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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

     3 Hydrolases
         3.2 Glycosylases
             3.2.2 Hydrolysing N-glycosyl compounds
                3.2.2.22 rRNA N-glycosylase

Engineering

Engineering on EC 3.2.2.22 - rRNA N-glycosylase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K213A
-
the mutation results in a loss of 1-2 logs of cytotoxic potency relative to the wild type fusion protein toxin
K215A
-
the mutant retains full cytotoxic activity
K217A
-
the mutation results in a loss of 1-2 logs of cytotoxic potency relative to the wild type fusion protein toxin
K222A
-
the mutation results in a loss of 1-2 logs of cytotoxic potency relative to the wild type fusion protein toxin
E167K
-
the mutation reduces the toxicity of Shiga toxins 1 and 2
E167K/R176K
-
the mutations reduce the toxicity of Shiga toxins 1 and 2
N75A
-
the mutation reduces the toxicity of Shiga toxins 1 and 2
R170A
R176K
-
the mutation reduces the toxicity of Shiga toxins 1 and 2
S31N
-
location within Stx 2 B subunit, mutation prevents extracellular release of enzyme
Y1477F
-
binding site for tyrosine kinase Syk at clathrin chain
Y77A
-
the mutation reduces the toxicity of Shiga toxins 1 and 2
E168D
-
replacing DNA fragments of the total synthetic gene of MAP, weaker inhibitory effect
R26L
-
replacing DNA fragments of the total synthetic gene of MAP
R48L
-
replacing DNA fragments of the total synthetic gene of MAP
Y118F
-
replacing DNA fragments of the total synthetic gene of MAP, slightly stronger inhibitory effect
Y72F
-
replacing DNA fragments of the total synthetic gene of MAP, slightly stronger inhibitory effect
C259A
-
decrease in processing of the C-terminal extension
E176V
site-directed mutagenesis, inactive mutant showing no cytotoxicity
G75D
-
no maturation of precursor form, localization exclusivelly in the membrane fraction
L252K
-
delayed appearance of mature form in the cytosol
L252stop
-
accumulation of the truncated protein primarily in the membrane fraction, at the lumenal side of microsomal membranes
N253A
-
like wild-type, localization in the cytosol
N253R
-
like wild-type, localization in the cytosol
N253stop
-
reduced accumulation of the protein in the cytosol, appearance of a slightly larger form in the membrane fraction
N70A
site-directed mutagenesis, the mutation delays the enzyme depurination activity on ribosomes and the onset of translation arrest, N70A PAP shows highly reduced cytotoxicity and destabilizes its own mRNA, but binds to cap and blocks cap-dependent translation
T262stop
-
present in both the membrane fraction and the cytosol
V73E
-
no maturation of precursor form, reduced stability, localized to the lumenal side of microsomal membranes
Y254stop
-
retains the ability to accumulate in the cytosol
S211A
no influence on N-beta-glycosidase activity, but reduction of adenine polynucleotide glycosylase activity. Residual activity on deadenylation is 33% on polyA, 73% on DNA, and 66% on rRNA
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
D231E
-
B chain mutation in one carbohydrate binding site, reduced insecticidal activity, recombinant tobacco plant mutants SNA-I 103M1 and SNA-I 107M1
N48S/D231E
-
B chain mutation in both carbohydrate binding sites almost abolished insecticidal activity comparable to control plants, recombinant tobacco plant mutants SNA-I 109M2 and SNA-I 112M2
E176A
-
site-directed mutagenesis
R179A
R24A
-
site-directed mutagenesis
S255C
-
intact stable enzyme, site far away from ribosome inactivating site residues, N-terminal mutations were unstable, low tendency to dimerization by disulfide-bonding, but high level of cross-linking with nonspecific mouse anti-human IgG antibody
W208A
Y120A
-
site-directed mutagenesis
Y72A
-
site-directed mutagenesis
D176A
1.5fold increase in enzyme concentration required for 50% inhibition of protein synthesis
K173A
weakened binding to eukaryotic ribosomal protein P2, 7.5fold increase in enzyme concentration required for 50% inhibition of protein synthesis
K173A/R174A/K177A
K177A
weakened binding to eukaryotic ribosomal protein P2, 3fold increase in enzyme concentration required for 50% inhibition of protein synthesis
R174A
weakened binding to eukaryotic ribosomal protein P2, 6fold increase in enzyme concentration required for 50% inhibition of protein synthesis
V232K/N236D
17-fold reduced activity compared to wild-type, no ribosome interaction, V232K is at mouth of hydrophobic pocket, where the LF motif of c11-P binds, expected to block the access of the P-protein to the pocket, N236D substitution removes hydrogen bond between the amide of Asn236 and the backbone carbonyl of Leu9 of c11-P
E85A
-
site-directed mutagenesis
E85Q
-
site-directed mutagenesis
E85R
-
site-directed mutagenesis
Y70A
-
n-TCS mutant
additional information