3.2.2.22: rRNA N-glycosylase This is an abbreviated version! For detailed information about rRNA N-glycosylase, go to the full flat file .
Word Map on EC 3.2.2.22
Reaction
A4324 in 28S rRNA +
H2O =
deadenylated 28S rRNA +
adenine
Synonyms (ribosome-inactivating protein)-like protein, abelesculin, ABRaA, abrin, abrin-a A chain, Abrus precatorius agglutinin, alpha-MC, alpha-momorcharin, alpha-pisavin, antiviral protein DAP-30, aralin, B-32, balsamin, BBAP1, BE27, beta-momorcharin, beta-pisavin, Bougainvillea xbuttiana antiviral protein 1, bouganin, camphorin, CAP30, cinnamomin, Cochinin B, cytotoxic ribosome-inactivating lectin, D6D54_07625, D6D54_08385, D6D54_08880, depurinating rRNA N-glycosidase, dianthin 30, dianthin 32, dianthin-30, diphtheria toxin, ebulin b, ebulitin alpha, ebulitin beta, ebulitin gamma, gelonin, gysophilin, hispin, IRAb, IRIP, Iris agglutinin b, Iris ribosome-inactivating protein, JIP60, karasurin-A, KML, lamjapin, luffaculin I, luffin P1, lychnin, MAP, marmorin, ME1, Mirabilis antiviral protein, mistletoe lectin I, mistletoe lectin II, mistletoe lectin III, ML-I, MLI, MLII, MLIII, MOD, modeccin, momorcochin, momorcochin-S, momordin, momordin I, momordin II, momorgrosvin, More, N-glycosidase, n-TCS, neo-trichosanthin, nigrin b, nigritin f1, nigritin f2, PAG, PAGase, PAP, PAP-I, PAP-II, PAP-III, PAP-R, PAP-S, PD-L, PD-L1, PD-L4, pepocin, PGase, pokeweed anti-viral protein, pokeweed antiviral protein, polynucleotide:adenosine glycosidase, polynucleotide:adenosine glycosylase, porrectin, RA, RCA-II, ribosomal inactivating protein, ribosomal ribonucleate N-glycosidase, ribosome inactivating protein, ribosome-inactivating protein, ribosome-inactivating protein 3, ribosome-inactivating protein type II, ribosome-inactivating proteins, ribosome-inactivating type II protein, ribosome-specific N-glycosidase, ricin, ricin A, ricin A chain, ricin A-chain, ricin toxin A-chain, ricin-A-chain, ricin-like protein, Ricinus communis agglutinin, Ricinus communis agglutinin II, RIP, RIP-1, RIP1, RIP2, RIPII, riproximin, RLP1, RLP2, RLP3, RLP4, RLP5, RLP6, RNA N-glycosidase, RNA-NGA, RNA-specific N-glycosidase, RNase Bo, Rpx, rRNA N-glycosidase, RTA, Sambucus nigra agglutinin, Sambucus nigra agglutinin I, SAP, saporin, saporin 6, saporin S-6, saporin S6, saporin-6, saporin-L1, saporin-S6, saporins, SBA, SCO7092, SEPIN, Shiga toxin, Shiga toxin 1, Shiga toxin 1 subunit A, Shiga toxin 2, Shiga toxin 2 subunit A, Shiga toxin type 1, Shiga toxin type 2, Shiga toxin-1, shiga-like toxin, shiga-like toxin I, sieboldin-b, single-chain ribosome-inactivating protein, SLT-I, SLT-II, SLT-IIv, SNA, SNA-I, SNA-V, SnaI, SNAIf, SNAV, SNLRP, SoRIP1, SoRIP2, stenodactylin, Stx, Stx type 1, Stx-1, Stx1, Stx1A, Stx2, Stx2A, Stx2dact, StxB, TCS, trichoanguin, trichomaglin, trichosanthin, Trichosanthrip, trichosnathin, TRIP, tritin-L, tritin-S, TYchi, type 1 ribosome inactivating protein, type 1 ribosome-inactivating protein, type 1 RIP, type 2 ribosome inactivating protein, type 2 ribosome-inactivating protein, type 2 RIP, type 2RIP, type 3 RIP, type I ribosome inactivating protein, type I ribosome-inactivating protein, type I RIP, type II ribosome inactivating protein, type II ribosome-inactivating protein, type II RIP, type III ribosome-inactivating protein, type III RIP, type-1 ribosome-inactivating protein, type-1 RIP, type-2 ribosome-inactivating protein, type-2 RIP, VAA-I, viscinum, Viscum album agglutinin I, viscumin, volkensin
ECTree
Subunits
Subunits on EC 3.2.2.22 - rRNA N-glycosylase
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x * 30000, SDS-PAGE
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x * 28000, A chain, + x * 29000, B chain, SDS-PAGE
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x * 32500, mature enzyme, SDS-PAGE
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x * 35000, precursor, SDS-PAGE
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x * 28000, subunit A1, SDS-PAGE
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x * 29310, MALDI-TOF, recombinant protein
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x * 29094, calculated from amino acid sequence
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x * 29000, A chain, + x * 28000, B chain, SDS-PAGE
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x * 62912, MALDI-TOF mass spectrometry
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x * 30000-35000, recombinant SNA-I, SNA-IV, SNA-V, and SNLRP, SDS-PAGE
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x * 29770, calculated from sequence
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x * 13000, SDS-PAGE, x * 10964.6, mass spectrometry
dimer
2 * 30000, recombinant abricin A-chain, SDS-PAGE
dimer
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subunit A and subunit B connected by a disulfide bridge
dimer
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(alphabeta) structure
dimer
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subunit A and subunit B connected by a disulfide bridge
dimer
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subunit A and subunit B connected by a disulfide bridge
dimer
-
1 * 29000, A-chain, + 1 * 32000, B-chain, SDS-PAGE
dimer
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1 * 21000, SDS-PAGE
dimer
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1 * 33000 + 1 * 30000, cinnamomin, SDS-PAGE
dimer
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1 * 30500 + 1 * 34500, cinnamomin, A- and B-chain, SDS-PAGE
dimer
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heterodimer formed by a catalytic subunit A, the A-chain, and a carbohydrate binding subunit B, the B-chain
dimer
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1 * 30500 + 1 * 33500, A-chain and B-chain, SDS-PAGE
dimer
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subunit A and subunit B connected by a disulfide bridge
dimer
-
(alphabeta) structure
dimer
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heterodimer formed by a catalytic subunit A and a carbohydrate binding subunit B
dimer
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heterodimer formed by a catalytic subunit A, RTA and a carbohydrate binding subunit B, RTB
dimer
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heterodimer formed by a catalytic subunit A, RTA, and a carbohydrate binding subunit B, RTB
dimer
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heterodimer formed by a catalytic subunit A, the A-chain, and a carbohydrate binding subunit B, the B-chain
dimer
heterodimer, subunits A and B, RTA and RTB, are derived from a single precursor protein, structure comparison and analysis
dimer
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subunit A and subunit B connected by a disulfide bridge
dimer
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subunit A and subunit B connected by a disulfide bridge
dimer
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1 * 27000 + 1 * 33000, SDS-PAGE
dimer
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heterodimer formed by a catalytic subunit A and a carbohydrate binding subunit B
dimer
-
subunit A and subunit B connected by a disulfide bridge
dimer
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1 * 28478, ML-I subunit A + 1 * 28981, ML-I subunits B, sequence calculation
dimer
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1 * 30000, recombinant B-subunit, the enzyme forms a heterodimer comprising subunits A and B, the latter is the carbohydrate-binding subunit
dimer
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heterodimer formed by a catalytic subunit A and a carbohydrate binding subunit B
dimer
-
subunit A and subunit B connected by a disulfide bridge
dimer
type III RIP isozyme RIP1 forms dimers and ressembles type II RIPs concerning its subunit structure
dimer
type III RIP isozyme RIP2 forms dimers and ressembles type II RIPs concerning its subunit structure
heterodimer
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1 * 40000 + 1 * 22000, chain B and chain A, SDS-PAGE
heterodimer
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1 * 40000 + 1 * 22000, chain B and chain A, SDS-PAGE
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heterodimer
1 * 29000 + 1 * 31000, SDS-PAGE
monomer
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1 * 35000, SDS-PAGE, 1 * 34600, calculated for mature protein, 1 * 62000, calculated for full-length protein including N-terminal leader sequence, pectin methylesterase inhibitor domain, pectin esterase domain and pectin esterase signature sequences 1 and 2
monomer
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1 * 25000, SDS-PAGE
monomer
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1 * 22500, camphorin, SDS-PAGE
monomer
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1 * 27700, SDS-PAGE
monomer
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1 * 10000, SDS-PAGE
monomer
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1 * 28000, SDS-PAGE
monomer
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1 * 30700, momorchochin-S, SDS-PAGE
monomer
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1 * 30200, SDS-PAGE
monomer
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1 * 30200, SO-R1, SDS-PAGE
monomer
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1 * 31600, SO-L1, SO-L2, and SO-S6, SDS-PAGE
monomer
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1 * 30200-31600, 7 major saporins, SDS-PAGE
monomer
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1 * 30900, SO-R2, SO-R3, and SO-S%, SDS-PAGE
monomer
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1 * 27000, SDS-PAGE
pentamer
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one of two Stx liberated by Stx-producing Escherichia coli is composed of an A subunit monomer and a B subunit pentamer
additional information
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structure comparison and analysis
additional information
the A-chain exhibits the RNA N-glycosidase activity, while the B-chain mediates cell entry by binding to the target cell surface glycolipid receptor
additional information
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structure comparison and analysis
additional information
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volkensin binds strongly to asialofetuin, but does not show any affnity to fetuin, carboxypeptidase Y and transferrin
additional information
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structure comparison and analysis
additional information
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the A1 chain of shiga-like toxin 1 binds to the human ribosomal proteins P0, P1, and P2. Removal of the C-terminal 17 amino acids of either protein P1 or P2 abolishes the interaction, whereas P0 still binds to the A1 domain even without its C-terminus
additional information
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2 domains connected by a covalent linker
additional information
Iris sp.
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overall enzyme structure, overview
additional information
structure modeling of ME1
additional information
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structure modeling of ME1
additional information
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structure comparison and analysis
additional information
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the N-terminal amino acid sequence of the enzyme is identical with that of several superoxide dimutases
additional information
isozyme structure analysis by ESI/Q-TOF mass spectrometric and circular dichroism analysis, structure-function relationship, influence of carbohydrate moieties, overview
additional information
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isozyme structure analysis by ESI/Q-TOF mass spectrometric and circular dichroism analysis, structure-function relationship, influence of carbohydrate moieties, overview
additional information
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the heterodimeric enzyme consists of the catalytic ricin A chain, RTA, and the cabohydrate-binding B chain, RTB
additional information
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analysis of amino acid composition of A and B chain. The total helical content of ricin is 53.6%
additional information
comparison of binding properties of ricin B chain toward different mono- and disaccharide ligands, calculation of free energies of binding and analysis of epimeric specificity of the protein
additional information
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ricin interacts with the ER degradation enhancing alpha-mannosidase I-like protein EDEM responsible for redirecting aberrant proteins for ER-associated protein degradation and with Sec61alpha, and both kifunensin and puromycin enhance these interactions. Overexpression of EDEM strongly protects against ricin. In presence of kifunensin, EDEM promotes retranslocation of ricin from the ER to the cytosol
additional information
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structure comparison and analysis
additional information
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structure comparison and analysis
additional information
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structure comparison and analysis
additional information
the 5'-flanking regions of the isozymes contains functional motifs involved in e.g. plant defense in SoRIP2 and with functions related to embryonic development in SoRIP1, overview
additional information
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the 5'-flanking regions of the isozymes contains functional motifs involved in e.g. plant defense in SoRIP2 and with functions related to embryonic development in SoRIP1, overview
additional information
trichosanthin interacts with the C-terminal tail of eukaryotic ribosomal protein P2, involving residues K173, R174, and K177 of trichosanthin
additional information
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tryptic peptides mapping, overview
additional information
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amino acid sequence analysis and comparison with other toxin sequences, overview
additional information
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structure comparison and analysis
additional information
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2 domains connected by a covalent linker
additional information
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MOD structure determination and comparison using the crystal structure of DELTAN5-MOD, PDB ID 2PQI, and by determination of the NMR solution structure of MOD, PDB ID 2k6H, detailed overview. MOD has shorter beta6 and alphaB segments, probably for accommodating easier substrate binding, and an alpha-helix instead of an antiparallel beta-sheet in the C-terminal domain, which is involved in binding ribosomal protein P2 in some RIPs, compared to type I and II RIPs. The P2 binding site on MOD is located at the N-terminal domain near the internal inactivation region