BRENDA - Enzyme Database
show all sequences of 2.1.1.228

Structural insight into the methyltransfer mechanism of the bifunctional Trm5

Wang, C.; Jia, Q.; Zeng, J.; Chen, R.; Xie, W.; Sci. Adv. 3, e1700195 (2017) View publication on PubMedView publication on EuropePMC

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
gene trm5a, recombinant expression of His6-tagged wild-type and mutant enzymes
Pyrococcus abyssi
Crystallization (Commentary)
Crystallization (Commentary)
Organism
analysis of enzyme complex structures of Trm5b (MjTrm5b, PDB IDs 2YX1 and 3AY0) from Methanococcus jannaschii
Methanocaldococcus jannaschii
purified recombinant apo-PaTrm5a and PaTrm5a in complex with tRNAPhe, with SAM, and as PaTrm5a-tRNAPhe (imG-14)-SAH ternary complex, sitting drop vapor diffusion method, 6 mg/ml recombinant His6-tagged enzyme protein is mixed with tRNAPhe at a molar ratio of 1:0.4 in a buffer containing 20 mM Tris-HCl, pH 8.0, 150 mM NaCl, 1 mM DTT, and 1.5 mM SAH or SAM, and equilibration against a reservoir solution containing 45% 2-methyl-2,4-pentanediol, 100 mM MES, pH 6.5, and 200 mM NH4OAc, 1 week, X-ray diffraction structure determination and analysis at 2.6-3.2 A resolution, molecular replacement using complex structure of the MjTrm5b-tRNACys-SAM complex (PDB ID 2ZZN) as the search model, modelling
Pyrococcus abyssi
Engineering
Protein Variants
Commentary
Organism
D243A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
Pyrococcus abyssi
E213A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
Pyrococcus abyssi
H128A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
Pyrococcus abyssi
R133A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
Pyrococcus abyssi
R135A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
Pyrococcus abyssi
R174A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
Pyrococcus abyssi
Y318A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
Pyrococcus abyssi
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Methanocaldococcus jannaschii
Mg2+
required
Pyrococcus abyssi
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
additional information
Pyrococcus abyssi
bifunctional Trm5a from Pyrococcus abyssi (PaTrm5a) catalyses not only the methylation of N1, but also the further methylation of C7 on 4 demethylwyosine at position 37 to produce isowyosine (EC 2.1.1.228 and EC 2.1.1.282, respectively)
?
-
-
-
S-adenosyl-L-methionine + guanine37 in tRNAPhe
Methanocaldococcus jannaschii
-
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPhe
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPhe
Pyrococcus abyssi
-
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPhe
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPhe
Methanocaldococcus jannaschii DSM 2661
-
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPhe
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Methanocaldococcus jannaschii
Q58293
-
-
Methanocaldococcus jannaschii DSM 2661
Q58293
-
-
Pyrococcus abyssi
Q9V2G1
-
-
Purification (Commentary)
Purification (Commentary)
Organism
recombinant His6-tagged wild-type and mutant enzymes
Pyrococcus abyssi
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
additional information
bifunctional Trm5a from Pyrococcus abyssi (PaTrm5a) catalyses not only the methylation of N1, but also the further methylation of C7 on 4 demethylwyosine at position 37 to produce isowyosine (EC 2.1.1.228 and EC 2.1.1.282, respectively)
758348
Pyrococcus abyssi
?
-
-
-
-
additional information
structural basis for substrate recognition, the D1 domain of the enzyme undergoes large conformational changes upon the binding of tRNA, the enzyme recognizes the overall shape of tRNA, overview. Enzyme-substrate interactions in the catalytic domain, D1 domain ofMjTrm5b transitions, overview
758348
Methanocaldococcus jannaschii
?
-
-
-
-
additional information
structural basis for substrate recognition, the D1 domain of the enzyme undergoes large conformational changes upon the binding of tRNA. The enzyme recognizes the overall shape of tRNA. PaTrm5a adopts distinct open conformations before and after the binding of tRNA. Enzyme-substrate interactions in the catalytic domain. The anticodon interactions mostly concentrate on the A36-G37-A38 triplet. Proposed reaction mechanism of Trm5a with modified yeast tRNAPhe, overview
758348
Pyrococcus abyssi
?
-
-
-
-
additional information
structural basis for substrate recognition, the D1 domain of the enzyme undergoes large conformational changes upon the binding of tRNA, the enzyme recognizes the overall shape of tRNA, overview. Enzyme-substrate interactions in the catalytic domain, D1 domain ofMjTrm5b transitions, overview
758348
Methanocaldococcus jannaschii DSM 2661
?
-
-
-
-
S-adenosyl-L-methionine + guanine37 in tRNAPhe
-
758348
Methanocaldococcus jannaschii
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPhe
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPhe
-
758348
Pyrococcus abyssi
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPhe
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPhe
-
758348
Methanocaldococcus jannaschii DSM 2661
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPhe
-
-
-
?
Subunits
Subunits
Commentary
Organism
More
substrate interactions with the catalytic region in the PaTrm5a-tRNAPhe-SAH ternary complex, overview
Pyrococcus abyssi
Synonyms
Synonyms
Commentary
Organism
MjTrm5b
-
Methanocaldococcus jannaschii
More
see also EC 2.1.1.282
Pyrococcus abyssi
PaTrm5a
-
Pyrococcus abyssi
TAW22
-
Pyrococcus abyssi
Trm5a
-
Pyrococcus abyssi
trm5b
-
Methanocaldococcus jannaschii
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Methanocaldococcus jannaschii
37
-
assay at
Pyrococcus abyssi
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Methanocaldococcus jannaschii
8
-
assay at
Pyrococcus abyssi
Cofactor
Cofactor
Commentary
Organism
Structure
S-adenosyl-L-methionine
-
Methanocaldococcus jannaschii
S-adenosyl-L-methionine
-
Pyrococcus abyssi
Cloned(Commentary) (protein specific)
Commentary
Organism
gene trm5a, recombinant expression of His6-tagged wild-type and mutant enzymes
Pyrococcus abyssi
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
S-adenosyl-L-methionine
-
Methanocaldococcus jannaschii
S-adenosyl-L-methionine
-
Pyrococcus abyssi
Crystallization (Commentary) (protein specific)
Crystallization
Organism
analysis of enzyme complex structures of Trm5b (MjTrm5b, PDB IDs 2YX1 and 3AY0) from Methanococcus jannaschii
Methanocaldococcus jannaschii
purified recombinant apo-PaTrm5a and PaTrm5a in complex with tRNAPhe, with SAM, and as PaTrm5a-tRNAPhe (imG-14)-SAH ternary complex, sitting drop vapor diffusion method, 6 mg/ml recombinant His6-tagged enzyme protein is mixed with tRNAPhe at a molar ratio of 1:0.4 in a buffer containing 20 mM Tris-HCl, pH 8.0, 150 mM NaCl, 1 mM DTT, and 1.5 mM SAH or SAM, and equilibration against a reservoir solution containing 45% 2-methyl-2,4-pentanediol, 100 mM MES, pH 6.5, and 200 mM NH4OAc, 1 week, X-ray diffraction structure determination and analysis at 2.6-3.2 A resolution, molecular replacement using complex structure of the MjTrm5b-tRNACys-SAM complex (PDB ID 2ZZN) as the search model, modelling
Pyrococcus abyssi
Engineering (protein specific)
Protein Variants
Commentary
Organism
D243A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
Pyrococcus abyssi
E213A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
Pyrococcus abyssi
H128A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
Pyrococcus abyssi
R133A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
Pyrococcus abyssi
R135A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
Pyrococcus abyssi
R174A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
Pyrococcus abyssi
Y318A
site-directed mutagenesis, substrate binding compared to wild-type enzyme
Pyrococcus abyssi
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Methanocaldococcus jannaschii
Mg2+
required
Pyrococcus abyssi
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
additional information
Pyrococcus abyssi
bifunctional Trm5a from Pyrococcus abyssi (PaTrm5a) catalyses not only the methylation of N1, but also the further methylation of C7 on 4 demethylwyosine at position 37 to produce isowyosine (EC 2.1.1.228 and EC 2.1.1.282, respectively)
?
-
-
-
S-adenosyl-L-methionine + guanine37 in tRNAPhe
Methanocaldococcus jannaschii
-
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPhe
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPhe
Pyrococcus abyssi
-
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPhe
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPhe
Methanocaldococcus jannaschii DSM 2661
-
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPhe
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His6-tagged wild-type and mutant enzymes
Pyrococcus abyssi
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
additional information
bifunctional Trm5a from Pyrococcus abyssi (PaTrm5a) catalyses not only the methylation of N1, but also the further methylation of C7 on 4 demethylwyosine at position 37 to produce isowyosine (EC 2.1.1.228 and EC 2.1.1.282, respectively)
758348
Pyrococcus abyssi
?
-
-
-
-
additional information
structural basis for substrate recognition, the D1 domain of the enzyme undergoes large conformational changes upon the binding of tRNA, the enzyme recognizes the overall shape of tRNA, overview. Enzyme-substrate interactions in the catalytic domain, D1 domain ofMjTrm5b transitions, overview
758348
Methanocaldococcus jannaschii
?
-
-
-
-
additional information
structural basis for substrate recognition, the D1 domain of the enzyme undergoes large conformational changes upon the binding of tRNA. The enzyme recognizes the overall shape of tRNA. PaTrm5a adopts distinct open conformations before and after the binding of tRNA. Enzyme-substrate interactions in the catalytic domain. The anticodon interactions mostly concentrate on the A36-G37-A38 triplet. Proposed reaction mechanism of Trm5a with modified yeast tRNAPhe, overview
758348
Pyrococcus abyssi
?
-
-
-
-
additional information
structural basis for substrate recognition, the D1 domain of the enzyme undergoes large conformational changes upon the binding of tRNA, the enzyme recognizes the overall shape of tRNA, overview. Enzyme-substrate interactions in the catalytic domain, D1 domain ofMjTrm5b transitions, overview
758348
Methanocaldococcus jannaschii DSM 2661
?
-
-
-
-
S-adenosyl-L-methionine + guanine37 in tRNAPhe
-
758348
Methanocaldococcus jannaschii
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPhe
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPhe
-
758348
Pyrococcus abyssi
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPhe
-
-
-
?
S-adenosyl-L-methionine + guanine37 in tRNAPhe
-
758348
Methanocaldococcus jannaschii DSM 2661
S-adenosyl-L-homocysteine + N1-methylguanine37 in tRNAPhe
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
substrate interactions with the catalytic region in the PaTrm5a-tRNAPhe-SAH ternary complex, overview
Pyrococcus abyssi
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Methanocaldococcus jannaschii
37
-
assay at
Pyrococcus abyssi
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Methanocaldococcus jannaschii
8
-
assay at
Pyrococcus abyssi
General Information
General Information
Commentary
Organism
malfunction
deletion of the D1 domain greatly reduces the affinity and activity of PaTrm5a toward its RNA substrate
Pyrococcus abyssi
additional information
structure comparison of the Pyrococcus abyssii Trm5a enzyme structure (PDB IDs 5HJJ and 5WT1) with the structure of its orthologue Trm5b (MjTrm5b, PDB IDs 2YX1 and 3AY0) from Methanococcus jannaschii, overview
Methanocaldococcus jannaschii
additional information
structure comparison of the Pyrococcus abyssii Trm5a enzyme structure (PDB IDs 5HJJ and 5WT1) with the structure of its orthologue Trm5b (MjTrm5b, PDB IDs 2YX1 and 3AY0) from Methanococcus jannaschii, overview
Pyrococcus abyssi
physiological function
the methyltransferase Trm5a from Pyrococcus abyssi (PaTrm5a) plays a key role in this hypermodification process in generating m1G37 (EC 2.1.1.228) and imG2 (EC 2.1.1.282), two products of the wyosine biosynthetic pathway, through two methyl transfers to distinct substrates
Pyrococcus abyssi
General Information (protein specific)
General Information
Commentary
Organism
malfunction
deletion of the D1 domain greatly reduces the affinity and activity of PaTrm5a toward its RNA substrate
Pyrococcus abyssi
additional information
structure comparison of the Pyrococcus abyssii Trm5a enzyme structure (PDB IDs 5HJJ and 5WT1) with the structure of its orthologue Trm5b (MjTrm5b, PDB IDs 2YX1 and 3AY0) from Methanococcus jannaschii, overview
Methanocaldococcus jannaschii
additional information
structure comparison of the Pyrococcus abyssii Trm5a enzyme structure (PDB IDs 5HJJ and 5WT1) with the structure of its orthologue Trm5b (MjTrm5b, PDB IDs 2YX1 and 3AY0) from Methanococcus jannaschii, overview
Pyrococcus abyssi
physiological function
the methyltransferase Trm5a from Pyrococcus abyssi (PaTrm5a) plays a key role in this hypermodification process in generating m1G37 (EC 2.1.1.228) and imG2 (EC 2.1.1.282), two products of the wyosine biosynthetic pathway, through two methyl transfers to distinct substrates
Pyrococcus abyssi
Other publictions for EC 2.1.1.228
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
755697
Zhong
Targeting the bacterial epitr ...
Pseudomonas aeruginosa, Pseudomonas aeruginosa UCBPP-PA14
ACS Infect. Dis.
5
326-335
2019
-
1
1
-
-
-
63
2
-
-
-
2
-
8
-
-
-
-
-
-
-
-
6
-
3
-
-
1
2
-
-
-
1
-
-
63
-
1
1
1
-
-
-
63
63
-
2
-
-
-
2
-
-
-
-
-
-
-
-
6
-
-
-
1
2
-
-
-
-
-
1
1
-
2
2
756152
Li
Backbone resonance assignment ...
Pseudomonas aeruginosa, Pseudomonas aeruginosa UCBPP-PA14
Biomol. NMR Assign.
13
327-332
2019
-
1
1
-
-
-
1
-
-
-
-
2
-
7
-
-
1
-
-
1
-
-
2
2
2
-
-
-
-
1
-
-
1
-
-
-
-
1
1
1
-
-
-
-
1
-
-
-
-
-
2
-
-
-
1
-
1
-
-
2
2
-
-
-
-
1
-
-
-
-
2
2
-
-
-
756153
Li
Backbone resonance assignment ...
Pseudomonas aeruginosa, Pseudomonas aeruginosa UCBPP-PA14
Biomol. NMR Assign.
13
49-53
2019
-
-
1
-
-
-
2
-
-
-
-
2
-
6
-
-
1
-
-
-
-
-
2
-
2
-
-
1
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
2
-
-
-
-
-
2
-
-
-
1
-
-
-
-
2
-
-
-
1
-
-
-
-
-
-
1
1
-
-
-
756774
Hou
Codon-specific translation by ...
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium, Saccharomyces cerevisiae, Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412, Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720, Saccharomyces cerevisiae ATCC 204508
Front. Genet.
10
713
2019
-
-
-
-
1
-
-
-
-
2
-
7
-
8
-
-
-
-
-
-
-
-
7
-
4
-
-
-
-
-
-
-
3
-
-
-
-
-
-
3
-
1
-
-
-
-
-
-
2
-
7
-
-
-
-
-
-
-
-
7
-
-
-
-
-
-
-
-
-
1
8
8
1
-
-
757408
Whitehouse
Development of inhibitors aga ...
Mycobacteroides abscessus
J. Med. Chem.
62
7210-7232
2019
-
1
1
1
-
-
50
-
-
-
-
1
-
6
-
-
1
-
-
-
-
-
1
1
2
-
-
-
-
-
-
-
1
-
-
-
-
1
1
1
1
-
-
-
50
-
-
-
-
-
1
-
-
-
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
2
2
-
-
-
757409
Zhong
Thienopyrimidinone derivative ...
Staphylococcus aureus, Mycobacterium tuberculosis, Pseudomonas aeruginosa
J. Med. Chem.
62
7788-7805
2019
-
-
3
2
-
3
42
3
-
2
-
3
-
5
-
-
-
-
-
-
-
-
3
-
12
1
-
-
-
1
-
-
3
-
-
26
-
-
3
3
2
-
3
26
42
-
3
-
2
-
3
-
-
-
-
-
-
-
-
3
-
1
-
-
-
1
-
-
-
-
3
3
-
-
-
757863
Jin
AtTrm5a catalyses 1-methylgua ...
Arabidopsis thaliana
Nucleic Acids Res.
47
883-898
2019
-
-
1
-
1
-
-
-
1
1
-
2
-
8
-
-
1
-
-
2
-
-
2
-
3
1
-
-
-
1
-
-
1
-
-
-
-
-
1
1
-
1
-
-
-
-
-
1
1
-
2
-
-
-
1
-
2
-
-
2
-
1
-
-
-
1
-
-
-
-
2
2
-
-
-
758329
Jaroensuk
Crystal structure and catalyt ...
Pseudomonas aeruginosa, Pseudomonas aeruginosa UCBPP-PA14
RNA
25
1481-1496
2019
-
1
1
1
1
-
1
3
-
2
-
2
-
10
-
-
1
-
-
-
-
-
14
2
5
1
-
-
2
1
-
-
1
3
-
-
-
1
1
1
1
1
-
-
1
3
3
-
2
-
2
-
-
-
1
-
-
-
-
14
2
1
-
-
2
1
-
-
-
-
2
2
-
2
2
757201
Zhou
A hypertension-associated mit ...
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii NBRC 100440, Methanocaldococcus jannaschii DSM 2661, Methanocaldococcus jannaschii ATCC 43067, Methanocaldococcus jannaschii JAL-1, Methanocaldococcus jannaschii JCM 10045
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12
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755960
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The crystal structure of the ...
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2
1
1
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1
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4
4
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756161
Goto-Ito
Trm5 and TrmD two enzymes fr ...
Escherichia coli, Haemophilus influenzae, Methanocaldococcus jannaschii, Pyrococcus abyssi, Pyrococcus abyssi Orsay, Methanocaldococcus jannaschii NBRC 100440, Haemophilus influenzae RD, Methanocaldococcus jannaschii DSM 2661, Methanocaldococcus jannaschii ATCC 43067, Methanocaldococcus jannaschii JAL-1, Haemophilus influenzae DSM 11121, Haemophilus influenzae KW20, Haemophilus influenzae ATCC 51907, Methanocaldococcus jannaschii JCM 10045
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32
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10
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1
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16
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30
4
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14
14
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756163
Hori
Transfer RNA methyltransferas ...
Haemophilus influenzae, Aquifex aeolicus, Escherichia coli
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E23
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6
3
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7
7
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756631
Hou
TrmD A methyl transferase fo ...
Haemophilus influenzae, Aquifex aeolicus, Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412, Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720
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6
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8
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16
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758348
Wang
Structural insight into the m ...
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1
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Methyl transfer by substrate ...
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758324
Urbonavicius
Evolution of tRNAPhe imG2 met ...
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22
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2016
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Wang
Crystal structures of the bif ...
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2
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TRMT5 mutations cause a defect ...
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737174
Ito
Structural basis for methyl-do ...
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4
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10
757582
Hou
Kinetic analysis of tRNA meth ...
Escherichia coli, Haemophilus influenzae, Homo sapiens, Methanocaldococcus jannaschii, Methanocaldococcus jannaschii NBRC 100440, Haemophilus influenzae RD, Methanocaldococcus jannaschii DSM 2661, Methanocaldococcus jannaschii ATCC 43067, Methanocaldococcus jannaschii JAL-1, Haemophilus influenzae DSM 11121, Haemophilus influenzae KW20, Haemophilus influenzae ATCC 51907, Methanocaldococcus jannaschii JCM 10045
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729858
Kawamura
Transfer RNA methyltransferase ...
Thermoplasma acidophilum, Thermoplasma acidophilum HO-62
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2014
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735927
Sakaguchi
A divalent metal ion-dependent ...
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1
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2
1
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736428
Masuda
The temperature sensitivity of ...
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1
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6
737226
Christian
Conservation of structure and ...
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9
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12
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1
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737228
Paris
The T. brucei TRM5 methyltrans ...
Trypanosoma brucei brucei, Trametes pubescens 927 / 4 GUTat10.1 / TREU927
RNA
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721035
Sakaguchi
Recognition of guanosine by di ...
Escherichia coli, Methanocaldococcus jannaschii
RNA
18
1687-1701
2012
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2
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2
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2
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10
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2
2
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721029
Lahoud
Differentiating analogous tRNA ...
Escherichia coli, Methanocaldococcus jannaschii
RNA
17
1236-1246
2011
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24
2
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2
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2
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24
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24
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Christian
Control of catalytic cycle by ...
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2
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2
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2
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721026
Christian
Mechanism of N-methylation by ...
Methanocaldococcus jannaschii
RNA
16
2484-2492
2010
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1
18
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1
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1
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1
18
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1
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701123
Goto-Ito
Crystal structure of archaeal ...
Methanocaldococcus jannaschii
Proteins
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2008
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1
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1
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1
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1
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1
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1
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1
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1
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1
1
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1
1
712103
Toyooka
Stabilization of tRNA (mG37) m ...
Aquifex aeolicus
Genes Cells
13
807-816
2008
-
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1
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1
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687609
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Yeast mitochondrial initiator ...
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2
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1
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Christian
Distinct determinants of tRNA ...
Escherichia coli, Methanocaldococcus jannaschii
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5
2
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5
673850
Takeda
The substrate specificity of t ...
Aquifex aeolicus
Genes Cells
11
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2006
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1
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13
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6
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1
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15
-
3
1
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1
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1
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13
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1
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1
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15
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1
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711197
Christian
Catalysis by the second class ...
Methanocaldococcus jannaschii
Biochemistry
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9
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11
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1
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1
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2
1
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11
1
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9
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-
11
-
-
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1
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1
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1
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11
1
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1
1
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11
11
661154
Brule
Isolation and characterization ...
Escherichia coli, Homo sapiens
Biochemistry
43
9243-9255
2004
1
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2
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5
13
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3
2
2
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9
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2
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20
2
4
2
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-
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4
2
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1
-
2
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-
-
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-
5
-
13
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3
2
2
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-
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2
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-
-
20
2
2
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4
2
-
-
-
-
-
-
-
-
662010
O'Dwyer
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Liu
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710708
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