGA substrate hybridized with ruthenylated oligodeoxynucleotide 50/Ru/TTTTTdAdCdCTdCTdCTdCdGdCTdC to give a electrochemiluminescence signal to test for false positive signal
-
-
?
A-14 2-dA stem-loop RNA/DNA hybrid + H2O
?
show the reaction diagram
-
-
-
-
?
cyclic dG-(N-benzyl-aza-deoxyribosyl)-dGdA + H2O
?
show the reaction diagram
-
-
-
-
?
cyclic dGdAdGdA + H2O
?
show the reaction diagram
-
-
-
-
?
cyclic GdAGA + H2O
?
show the reaction diagram
-
-
-
-
?
cyclic phosphorothioyl dGdAdGdA + H2O
?
show the reaction diagram
-
ring closure via a phosphorothioate bond
-
-
?
dGdAdGdA + H2O
?
show the reaction diagram
-
-
-
-
?
dGdCdGdCdGdAdGdAdGdCdGdC + H2O
?
show the reaction diagram
-
-
-
-
?
GCGCGAGAGCGC + H2O
GCGCGGAGCGC + ?
show the reaction diagram
-
DNA substrate (100 pmol/microl) mimicking natural rRNA substrate, reaction buffer: 10 mM ammonium citrate with 1 mM ethylenediaminetetraacetic acid, pH 4, 37°C, 4 h
-
-
?
GdAGA + H2O
?
show the reaction diagram
large rRNA + H2O
?
show the reaction diagram
-
the enzyme highly inhibits protein synthesis by ribosome inactivation via depurination of rRNA at a specific site
-
-
?
rabbit reticulocyte 80S rRNA + H2O
?
show the reaction diagram
-
-
-
-
?
ribosomes + H2O
?
show the reaction diagram
-
substrate from yeast
-
-
?
rRNA + H2O
?
show the reaction diagram
sarcin/ricin domains of Escherichia coli 23S rRNA + H2O
?
show the reaction diagram
-
-
-
-
?
sarcin/ricin domains of Rattus norvegicus 28S rRNA + H2O
?
show the reaction diagram
-
-
-
-
?
stem-loop substrate A-10 + H2O
?
show the reaction diagram
-
-
-
-
?
yeast 60S rRNA + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
28S rRNA + H2O
28S rRNA fragment + ?
show the reaction diagram
depurination or 28S rRNA, removal of adenine from rRNA, inactivating ribosomal function in translation
-
-
?
rRNA + H2O
?
show the reaction diagram
-
-
-
?
28S rRNA + H2O
apurinic 28S rRNA + adenine
show the reaction diagram
-
depurination of a specific adenine in 28S rRNA
-
-
?
large rRNA + H2O
?
show the reaction diagram
-
the enzyme highly inhibits protein synthesis by ribosome inactivation via depurination of rRNA at a specific site
-
-
?
rRNA + H2O
?
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
activates
NH4+
activates
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
((5-(2-amino-4,6-dihydroxy-5-pyrimidinyl)pentanoyl)amino)acetic acid
-
(E)-3-(5-methylfuran-2-yl)-N-(1,2,3,4-tetrahydronaphthalen-1-yl)prop-2-enamide
CID 16271106, a group III compound, dose-dependent inhibition of ricin activity, mildly or moderately cytotoxic
2-amino-1,4-dihydro-6-hydroxy-4-oxo-5-pyrimidinepentanoic acid
-
2-amino-1,4-dihydro-6-hydroxy-4-oxo-a-phenyl-pyrimidinepentanoic acid
PPA
2-methylsulfonyl-1-(naphthalen-1-ylmethyl)benzimidazole
CID 18576762, a group III compound, dose-dependent inhibition of ricin activity, mildly or moderately cytotoxic
4,6-bis(propan-2-ylamino)-1,3,5-triazine-2-carbonitrile
CID 644401, a group III compound, dose-dependent inhibition of ricin activity, mildly or moderately cytotoxic
4-(3-(2-amino-1,4-dihydro-6-hydroxy-4-oxo-5-pyrimidinyl)propyl)-benzoic acid
PBA
8-vinyl-2'-deoxyadenosine containing 10-mer stem-tetraloop RNA
i.e. 8VdA-10, active site analogue, no substrate. Role of residue R180 in oxacarbenium ion destabilization, adenine is released from a second site within the molecule
9-deazaadenine-9-methylene-N-hydroxypyrrolidine
transition state analogue inhibitors contraining 9-deazaadenine-9-methylene-N-hydroxypyrrolidine. The tight-binding inhibitors mimic the sarcin-ricin recognition loop of 28S rRNA and the dissociative ribocation transition state established for RTA catalysis. RTA has a unique purine-binding geometry with quadruple pi-stacking interactions between adjacent adenine and guanine bases and 2 conserved tyrosines. An arginine at one end of the pi-stack provides cationic polarization and enhanced leaving group ability to the susceptible adenine. Inhibition mechanism, overview
brefeldin A
shows significant anti-ricin activity
gliotoxin
shows significant anti-ricin activity
methyl 2-[(5E)-5-[[5-(azepan-1-yl)furan-2-yl]methylidene]-2,4-dioxo-1,3-thiazolidin-3-yl]propanoate
CID 5737931, a group III compound, dose-dependent inhibition of ricin activity, mildly or moderately cytotoxic
milk
competitively inhibits the biological activity of 1 ng/ml ricin. Milk does not inhibit ricin at concentrations of 10 or 100 ng/ml
-
N-cyclohexyl-N-[(4-fluorophenyl)methyl]-2-(4H-1,2,4-triazol-3-ylsulfanyl)acetamide
CID 7531223
Thiostrepton
shows significant anti-ricin activity
TPCK
shows significant anti-ricin activity
2,2-dimethyl-4-[(E)-2-phenylethenyl]-2,3-dihydro-1H-1,5-benzodiazepine
-
-
2-(methylsulfonyl)-1-(naphthalen-1-ylmethyl)-1H-benzimidazole
-
-
2-amino-4-oxo-3,4-dihydro-pteridine 7-carbohydrazide
-
35% inhibition at 0.5 mM
2-[(E)-[(5-methylthiophen-2-yl)methylidene]amino]-N-phenylbenzamide
-
-
4,6-bis(propan-2-ylamino)-1,3,5-triazine-2-carbonitrile
-
-
4-bromo-2-[6-[(2,6-dimethylphenyl)amino]-3H-imidazo[1,2-b][1,2,4]triazol-5-yl]phenol
-
-
7-acetylpterin
-
20% inhibition at 0.5 mM
7-bromo-5-phenyl-4-propanoyl-1,3,4,5-tetrahydro-2H-1,4-benzodiazepin-2-one
-
-
7-carboxypterin
-
-
7-propionylpterin
-
-
beta-methyl galactoside
-
50% inhibition of ricin binding to immobilized asialofetuin in ELIZA-type assay at 1.78 mM, 50% inhibition in ricin cytotoxicity at 6.7 mM
beta-methyl lactoside
-
50% inhibition of ricin binding to immobilized asialofetuin in ELIZA-type assay at 0.55 mM, 50% inhibition in ricin cytotoxicity at 4.0 mM
brefeldin A
CGCG-(N-benzyl-aza-ribosyl)-GAGCG
-
-
cyclic dG-(N-benzyl-aza-deoxyribosyl)-dGd-N-benzyl-aza-deoxyribose
-
-
cyclic dG-(N-benzyl-aza-deoxyribosyl)-dGdA
-
-
cyclic G-(N-benzyl-aza-ribosyl)-GA
-
-
D-galactose
-
50% inhibition of ricin binding to immobilized asialofetuin in ELIZA-type assay at 1.39 mM, 50% inhibition in ricin cytotoxicity at 65 mM
dithiothreitol
-
20 mM, 74% residual activity
golgicide A
-
-
HCl
-
20 mM, 38% residual activity
ilimaquinone
-
-
KCl
-
20 mM, 79% residual activity
lactose
methyl 2-[(5E)-5-[[5-(azepan-1-yl)furan-2-yl]methylidene]-2,4-dioxo-1,3-thiazolidin-3-yl]propanoate
-
-
MgCl2
-
10 mM, 65% residual activity
N-(2-(phenylamino) ethyl)-7-carbamoylpterin
-
-
N-(4-fluorobenzyl)-7-carbamoylpterin
-
-
N-(furanylmethyl)-7-carbamoylpterin
-
-
N-(methylamino pyridinyl)-7-carbamoylpterin
-
-
N-methyl-7-carbamoylpterin
-
-
NaCl
-
20 mM, 90% residual activity
NaOH
-
20 mM, 41% residual activity
Triton X-100
-
inhibits at 0.1-0.5%
Tween-80
-
inhibits at 0.1-0.5%
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0026
28S rRNA within the native ribosome
-
-
0.0058
naked 28S rRNA
-
-
0.01
5'-dG1dC2dG3dC4dG5A6dG7dA8dG9dC10dG11dC12-3'
-
37°C
0.005
5'-dG1dC2dG3dC4dG5dA6dG7A8dG9dC10dG11dC12-3'
-
37°C
0.0152
5'-dG1dC2dG3dC4dG5dA6G7dA8dG9dC10dG11dC12-3'
-
37°C
0.0094
5'-dG1dC2dG3dC4G5dA6dG7dA8dG9dC10dG11dC12-3'
-
37°C
0.1
5'-G1C2G3C4dG5A6dG7A8G9C10G11C12-3'
-
37°C
0.0007
5'-G1C2G3C4dG5A6G7A8G9C10G11C12-3'
-
37°C
0.0018
5'-G1C2G3C4dG5A6G7dA8G9C10G11C12-3'
-
37°C
0.0009
5'-G1C2G3C4G5A6dG7A8G9C10G11C12-3'
-
37°C
0.0027
5'-G1C2G3C4G5A6G7A8G9C10G11C12-3'
-
37°C
0.0057
5'-G1C2G3C4G5A6G7dA8G9C10G11C12-3'
-
37°C
0.0097
5'-G1C2G3C4G5A6G7mA8G9C10G11C12-3'
-
37°C
0.0063
5'-G1C2G3C4G5A6mG7A8G9C10G11C12-3'
-
37°C
0.032
5'-G1C2G3C4G5dA6G7A8G9C10G11C12-3'
-
37°C
0.3
5'-G1C2G3C4G5mA6G7A8G9C10G11C12-3'
-
37°C
0.0029
5'-G1C2G3C4mG5A6G7A8G9C10G11C12-3'
-
37°C
0.0103
A-14 2-dA stem-loop RNA/DNA hybrid
-
pH 4.0
-
0.039
cyclic dG-(N-benzyl-aza-deoxyribosyl)-dGdA
-
pH 4.0, 37°C
0.097
cyclic dGdAdGdA
-
pH 4.0, 37°C
0.038
cyclic GdAGA
-
pH 4.0, 37°C
0.046
cyclic phosphorothioyl dGdAdGdA
-
pH 4.0, 37°C
0.112
dGdAdGdA
-
pH 4.0, 37°C
0.0084
dGdCdGdCdGdAdGdAdGdCdGdC
-
pH 4.0, 37°C
0.065
GdAGA
-
pH 4.0, 37°C
0.0001
rabbit reticulocyte 80S rRNA
-
pH 4.0
-
0.0026 - 0.0058
rRNA
0.00464
sarcin/ricin domains of Escherichia coli 23S rRNA
-
pH 5.0
-
0.00457
sarcin/ricin domains of Rattus norvegicus 28S rRNA
-
pH 5.0
-
0.0022
stem-loop substrate A-10
-
pH 4.0
-
0.00006
yeast 60S rRNA
-
pH 4.0
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0083
5'-dG1dC2dG3dC4dG5A6dG7dA8dG9dC10dG11dC12-3'
-
37°C
0.015
5'-dG1dC2dG3dC4dG5dA6dG7A8dG9dC10dG11dC12-3'
-
37°C
0.0015
5'-dG1dC2dG3dC4dG5dA6G7dA8dG9dC10dG11dC12-3'
-
37°C
0.0038
5'-dG1dC2dG3dC4G5dA6dG7dA8dG9dC10dG11dC12-3'
-
37°C
0.0007
5'-G1C2G3C4dG5A6dG7A8G9C10G11C12-3'
-
37°C
0.005
5'-G1C2G3C4dG5A6G7A8G9C10G11C12-3'
-
37°C
0.01
5'-G1C2G3C4dG5A6G7dA8G9C10G11C12-3'
-
37°C
0.011
5'-G1C2G3C4G5A6dG7A8G9C10G11C12-3'
-
37°C
1.68
5'-G1C2G3C4G5A6G7A8G9C10G11C12-3'
-
37°C
0.055
5'-G1C2G3C4G5A6G7dA8G9C10G11C12-3'
-
37°C
0.085
5'-G1C2G3C4G5A6G7mA8G9C10G11C12-3'
-
37°C
0.005
5'-G1C2G3C4G5A6mG7A8G9C10G11C12-3'
-
37°C
27.67
5'-G1C2G3C4G5dA6G7A8G9C10G11C12-3'
-
37°C
0.07
5'-G1C2G3C4G5mA6G7A8G9C10G11C12-3'
-
37°C
0.001
5'-G1C2G3C4mG5A6G7A8G9C10G11C12-3'
-
37°C
18.5
A-14 2-dA stem-loop RNA/DNA hybrid
-
pH 4.0
-
0.018
cyclic dG-(N-benzyl-aza-deoxyribosyl)-dGdA
-
pH 4.0, 37°C
0.108
cyclic dGdAdGdA
-
pH 4.0, 37°C
0.018
cyclic GdAGA
-
pH 4.0, 37°C
0.15
cyclic phosphorothioyl dGdAdGdA
-
pH 4.0, 37°C
0.0045
dGdAdGdA
-
pH 4.0, 37°C
0.0083
dGdCdGdCdGdAdGdAdGdCdGdC
-
pH 4.0, 37°C
0.003
GdAGA
-
pH 4.0, 37°C
0.000333 - 29.6
rRNA
0.0012
sarcin/ricin domains of Escherichia coli 23S rRNA
-
pH 5.0
-
0.0018
sarcin/ricin domains of Rattus norvegicus 28S rRNA
-
pH 5.0
-
0.078
stem-loop substrate A-10
-
pH 4.0
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
catalysis of 80S ribosome by RTA approaches the diffusion rate limit for enzymatic reactions
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0024
8-vinyl-2'-deoxyadenosine containing 10-mer stem-tetraloop RNA
37°C, pH 4.0
0.000099
CGCG-(N-benzyl-aza-ribosyl)-GAGCG
-
37°C, pH 4.0
0.0013
cyclic dG-(N-benzyl-aza-deoxyribosyl)-dGd-N-benzyl-aza-deoxyribose
-
37°C, pH 4.0
0.0027
cyclic dG-(N-benzyl-aza-deoxyribosyl)-dGdA
-
37°C, pH 4.0
0.00007
cyclic G-(N-benzyl-aza-ribosyl)-GA
-
37°C, pH 4.0
additional information
additional information
-
thermodynamics and kinetics of catayltic subunit inhibition with pyrrolidine mimics of the oxacarbenium ion transition state
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
((5-(2-amino-4,6-dihydroxy-5-pyrimidinyl)pentanoyl)amino)acetic acid
Ricinus communis
-
0.27
4-(3-(2-amino-1,4-dihydro-6-hydroxy-4-oxo-5-pyrimidinyl)propyl)-benzoic acid
Ricinus communis
30°C
0.25
N-cyclohexyl-N-[(4-fluorophenyl)methyl]-2-(4H-1,2,4-triazol-3-ylsulfanyl)acetamide
Ricinus communis
-
0.2
7-carboxypterin
Ricinus communis
-
in 100 mM HEPES pH 7.5, 125 mM NaCl, at 25°C
0.7
7-propionylpterin
Ricinus communis
-
in 100 mM HEPES pH 7.5, 125 mM NaCl, at 25°C
0.2
N-(2-(phenylamino) ethyl)-7-carbamoylpterin
Ricinus communis
-
in 100 mM HEPES pH 7.5, 125 mM NaCl, at 25°C
0.6
N-(4-fluorobenzyl)-7-carbamoylpterin
Ricinus communis
-
in 100 mM HEPES pH 7.5, 125 mM NaCl, at 25°C
0.4
N-(furanylmethyl)-7-carbamoylpterin
Ricinus communis
-
in 100 mM HEPES pH 7.5, 125 mM NaCl, at 25°C
0.5
N-(methylamino pyridinyl)-7-carbamoylpterin
Ricinus communis
-
in 100 mM HEPES pH 7.5, 125 mM NaCl, at 25°C
1.6
N-methyl-7-carbamoylpterin
Ricinus communis
-
in 100 mM HEPES pH 7.5, 125 mM NaCl, at 25°C
additional information
2-amino-1,4-dihydro-6-hydroxy-4-oxo-5-pyrimidinepentanoic acid
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
polynucleotide:adenosine glycosidase activity
7.8
type II ribosome-inactivating protein
5.6
-
assay at
7.6
-
assay at
8
-
assay at
additional information
-
pH-dependency with stem-loop and unstructured DNA substrates, overview
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 5
-
pH-dependence of the reaction, overview
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 35
-
assay at
48
-
optimal temperature of ricin activity at 1 ng/ml based on signal-to-background ratios, 1.8fold higher than at 37°C, and 1.2fold higher than at 57°C
55
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 80
-
activity range, profile, overview
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
accumulation in protein storage vacuoles
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
protein storage vacuole
Manually annotated by BRENDA team
-
stably membrane-bound at 37°C, even under sodium carbonate treatment at pH 11.5, extractable at 20°C
Manually annotated by BRENDA team
-
the enzyme enters target cells via its cell surface receptor
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
the enzyme causes inhibition of protein synthesis by loss of elongation factor binding resulting in cell death
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
RICI_RICCO
576
1
64091
Swiss-Prot
Secretory Pathway (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31200
C-terminal His-tag version
31600
N-terminal His-tag version
62925
x * 62925, MALDI-TOF
28000
-
x * 29000, A chain, + x * 28000, B chain, SDS-PAGE
29000
-
x * 29000, A chain, + x * 28000, B chain, SDS-PAGE
32000
-
x * 32000, SDS-PAGE
36000
-
x * 36000
62912
-
x * 62912, MALDI-TOF mass spectrometry
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 62925, MALDI-TOF
dimer
heterodimer, subunits A and B, RTA and RTB, are derived from a single precursor protein, structure comparison and analysis
dimer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
proteolytic modification
cleavage of the single precursor protein into subunit A and B
glycoprotein
-
-
proteolytic modification
-
removal of the signal peptide of ricin precursor generates proricin in which the mature A- and B-chains are joined by an intervening propeptide and a 9-residue propeptide persists at the N terminus. The N-terminal propeptide of proricin acts as a nonspecific spacer to ensure efficient ER import and glycosylation. The propeptide does not influence catalytic activity per se or the vacuolar targeting of proricin or the rate of retrotranslocation/degradation of A-chain in the cytosol
additional information
-
temperature induced major structural rearrangements of endoplasmic reticulum membrane-bound toxin at 37°C: loss of helical content, increase of beta sheets, C-terminus moves closer to membrane surface, insertion into the bilayer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
dynamics calculations suggest that steric factors cause the nucleoside to bind in an orientation where the enzyme destabilizes the formation of the oxacarbeniumion and thus precludes catalysis
RTA with 4-(3-(2-amino-4,6-dihydroxy-5-pyrimidinyl)propyl) benzoic acid
sitting drop vapor diffusion method, using 100 mM N,N-bis(2-hydroxyethyl)glycine (pH 8.5) and 20% (w/v) polyethylene glycol (PEG) 6000 (in complex with antigen binding domain E5 of single-chain monoclonal antibody) or 100 mM Na acetate (pH 4.5), 200 mM zinc acetate and 10% (w/v) PEG 3000 (in complex with antigen binding domain D10 of single-chain monoclonal antibody) or 100 mM Na-Hepes (pH 7.5) and 20% (w/v) PEG 8000 (in complex with antigen binding domain G12 of single-chain monoclonal antibody) or 100 mM Na acetate (pH 4.5), 200 mM NaCl and 40% (w/v) PEG 300 (in complex with antigen binding domain G11 of single-chain monoclonal antibody)
structure of ricin-A chain in a complex with the C-terminal domain of the human ribosomal protein P2. The Phe111, Leu113 and Phe114 residues of P2 insert into a hydrophobic pocket formed by the Tyr183, Arg235, Phe240 and Ile251 residues of ricin A-chain, while Asp115 of P2 forms hydrogen bonds with Arg235 of ricin A-chain. The interaction with P stalk proteins is essential for the inhibition of protein synthesis by ricin A-chain
the smallest ligand stabilizing an open conformer of the ricin A chain active site pocket is an amide group, bound weakly by only a few hydrogen bonds to the protein. Complexes with small amide-containing molecules also reveal a switch in geometry from a parallel towards a splayed arrangement of an arginine-tryptophan cation-pi interaction that was associated with an increase and redshift in tryptophan fluorescence upon ligand binding. Urea binding has a favorable enthalpy change and unfavorable entropy change. The side-chain position of residue >80 in a complex with adenine suggests a smaller role for aromatic stacking at the ricin active site
coarse-grained latice simulation model of sequence-structure modifications of the ricin A chain protein fold. Calculation of unfolding-folding transition temperature and evaluation of a possible unfolding model
-
determination of the coupling of tyrosine residues, presence of energy transfer from tyrosine to tryptophan residues. The molar absorption coefficient of ricin in phosphate-buffered saline is 93900 per mol and cm
-
purified recombinant mutant RTAs N122A and R213D, sitting drop vapour diffusion method using microbridges, X-ray diffraction structure determination and analysis at 1.4 A and 1.9 A resolution, respectively
-
ricin A chain in complex with inhibitor 7-carboxy pterin, hanging drop vapor diffusion method, using 75 mM Tris-HCl pH 8.9, 10 mM BME, 1 mM EDTA, 4.1% (w/v) PEG MW 8000
-
the total helical content of ricin is 53.6%
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C171A
-
does not infer with enzymatic depurination activity, leaving C259 as docking station for the fluorescence dye, which changes its emission properties upon change from aqueous to hydrophobic (membrane) environment, C259 is reduced in the lumen of the endoplasmic reticulum
D75A
-
site-directed mutagenesis of the RTA residue, the mutant RTA shows very low expression levels so that purification to homogeneity is not achieved
D75N
-
site-directed mutagenesis of the RTA residue, the mutant RTA shows very low expression levels so that purification to homogeneity is not achieved
D75S
-
site-directed mutagenesis of the RTA residue, the mutant RTA shows very low expression levels so that purification to homogeneity is not achieved
E177D/C259S/I249C
-
residues 249 and 259 show membrane- and temperature-induced structural transition, meaning that the residues are exposed to the bilayer interior, both labeled with N,N'-dimethyl-N-(iodoacetyl)-N'-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)ethylenediamine
E177K
K4R/C171A/E177D/K239R/E135K
-
no temperature-induced change, meaning that residue 135 is bound within the membrane right away, labeled with succinimidyl 6-(N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino)hexanoate
K4R/C171A/E177D/K239R/E61K
-
no temperature-induced change, meaning that residue 61 is bound within the membrane right away, labeled with succinimidyl 6-(N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino)hexanoate
K4R/C171A/E177D/K239R/Q128K
-
no temperature-induced change, meaning that residue 128 is bound within the membrane right away, labeled with succinimidyl 6-(N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino)hexanoate
K4R/C171A/E177D/K239R/Q98K
-
no temperature-induced change, meaning that residue 98 is bound within the membrane right away, labeled with succinimidyl 6-(N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino)hexanoate
K4R/C171A/E177D/K239R/R114K
-
no temperature-induced change, meaning that residue 114 is bound within the membrane right away, labeled with succinimidyl 6-(N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino)hexanoate
K4R/C171A/E177D/K239R/R31K
-
residues 31 shows membrane- and temperature-induced structural transition, meaning that the residues are exposed to the bilayer interior, labeled with succinimidyl 6-(N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino)hexanoate
N122A
-
site-directed mutagenesis of the RTA residue, 37.5fold reduced activity compared to the wild-type RTA, the reconstituted enzyme comprising RTB and N122A RTA shows about 30fold reduced cytotoxicity compared to the wild-type enzyme
N78S
-
site-directed mutagenesis of the RTA residue, less than 2fold reduced activity compared to the wild-type RTA, the reconstituted enzyme comprising RTB and N78S RTA shows about 2fold reduced cytotoxicity compared to the wild-type enzyme
P250L/A253V
-
mutant of ricin A chain, catalytically inactive, not cytotoxic in yeast
P95L/E145K
-
mutant of ricin A chain, catalytically active but not cytotoxic in yeast
R134A
-
site-directed mutagenesis of the RTA residue, the expression of the recombinant mutant is abolished, R134 probably plays a structural role
R134Q
-
site-directed mutagenesis of the RTA residue, the expression of the recombinant mutant is abolished, R134 probably plays a structural role
R213A
-
site-directed mutagenesis of the RTA residue, the mutant RTA shows unaltered structure, but 10fold reduced activity compared to the wild-type RTA
R213D
-
site-directed mutagenesis of the RTA residue, the mutant RTA shows unaltered structure, but 2fold reduced activity compared to the wild-type RTA
R258A
-
site-directed mutagenesis of the RTA residue, similar activity compared to the wild-type RTA
R258D
-
site-directed mutagenesis of the RTA residue, slightly reduced activity compared to the wild-type RTA
R48A
-
site-directed mutagenesis of the RTA residue, slightly reduced activity compared to the wild-type RTA
S215F
-
mutant of ricin A chain, catalytically active but not cytotoxic in yeast
V76M/Y80A
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65 - 70
-
irreversible thermal unfolding
70
-
half-life in milk-based infant formula 9.8 min, in soy-based infant formula 16 min
75
-
half-life in milk-based infant formula 5.8 min, in soy-based infant formula 8.7 min
80
-
half-life in milk-based infant formula 5.1 min, in soy-based infant formula 6.9 min
85
-
half-life in milk-based infant formula 3.1 min, in soy-based infant formula 3.0 min
90
-
half-life in milk-based infant formula 1.8 min, in soy-based infant formula 2.0 min
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the recombinant secreted ricin-B expressed in tobacco hairy root culture is degraded in the medium within 24 h with complete loss after 72 h, the recombinant ricin-B can be recovered by aqueous two-phase extraction using PEG/potassium phosphate or PEG/sodium sulfate, the latter is more efficient
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
according to Deeks et al., Biochemistry 41, p. 3405-3413, 2002
-
HisTrap column chromatography and Superdex 200 gel filtration
-
immunoaffinity capture with antiricinus communis agglutinin, immobilized and cross-linked to Dynabeads Protein G
-
native enzyme from seeds
-
Ni-NTA column chromatography
-
particle removal by centrifugation of ground material and concentration by dialysis against PEG
-
recombinant fusion protein
-
recombinant His-tagged RTA and RLPs from Escherichia coli BL21-AI cells by nickel affinity chromatography
-
recombinant ricin A-chain RTA V81M without N- and C-terminal extensions from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation and anion exchange chromatography
-
recombinant secreted ricin-B from tobacco hairy root culture medium
-
recombinant wild-type and mutant ricin A chains from Escherichia coli strain JM101 by anion exchange chromatography and cobalt affinity chromatography to homogeneity
-
recombinant wild-type and some mutant RTAs from Escherichia coli strain JM101 by cation exchange chromatography to homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli JM 101
expression of A chain in Escherichia coli with His-tag. Construction of replication-deficient ricin B chain adenovirus-green fluorescent protein fusion protein
-
expression of precursor form of ricin A chain in Saccharomyces cerevisiae
-
expression of ricin A chain in Saccharomyces cerevisiae
-
expression of ricin B-subunit in Nicotiana tabacum hairy roots, the recombinant protein is secreted to the culture medium
-
expression of RTA and each of the six RLPs in polyhistidine-tagged form in Escherichia coli BL21-AI cells
-
expression of wild-type and mutant ricin A chains in Escherichia coli strain JM101
-
expression of wild-type and mutant RTAs in Escherichia coli strain JM101
-
fusion gene of enhanced green fluorescent protein and ricin A chain, expression in Escherichia coli
-
fusion protein of a 90-amino acid peptide from the simian rotavirus SA-11 nonstructural protein, NSP4 linked to the N-terminus of the ricin B subunit protein, expression in Escherichia coli
-
overexpression of ricin A-chain RTA V81M without N- and C-terminal extensions in Escherichia coli strain BL21(DE3)
-
RTA gene from genomic DANN cloned and expressed in Escherichia coli XL-1 blue
-
the enzymatically active ricin A chain is expressed in Escherichia coli BL21(DE3)pLysS cells
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
coarse-grained latice simulation model of sequence-structure modifications of the ricin A chain protein fold. Calculation of unfolding-folding transition temperature and evaluation of a possible unfolding model
-
reassociation of purified recombinant RTAs mixed with RTB in presence of 0.1 M lactose and 2% v/v 2-mercaptoethanol by dialysis for 24 h against 1 l of NaCl/phosphate solution containing 0.1 M lactose, followed by further 36 h against 5 l of NaCl/phosphate solution
-
the recombinant secreted ricin-B expressed in tobacco hairy root culture is degraded in the medium within 24 h with complete loss after 72 h, the recombinant ricin-B can be recovered by aqueous two-phase extraction using PEG/potassium phosphate or PEG/sodium sulfate, the latter is more efficient
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
isolation of aptamers that specifically recognize ricin by affinity chromatography and by capillary electrophoresis/systematic evolution of ligands by exponential enrichment, i.e. CE-SELEX. Identification of three aptamers with Kd values in the nanomolar range that do not recognize abrin toxin
medicine
the conserved alpha-helix is considered as a potential target for the prevention and treatment of ribosome-inactivating protein poisoning
analysis
biotechnology
-
ricin is a prototype for the construction of chimeric molecules, called immunotoxins, based on the structure of the A-B toxins. An application of the ricin B as a carrier is the fusion and expression with different viral antigens used for vaccination therapies. A fusion protein combining the genes for endotoxin of Bacillus thuringiensis with the ricin B chain, and transgenic rice and maize plants expressing the fusion protein are more toxic to insects than plants containing the toxin gene alone
diagnostics
medicine
nutrition
-
study on the effects of heat treatment on the detection and toxicity of ricin added to milk- and soy-based infant formulas. Half-lives of ricin cytotoxicactivity in a milk-based infant formula at 70°C, 75°C, 80°C, 85°C, and 90°C are 9.8, 5.8, 5.1, 3.1, and 1.8 min, respectively, the comparable values for a soy-based infant formula are 16, 8.7, 6.9, 3.0, and 2.0 min
additional information
-
ricin is used as biological weapon for warefare and terrorism
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Xu, Y.Z.; Liu, W.Y.
Effects of the active aldehyde group generated by RNA N-glycosidase in the sarcin/ricin domain of rat 28S ribosomal RNA on peptide elongation
Biol. Chem.
381
113-119
2000
Ricinus communis, Cinnamomum camphora, Saponaria ocymoides, Trichosanthes sp., Gypsophila vaccaria
Manually annotated by BRENDA team
Endo, Y.; Tsurugi, K.
The RNA N-glycosidase activity of ricin A-chain. The characteristics of the enzymatic activity of ricin A-chain with ribosomes and with rRNA
J. Biol. Chem.
263
8735-8739
1988
Ricinus communis
Manually annotated by BRENDA team
Endo, Y.; Tsurugi, K.
The RNA N-glycosidase activity of ricin A-chain
Nucleic Acids Symp. Ser.
19
139-142
1988
Ricinus communis
Manually annotated by BRENDA team
Peumans, W.J.; Hao, Q.; Van Damme, E.J.
Ribosome-inactivating proteins from plants: more than RNA N-glycosidases?
FASEB J.
15
1493-1506
2001
Abrus precatorius, Ricinus communis, Eranthis hyemalis, Suregada multiflora, Hordeum vulgare, Momordica charantia, no activity in Arabidopsis thaliana, Phytolacca americana, Phytolacca insularis, Saponaria officinalis, Trichosanthes kirilowii, Trichosanthes sp.
Manually annotated by BRENDA team
Zhang, A.H.; Tang, S.; Liu, W.y.
Substrate-structure dependence of ribotoxins on cleaving RNA in C. camphora ribosome
J. Nat. Toxins
10
119-125
2001
Ricinus communis, Cinnamomum camphora
Manually annotated by BRENDA team
Honjo, E.; Watanabe, K.; Tsukamoto, T.
Real-time kinetic analyses of the interaction of ricin toxin A-chain with ribosomes prove a conformational change involved in complex formation
J. Biochem.
131
267-275
2002
Ricinus communis
Manually annotated by BRENDA team
Wang, B.Z.; Zou, W.G.; Liu, W.Y.; Liu, X.Y.
The lower cytotoxicity of cinnamomin (a type II RIP) is due to its B-chain
Arch. Biochem. Biophys.
451
91-96
2006
Ricinus communis, Cinnamomum camphora
Manually annotated by BRENDA team
Amukele, T.K.; Schramm, V.L.
Ricin A-chain substrate specificity in RNA, DNA, and hybrid stem-loop structures
Biochemistry
43
4913-4922
2004
Ricinus communis
Manually annotated by BRENDA team
Roday, S.; Amukele, T.; Evans, G.B.; Tyler, P.C.; Furneaux, R.H.; Schramm, V.L.
Inhibition of ricin A-chain with pyrrolidine mimics of the oxacarbenium ion transition state
Biochemistry
43
4923-4933
2004
Ricinus communis
Manually annotated by BRENDA team
Amukele, T.K.; Roday, S.; Schramm, V.L.
Ricin A-chain activity on stem-loop and unstructured DNA substrates
Biochemistry
44
4416-4425
2005
Ricinus communis
Manually annotated by BRENDA team
Yamasaki, C.; Nishikawa, K.; Zeng, X.T.; Katayama, Y.; Natori, Y.; Komatsu, N.; Oda, T.
Induction of cytokines by toxins that have an identical RNA N-glycosidase activity: Shiga toxin, ricin, and modeccin
Biochim. Biophys. Acta
1671
44-50
2004
Ricinus communis, Corynebacterium diphtheriae, Shigella dysenteriae, Adenia digitata
Manually annotated by BRENDA team
Hartley, M.R.; Lord, J.M.
Cytotoxic ribosome-inactivating lectins from plants
Biochim. Biophys. Acta
1701
1-14
2004
Abrus precatorius, Cucurbita pepo, Dianthus caryophyllus, Escherichia coli, Mirabilis jalapa, Momordica charantia, Phytolacca americana, Sambucus nigra, Saponaria officinalis, Shigella dysenteriae, Trichosanthes kirilowii, Triticum aestivum, Viscum album, Adenia volkensii, Sambucus ebulus, Ricinus communis (P02879)
Manually annotated by BRENDA team
Sestili, P.; Alfieri, R.; Carnicelli, D.; Martinelli, C.; Barbieri, L.; Stirpe, F.; Bonelli, M.; Petronini, P.G.; Brigotti, M.
Shiga toxin 1 and ricin inhibit the repair of H2O2-induced DNA single strand breaks in cultured mammalian cells
DNA Repair
4
271-277
2005
Ricinus communis, Shigella dysenteriae
Manually annotated by BRENDA team
Marsden, C.J.; Fueloep, V.; Day, P.J.; Lord, J.M.
The effect of mutations surrounding and within the active site on the catalytic activity of ricin A chain
Eur. J. Biochem.
271
153-162
2004
Ricinus communis
Manually annotated by BRENDA team
Zhang, C.; Medina-Bolivar, F.; Buswell, S.; Cramer, C.L.
Purification and stabilization of ricin B from tobacco hairy root culture medium by aqueous two-phase extraction
J. Biotechnol.
117
39-48
2005
Ricinus communis
Manually annotated by BRENDA team
Wang, S.; Feng, J.; Guo, J.; Guo, L.; Li, Y.; Sun, Y.; Qin, W.; Hu, M.; Han, G.; Shen, B.
A novel designed single domain antibody on 3-D-structure of ricin A chain remarkably blocked ricin-induced cytotoxicity
Mol. Immunol.
43
1912-1919
2006
Ricinus communis
Manually annotated by BRENDA team
Stirpe, F.
Ribosome-inactivating proteins
Toxicon
44
371-383
2004
Abrus precatorius, Ricinus communis, Suregada multiflora, Hordeum vulgare, Phytolacca americana, Sambucus nigra, Saponaria officinalis, Shigella dysenteriae, Trichosanthes kirilowii, Viscum album, Zea mays, Phoradendron californicum, Adenia volkensii, Adenia digitata, Mirabilis expansa
Manually annotated by BRENDA team
Marsden, C.J.; Knight, S.; Smith, D.C.; Day, P.J.; Roberts, L.M.; Phillips, G.J.; Lord, J.M.
Insertional mutagenesis of ricin A chain: a novel route to an anti-ricin vaccine
Vaccine
22
2800-2805
2004
Ricinus communis
Manually annotated by BRENDA team
Wang, H.B.; Xia, F.; Ge, J.; Yin, J.; Tan, L.S.; Zhang, P.D.; Zhong, J.
Co-application of ricin A chain and a recombinant adenovirus expressing ricin B chain as a novel approach for cancer therapy
Acta Pharmacol. Sin.
28
657-662
2007
Ricinus communis
Manually annotated by BRENDA team
Lubelli, C.; Chatgilialoglu, A.; Bolognesi, A.; Strocchi, P.; Colombatti, M.; Stirpe, F.
Detection of ricin and other ribosome-inactivating proteins by an immuno-polymerase chain reaction assay
Anal. Biochem.
355
102-109
2006
Ricinus communis, Dianthus caryophyllus
Manually annotated by BRENDA team
Keener, W.K.; Rivera, V.R.; Young, C.C.; Poli, M.A.
An activity-dependent assay for ricin and related RNA N-glycosidases based on electrochemiluminescence
Anal. Biochem.
357
200-207
2006
Abrus precatorius, Ricinus communis, Saponaria officinalis
Manually annotated by BRENDA team
Haes, A.J.; Giordano, B.C.; Collins, G.E.
Aptamer-based detection and quantitative analysis of ricin using affinity probe capillary electrophoresis
Anal. Chem.
78
3758-3764
2006
Ricinus communis
Manually annotated by BRENDA team
Mei, Q.; Fredrickson, C.K.; Lian, W.; Jin, S.; Fan, Z.H.
Ricin detection by biological signal amplification in a well-in-a-well device
Anal. Chem.
78
7659-7664
2006
Ricinus communis
Manually annotated by BRENDA team
Becher, F.; Duriez, E.; Volland, H.; Tabet, J.C.; Ezan, E.
Detection of functional ricin by immunoaffinity and liquid chromatography-tandem mass spectrometry
Anal. Chem.
79
659-665
2007
Ricinus communis
Manually annotated by BRENDA team
Liu, Q.; Zhan, J.; Chen, X.; Zheng, S.
Ricin A chain reaches the endoplasmic reticulum after endocytosis
Biochem. Biophys. Res. Commun.
343
857-863
2006
Ricinus communis
Manually annotated by BRENDA team
Roday, S.; Saen-oon, S.; Schramm, V.L.
Vinyldeoxyadenosine in a sarcin-ricin RNA loop and its binding to ricin toxin A-chain
Biochemistry
46
6169-6182
2007
Phytolacca americana, Ricinus communis (P02879)
Manually annotated by BRENDA team
Hartley, P.G.; Alderton, M.R.; Dawson, R.M.; Wells, D.
Ricin antitoxins based on lyotropic mesophases containing galactose amphiphiles
Bioconjug. Chem.
18
152-159
2007
Ricinus communis
Manually annotated by BRENDA team
Ganguly, D.; Mukhopadhyay, C.
Binding diversity of the two binding sites of ricin B lectin
Biopolymers
83
83-94
2006
Ricinus communis (P02879)
Manually annotated by BRENDA team
Ganguly, D.; Mukhopadhyay, C.
Extended binding site of ricin B lectin for oligosaccharide recognition
Biopolymers
86
311-320
2007
Ricinus communis (P02879)
Manually annotated by BRENDA team
Olson, M.A.; Yeh, I.C.; Lee, M.S.
Coarse-grained lattice model simulations of sequence-structure fitness of a ribosome-inactivating protein
Biopolymers
89
153-159
2008
Ricinus communis
Manually annotated by BRENDA team
Anderson, G.P.; Matney, R.; Liu, J.L.; Hayhurst, A.; Goldman, E.R.
Multiplexed fluid array screening of phage displayed anti-ricin single domain antibodies for rapid assessment of specificity
Biotechniques
43
806-811
2007
Ricinus communis
Manually annotated by BRENDA team
Wang, Y.; Guo, L.; Zhao, K.; Chen, J.; Feng, J.; Sun, Y.; Li, Y.; Shen, B.
Novel chimeric anti-ricin antibody C4C13 with neutralizing activity against ricin toxicity
Biotechnol. Lett.
29
1811-1816
2007
Ricinus communis
Manually annotated by BRENDA team
Carra, J.H.; McHugh, C.A.; Mulligan, S.; Machiesky, L.M.; Soares, A.S.; Millard, C.B.
Fragment-based identification of determinants of conformational and spectroscopic change at the ricin active site
BMC Struct. Biol.
7
72
2007
Ricinus communis (P02879)
Manually annotated by BRENDA team
Jandhyala, D.M.; Ahluwalia, A.; Obrig, T.; Thorpe, C.M.
ZAK: a MAP3Kinase that transduces Shiga toxin and ricin induced proinflammatory cytokine expression
Cell. Microbiol.
10
1468-1477
2008
Ricinus communis, Escherichia coli
Manually annotated by BRENDA team
Tang, J.; Xie, J.; Shao, N.; Yan, Y.
The DNA aptamers that specifically recognize ricin toxin are selected by two in vitro selection methods
Electrophoresis
27
1303-1311
2006
Ricinus communis (P02879)
Manually annotated by BRENDA team
Pratt, T.S.; Pincus, S.H.; Hale, M.L.; Moreira, A.L.; Roy, C.J.; Tchou-Wong, K.M.
Oropharyngeal aspiration of ricin as a lung challenge model for evaluation of the therapeutic index of antibodies against ricin A-chain for post-exposure treatment
Exp. Lung Res.
33
459-481
2007
Ricinus communis
Manually annotated by BRENDA team
Mantis, N.J.; McGuinness, C.R.; Sonuyi, O.; Edwards, G.; Farrant, S.A.
Immunoglobulin A antibodies against ricin A and B subunits protect epithelial cells from ricin intoxication
Infect. Immun.
74
3455-3462
2006
Ricinus communis
Manually annotated by BRENDA team
Li, X.P.; Baricevic, M.; Saidasan, H.; Tumer, N.E.
Ribosome depurination is not sufficient for ricin-mediated cell death in Saccharomyces cerevisiae
Infect. Immun.
75
417-428
2007
Ricinus communis
Manually annotated by BRENDA team
Rathore, S.S.; Ghosh, P.C.
Effect of surface charge and density of distearylphosphatidylethanolamine-mPEG-2000 (DSPE-mPEG-2000) on the cytotoxicity of liposome-entrapped ricin: effect of lysosomotropic agents
Int. J. Pharm.
350
79-94
2008
Ricinus communis
Manually annotated by BRENDA team
Bharadwaj, S.; Rathore, S.S.; Ghosh, P.C.
Enhancement of the cytotoxicity of liposomal ricin by the carboxylic ionophore monensin and the lysosomotropic amine NH4Cl in Chinese hamster ovary cells
Int. J. Toxicol.
25
349-359
2006
Ricinus communis
Manually annotated by BRENDA team
Jackson, L.S.; Tolleson, W.H.; Chirtel, S.J.
Thermal inactivation of ricin using infant formula as a food matrix
J. Agric. Food Chem.
54
7300-7304
2006
Ricinus communis
Manually annotated by BRENDA team
Sturm, M.B.; Roday, S.; Schramm, V.L.
Circular DNA and DNA/RNA hybrid molecules as scaffolds for ricin inhibitor design
J. Am. Chem. Soc.
129
5544-5550
2007
Ricinus communis
Manually annotated by BRENDA team
Lindsey, C.Y.; Richardson, J.D.; Brown, J.E.; Hale, M.L.
Intralaboratory validation of cell-free translation assay for detecting ricin toxin biological activity
J. AOAC Int.
90
1316-1325
2007
Ricinus communis
Manually annotated by BRENDA team
Dawson, R.M.; Alderton, M.R.; Wells, D.; Hartley, P.G.
Monovalent and polyvalent carbohydrate inhibitors of ricin binding to a model of the cell-surface receptor
J. Appl. Toxicol.
26
247-252
2006
Ricinus communis
Manually annotated by BRENDA team
Jolliffe, N.A.; Di Cola, A.; Marsden, C.J.; Lord, J.M.; Ceriotti, A.; Frigerio, L.; Roberts, L.M.
The N-terminal ricin propeptide influences the fate of ricin A-chain in tobacco protoplasts
J. Biol. Chem.
281
23377-23385
2006
Ricinus communis
Manually annotated by BRENDA team
Parikh, B.A.; Tortora, A.; Li, X.P.; Tumer, N.E.
Ricin inhibits activation of the unfolded protein response by preventing splicing of the HAC1 mRNA
J. Biol. Chem.
283
6145-6153
2008
Ricinus communis
Manually annotated by BRENDA team
Fulton, R.E.; Thompson, H.G.
Fluorogenic hand-held immunoassay for the identification of ricin - rapid analyte measurement platform
J. Immunoassay Immunochem.
28
227-241
2007
Ricinus communis
Manually annotated by BRENDA team
Mouser, P.; Filigenzi, M.S.; Puschner, B.; Johnson, V.; Miller, M.A.; Hooser, S.B.
Fatal ricin toxicosis in a puppy confirmed by liquid chromatography/mass spectrometry when using ricinine as a marker
J. Vet. Diagn. Invest.
19
216-220
2007
Ricinus communis
Manually annotated by BRENDA team
Slominska-Wojewodzka, M.; Gregers, T.F.; Waelchli, S.; Sandvig, K.
EDEM is involved in retrotranslocation of ricin from the endoplasmic reticulum to the cytosol
Mol. Biol. Cell
17
1664-1675
2006
Ricinus communis
Manually annotated by BRENDA team
Gonzalez, T.V.; Farrant, S.A.; Mantis, N.J.
Ricin induces IL-8 secretion from human monocyte/macrophages by activating the p38 MAP kinase pathway
Mol. Immunol.
43
1920-1923
2006
Ricinus communis
Manually annotated by BRENDA team
Chakravartula, S.V.; Guttarla, N.
Amino acids of ricin and its polypeptides
Nat. Prod. Res.
22
258-263
2008
Ricinus communis
Manually annotated by BRENDA team
Gaigalas, A.K.; Cole, K.D.; Bykadi, S.; Wang, L.; DeRose, P.
Photophysical properties of ricin
Photochem. Photobiol.
83
1149-1156
2007
Ricinus communis
Manually annotated by BRENDA team
Vitetta, E.S.; Smallshaw, J.E.; Coleman, E.; Jafri, H.; Foster, C.; Munford, R.; Schindler, J.
A pilot clinical trial of a recombinant ricin vaccine in normal humans
Proc. Natl. Acad. Sci. USA
103
2268-2273
2006
Ricinus communis
Manually annotated by BRENDA team
Korennykh, A.V.; Correll, C.C.; Piccirilli, J.A.
Evidence for the importance of electrostatics in the function of two distinct families of ribosome inactivating toxins
RNA
13
1391-1396
2007
Ricinus communis, Saponaria officinalis
Manually annotated by BRENDA team
Sha, O.; Kwong, W.H.; Pang Cho, E.Y.; Wai Yew, D.T.; Ng, T.B.
Different neuronal toxicity of single-chain ribosome-inactivating proteins on the rat retina
Toxicon
51
45-53
2008
Ricinus communis, Trichosanthes kirilowii
Manually annotated by BRENDA team
Grimmer, S.; Spilsberg, B.; Hanada, K.; Sandvig, K.
Depletion of sphingolipids facilitates endosome to Golgi transport of ricin
Traffic
7
1243-1253
2006
Ricinus communis
Manually annotated by BRENDA team
Utskarpen, A.; Slagsvold, H.H.; Iversen, T.G.; Waelchli, S.; Sandvig, K.
Transport of ricin from endosomes to the Golgi apparatus is regulated by Rab6A and Rab6A
Traffic
7
663-672
2006
Ricinus communis
Manually annotated by BRENDA team
Carra, J.H.; Wannemacher, R.W.; Tammariello, R.F.; Lindsey, C.Y.; Dinterman, R.E.; Schokman, R.D.; Smith, L.A.
Improved formulation of a recombinant ricin A-chain vaccine increases its stability and effective antigenicity
Vaccine
25
4149-4158
2007
Ricinus communis
Manually annotated by BRENDA team
Choi, N.W.; Estes, M.K.; Langridge, W.H.
Ricin toxin B subunit enhancement of rotavirus NSP4 immunogenicity in mice
Viral Immunol.
19
54-63
2006
Ricinus communis
Manually annotated by BRENDA team
Li, X.P.; Chiou, J.C.; Remacha, M.; Ballesta, J.P.; Tumer, N.E.
A Two-Step Binding Model Proposed for the Electrostatic Interactions of Ricin A Chain with Ribosomes
Biochemistry
48
3853-3863
2009
Ricinus communis (P02879)
Manually annotated by BRENDA team
Chiou, J.C.; Li, X.P.; Remacha, M.; Ballesta, J.P.; Tumer, N.E.
The ribosomal stalk is required for ribosome binding, depurination of the rRNA and cytotoxicity of ricin A chain in Saccharomyces cerevisiae
Mol. Microbiol.
70
1441-1452
2008
Ricinus communis
Manually annotated by BRENDA team
Keener, W.; Rivera, V.R.; Cho, C.Y.; Hale, M.L.; Garber, E.A.E; Poli, M.A.
Identifitcation of the RNA N-glycosidase activity of ricin in castor bean extracts by an electrochemiluminescence-based assay
Anal. Biochem.
378
87-89
2008
Abrus precatorius, Ricinus communis
Manually annotated by BRENDA team
Brinkworth, C.S.; Pigott, E.J.; Bourne, D.J.
Detection of intact ricin in crude and purified extracts from castor beans using matrix-assisted laser desorption ionization mass spectrometry
Anal. Chem.
81
1529-1535
2009
Ricinus communis
Manually annotated by BRENDA team
Bai, Y.; Monzingo, A.F.; Robertus, J.D.
The X-ray structure of ricin A chain with a novel inhibitor
Arch. Biochem. Biophys.
483
23-28
2009
Ricinus communis (P02879)
Manually annotated by BRENDA team
Roday, S.; Sturm, M.B.; Blakaj, D.; Schramm, V.L.
Detection of an abasic site in RNA with stem-loop DNA beacons: application to an activity assay for Ricin Toxin A-Chain
J. Biochem. Biophys. Methods
70
945-953
2008
Ricinus communis
Manually annotated by BRENDA team
Mayerhofer, P.U.; Cook, J.P.; Wahlman, J.; Pinheiro, T.T.; Moore, K.A.; Lord, J.M.; Johnson, A.E.; Roberts, L.M.
Ricin A chain insertion into endoplasmic reticulum membranes is triggered by a temperature increase to 37 {degrees}C
J. Biol. Chem.
284
10232-10242
2009
Ricinus communis
Manually annotated by BRENDA team
Melchior, W.B.; Tolleson, W.H.
A functional quantitative polymerase chain reaction assay for ricin, Shiga toxin, and related ribosome-inactivating proteins
Anal. Biochem.
396
204-211
2010
Ricinus communis, Escherichia coli
Manually annotated by BRENDA team
Sturm, M.B.; Schramm, V.L.
Detecting ricin: sensitive luminescent assay for ricin A-chain ribosome depurination kinetics
Anal. Chem.
81
2847-2853
2009
Ricinus communis
Manually annotated by BRENDA team
Tan, Q.; Dong, D.; Yin, X.; Sun, J.; Ren, H.; Li, R.
Comparative analysis of depurination catalyzed by ricin A-chain on synthetic 32mer and 25mer oligoribonucleotides mimicking the sarcin/ricin domain of the rat 28S rRNA and E. coli 23S rRNA
J. Biotechnol.
139
156-162
2009
Ricinus communis
Manually annotated by BRENDA team
Ho, M.C.; Sturm, M.B.; Almo, S.C.; Schramm, V.L.
Transition state analogues in structures of ricin and saporin ribosome-inactivating proteins
Proc. Natl. Acad. Sci. USA
106
20276-20281
2009
Ricinus communis (P02879), Saponaria officinalis (Q2QEH4)
Manually annotated by BRENDA team
Leshin, J.; Danielsen, M.; Credle, J.J.; Weeks, A.; O'Connell, K.P.; Dretchen, K.
Characterization of ricin toxin family members from Ricinus communis
Toxicon
55
658-661
2010
Ricinus communis
Manually annotated by BRENDA team
Wahome, P.G.; Bai, Y.; Neal, L.M.; Robertus, J.D.; Mantis, N.J.
Identification of small-molecule inhibitors of ricin and shiga toxin using a cell-based high-throughput screen
Toxicon
56
313-323
2010
Ricinus communis (P02879)
Manually annotated by BRENDA team
Arfilli, V.; Carnicelli, D.; Rocchi, L.; Ricci, F.; Pagliaro, P.; Tazzari, P.L.; Brigotti, M.
Shiga toxin 1 and ricin A chain bind to human polymorphonuclear leucocytes through a common receptor
Biochem. J.
432
173-180
2010
Ricinus communis, Suregada multiflora, Saponaria officinalis
Manually annotated by BRENDA team
Horrix, C.; Raviv, Z.; Flescher, E.; Voss, C.; Berger, M.
Plant ribosome-inactivating proteins type II induce the unfolded protein response in human cancer cells
Cell. Mol. Life Sci.
68
1269-1281
2011
Ricinus communis, Ximenia americana, Adenia volkensii
Manually annotated by BRENDA team
Giansanti, F.; Di Leandro, L.; Koutris, I.; Cialfi, A.; Benedetti, E.; Laurenti, G.; Pitari, G.; Ippoliti, R.
Ricin and saporin: Plant enzymes for the research and the clinics
Curr. Chem. Biol.
4
99-107
2010
Ricinus communis, Saponaria officinalis
-
Manually annotated by BRENDA team
Pruet, J.M.; Jasheway, K.R.; Manzano, L.A.; Bai, Y.; Anslyn, E.V.; Robertus, J.D.
7-Substituted pterins provide a new direction for ricin A chain inhibitors
Eur. J. Med. Chem.
46
3608-3615
2011
Ricinus communis
Manually annotated by BRENDA team
Dai, J.; Zhao, L.; Yang, H.; Guo, H.; Fan, K.; Wang, H.; Qian, W.; Zhang, D.; Li, B.; Wang, H.; Guo, Y.
Identification of a novel functional domain of ricin responsible for its potent toxicity
J. Biol. Chem.
286
12166-12171
2011
Ricinus communis (P02879)
Manually annotated by BRENDA team
Au, K.Y.; Wang, R.R.; Wong, Y.T.; Wong, K.B.; Zheng, Y.T.; Shaw, P.C.
Engineering a switch-on peptide to ricin A chain for increasing its specificity towards HIV-infected cells
Biochim. Biophys. Acta
1840
958-963
2014
Ricinus communis
Manually annotated by BRENDA team
O'Hara, J.M.; Brey, R.N.; Mantis, N.J.
Comparative efficacy of two leading candidate ricin toxin a subunit vaccines in mice
Clin. Vaccine Immunol.
20
789-794
2013
Ricinus communis
Manually annotated by BRENDA team
May, K.L.; Li, X.P.; Martinez-Azorin, F.; Ballesta, J.P.; Grela, P.; Tchorzewski, M.; Tumer, N.E.
The P1/P2 proteins of the human ribosomal stalk are required for ribosome binding and depurination by ricin in human cells
FEBS J.
279
3925-3936
2012
Ricinus communis
Manually annotated by BRENDA team
Rasooly, R.; He, X.; Friedman, M.
Milk inhibits the biological activity of ricin
J. Biol. Chem.
287
27924-27929
2012
Ricinus communis (P02879), Ricinus communis
Manually annotated by BRENDA team
Rudolph, M.J.; Vance, D.J.; Cheung, J.; Franklin, M.C.; Burshteyn, F.; Cassidy, M.S.; Gary, E.N.; Herrera, C.; Shoemaker, C.B.; Mantis, N.J.
Crystal structures of ricin toxins enzymatic subunit (RTA) in complex with neutralizing and non-neutralizing single-chain antibodies
J. Mol. Biol.
426
3057-3068
2014
Ricinus communis (P02879)
Manually annotated by BRENDA team
Schieltz, D.M.; McWilliams, L.G.; Kuklenyik, Z.; Prezioso, S.M.; Carter, A.J.; Williamson, Y.M.; McGrath, S.C.; Morse, S.A.; Barr, J.R.
Quantification of ricin, RCA and comparison of enzymatic activity in 18 Ricinus communis cultivars by isotope dilution mass spectrometry
Toxicon
95
72-83
2015
Ricinus communis
Manually annotated by BRENDA team
Barbier, J.; Bouclier, C.; Johannes, L.; Gillet, D.
Inhibitors of the cellular trafficking of ricin
Toxins
4
15-27
2012
Ricinus communis
Manually annotated by BRENDA team
Fan, X.; Zhu, Y.; Wang, C.; Niu, L.; Teng, M.; Li, X.
Structural insights into the interaction of the ribosomal P stalk protein P2 with a type II ribosome-inactivating protein ricin
Sci. Rep.
6
37803
2016
Ricinus communis (P02879)
Manually annotated by BRENDA team