BRENDA - Enzyme Database show
show all sequences of 2.4.2.29

An integrative approach combining noncovalent mass spectrometry, enzyme kinetics and X-ray crystallography to decipher Tgt protein-protein and protein-RNA interaction

Ritschel, T.; Atmanene, C.; Reuter, K.; Van Dorsselaer, A.; Sanglier-Cianferani, S.; Klebe, G.; J. Mol. Biol. 393, 833-847 (2009)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
mutants introduced into plasmid pET9d-ZM4 and transformed into Escherichia coli BL21(DE3) GOLD cells
Zymomonas mobilis
Crystallization (Commentary)
Crystallization
Organism
mutant K52M, by hanging-drop, vapor-diffusion method and followed by macroseeding, at a resolution of 2.0 A, forms crystals under the same conditions as wild-type, while all attempts to obtain diffracting crystals from mutant Y330F are unsuccessful. Compared to wild-type, crystals of mutant K52M are very fragile and show only a limited diffraction quality
Zymomonas mobilis
Engineering
Amino acid exchange
Commentary
Organism
K52M
reduced turnover value. At a concentration of protein of 0.01 mM appears almost exclusively as a homodimer as the wild-type, when the concentration of protein is lowered to a minimal value of 0.001 mM, a substantial proportion of monomer becomes evident
Zymomonas mobilis
Y330F
reduced turnover value. At a concentration of protein of 0.01 mM reveals a significant amount of monomer, when the concentration of protein is lowered to a minimal value of 0.001 mM, a substantial proportion of monomer becomes evident
Zymomonas mobilis
Inhibitors
Inhibitors
Commentary
Organism
Structure
6-amino-2-[(3-piperidin-1-ylpropyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
cannot modify the structure of the dimer interface, prevents the formation of the catalytically active Tgt:tRNA complex, and can disrupt the preformed complex
Zymomonas mobilis
6-amino-4-[2-(4-methoxyphenyl)ethyl]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
can modify the structure of the dimer interface, prevents the formation of the catalytically active Tgt:tRNA complex, and can disrupt the preformed complex
Zymomonas mobilis
6-amino-4-[2-(benzylamino)ethyl]-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
addresses a hydrophobic subpocket close to the dimer interface that may affect quarternary structure formation, prevents the formation of the catalytically active Tgt:tRNA complex, and can disrupt the preformed complex
Zymomonas mobilis
6-amino-4-[2-[(cyclohexylmethyl)amino]ethyl]-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
can modify the structure of the dimer interface, prevents the formation of the catalytically active Tgt:tRNA complex, and can disrupt the preformed complex
Zymomonas mobilis
6-amino-4-[2-[(cyclopentylmethyl)amino]ethyl]-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
addresses a hydrophobic subpocket close to the dimer interface that may affect quarternary structure formation, prevents the formation of the catalytically active Tgt:tRNA complex, and can disrupt the preformed complex
Zymomonas mobilis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.00098
-
[tRNATyr]7-aminomethyl-7-carbaguanine
mutant K52M
Zymomonas mobilis
0.00158
-
[tRNATyr]7-aminomethyl-7-carbaguanine
mutant Y330F
Zymomonas mobilis
0.00217
-
[tRNATyr]7-aminomethyl-7-carbaguanine
wild-type
Zymomonas mobilis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Zn2+
one structural Zn2+ per subunit
Zymomonas mobilis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
85600
-
expected for a Tgt dimer containing one structural Zn2+ per subunit
Zymomonas mobilis
85610
-
Tgt, noncovalent mass spectrometry
Zymomonas mobilis
113100
-
Tgt:tRNA complex, noncovalent mass spectrometry
Zymomonas mobilis
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Zymomonas mobilis
P28720
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
[tRNATyr]7-aminomethyl-7-carbaguanine + guanine
Tgt dimer binds specifically to a single tRNA molecule
705164
Zymomonas mobilis
[tRNATyr]-guanine + 7-aminomethyl-7-carbaguanine
-
-
-
?
Subunits
Subunits
Commentary
Organism
homodimer
noncovalent mass spectrometry, Tgt in solution
Zymomonas mobilis
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.00023
-
[tRNATyr]7-aminomethyl-7-carbaguanine
mutant K52M
Zymomonas mobilis
0.00095
-
[tRNATyr]7-aminomethyl-7-carbaguanine
mutant Y330F
Zymomonas mobilis
0.011
-
[tRNATyr]7-aminomethyl-7-carbaguanine
wild-type
Zymomonas mobilis
Cloned(Commentary) (protein specific)
Commentary
Organism
mutants introduced into plasmid pET9d-ZM4 and transformed into Escherichia coli BL21(DE3) GOLD cells
Zymomonas mobilis
Crystallization (Commentary) (protein specific)
Crystallization
Organism
mutant K52M, by hanging-drop, vapor-diffusion method and followed by macroseeding, at a resolution of 2.0 A, forms crystals under the same conditions as wild-type, while all attempts to obtain diffracting crystals from mutant Y330F are unsuccessful. Compared to wild-type, crystals of mutant K52M are very fragile and show only a limited diffraction quality
Zymomonas mobilis
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
K52M
reduced turnover value. At a concentration of protein of 0.01 mM appears almost exclusively as a homodimer as the wild-type, when the concentration of protein is lowered to a minimal value of 0.001 mM, a substantial proportion of monomer becomes evident
Zymomonas mobilis
Y330F
reduced turnover value. At a concentration of protein of 0.01 mM reveals a significant amount of monomer, when the concentration of protein is lowered to a minimal value of 0.001 mM, a substantial proportion of monomer becomes evident
Zymomonas mobilis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
6-amino-2-[(3-piperidin-1-ylpropyl)amino]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
cannot modify the structure of the dimer interface, prevents the formation of the catalytically active Tgt:tRNA complex, and can disrupt the preformed complex
Zymomonas mobilis
6-amino-4-[2-(4-methoxyphenyl)ethyl]-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
can modify the structure of the dimer interface, prevents the formation of the catalytically active Tgt:tRNA complex, and can disrupt the preformed complex
Zymomonas mobilis
6-amino-4-[2-(benzylamino)ethyl]-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
addresses a hydrophobic subpocket close to the dimer interface that may affect quarternary structure formation, prevents the formation of the catalytically active Tgt:tRNA complex, and can disrupt the preformed complex
Zymomonas mobilis
6-amino-4-[2-[(cyclohexylmethyl)amino]ethyl]-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
can modify the structure of the dimer interface, prevents the formation of the catalytically active Tgt:tRNA complex, and can disrupt the preformed complex
Zymomonas mobilis
6-amino-4-[2-[(cyclopentylmethyl)amino]ethyl]-2-(methylamino)-1,7-dihydro-8H-imidazo[4,5-g]quinazolin-8-one
addresses a hydrophobic subpocket close to the dimer interface that may affect quarternary structure formation, prevents the formation of the catalytically active Tgt:tRNA complex, and can disrupt the preformed complex
Zymomonas mobilis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.00098
-
[tRNATyr]7-aminomethyl-7-carbaguanine
mutant K52M
Zymomonas mobilis
0.00158
-
[tRNATyr]7-aminomethyl-7-carbaguanine
mutant Y330F
Zymomonas mobilis
0.00217
-
[tRNATyr]7-aminomethyl-7-carbaguanine
wild-type
Zymomonas mobilis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Zn2+
one structural Zn2+ per subunit
Zymomonas mobilis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
85600
-
expected for a Tgt dimer containing one structural Zn2+ per subunit
Zymomonas mobilis
85610
-
Tgt, noncovalent mass spectrometry
Zymomonas mobilis
113100
-
Tgt:tRNA complex, noncovalent mass spectrometry
Zymomonas mobilis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
[tRNATyr]7-aminomethyl-7-carbaguanine + guanine
Tgt dimer binds specifically to a single tRNA molecule
705164
Zymomonas mobilis
[tRNATyr]-guanine + 7-aminomethyl-7-carbaguanine
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
noncovalent mass spectrometry, Tgt in solution
Zymomonas mobilis
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.00023
-
[tRNATyr]7-aminomethyl-7-carbaguanine
mutant K52M
Zymomonas mobilis
0.00095
-
[tRNATyr]7-aminomethyl-7-carbaguanine
mutant Y330F
Zymomonas mobilis
0.011
-
[tRNATyr]7-aminomethyl-7-carbaguanine
wild-type
Zymomonas mobilis
Other publictions for EC 2.4.2.29
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
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)
735961
Barandun
Replacement of water molecules ...
Zymomonas mobilis
Chemistry
21
126-135
2015
-
-
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8
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-
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2
-
1
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2
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8
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8
8
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2
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2
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-
736521
Sawhney
Identification of Plasmodium f ...
Plasmodium falciparum
J. Biomol. Struct. Dyn.
33
2404-2420
2015
-
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-
-
-
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1
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1
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3
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1
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1
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728740
Nomura
Purification and comparison of ...
Methanosarcina acetivorans, Methanosarcina acetivorans DSM 2834
Protein Expr. Purif.
88
13-19
2013
-
-
1
-
-
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1
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1
3
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4
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1
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1
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1
1
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1
1
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1
1
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-
735359
Barandun
High-affinity inhibitors of Zy ...
Zymomonas mobilis
Acta Crystallogr. Sect. D
69
1798-1807
2013
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-
-
1
-
-
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-
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1
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2
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1
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1
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-
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-
722058
Barandun
From lin-benzoguanines to lin- ...
Zymomonas mobilis
Chemistry
18
9246-9257
2012
-
-
-
-
-
-
14
-
-
-
-
-
-
6
-
-
-
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-
-
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-
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14
-
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14
14
-
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-
721496
Eric Thomas
Differential heterocyclic subs ...
Escherichia coli, Homo sapiens
Biochem. Biophys. Res. Commun.
410
34-39
2011
-
-
-
-
4
-
4
6
-
-
-
-
-
7
-
-
-
-
-
-
-
-
2
-
2
-
-
6
2
-
-
-
10
-
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4
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4
10
6
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-
2
-
2
-
-
6
2
-
-
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-
-
-
-
6
6
706730
Chen
Characterization of the human ...
Homo sapiens
RNA
16
958-968
2010
1
-
1
-
-
-
-
-
-
-
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4
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1
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1
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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-
702263
Garcia
Identification of the rate-det ...
Escherichia coli
Biochemistry
48
11243-11251
2009
-
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-
1
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2
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1
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1
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3
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1
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2
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-
703202
Ritschel
Crystal structure analysis and ...
Zymomonas mobilis
ChemBioChem
10
716-727
2009
-
-
1
1
-
-
10
-
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2
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1
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1
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10
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10
10
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1
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1
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703213
Kohler
High-affinity inhibitors of tR ...
Zymomonas mobilis
Chemistry
15
10809-10817
2009
-
-
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1
-
-
30
-
-
-
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-
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3
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1
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11
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1
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30
11
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1
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703226
Ritschel
How to replace the residual so ...
Zymomonas mobilis
ChemMedChem
4
2012-2023
2009
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1
1
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4
4
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1
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1
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1
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4
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1
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4
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4
4
705164
Ritschel
An integrative approach combin ...
Zymomonas mobilis
J. Mol. Biol.
393
833-847
2009
-
-
1
1
2
-
5
3
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1
3
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3
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1
1
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3
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1
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1
2
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5
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3
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1
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1
1
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3
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681439
Stengl
Crystal structures of tRNA-gua ...
Zymomonas mobilis
J. Mol. Biol.
370
492-511
2007
-
1
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1
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-
18
-
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1
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4
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1
1
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17
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1
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2
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18
17
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1
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1
1
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684430
Hoertner
Potent inhibitors of tRNA-guan ...
Shigella flexneri
Angew. Chem.
46
8266-8269
2007
-
-
-
-
-
-
12
-
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-
-
3
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1
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12
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12
12
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1
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688390
Tidten
Glutamate versus glutamine exc ...
Zymomonas mobilis
J. Mol. Biol.
374
764-776
2007
-
-
1
1
1
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8
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3
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2
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8
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1
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1
1
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8
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2
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8
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689250
Hurt
Site-specific modification of ...
Escherichia coli
Nucleic Acids Res.
35
4905-4913
2007
-
-
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3
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6
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3
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3
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3
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3
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3
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678191
Todorov
Role of aspartate 143 in Esche ...
Escherichia coli
Biochemistry
45
617-625
2006
-
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10
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6
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680057
Meyer
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Synthesis, biological evaluati ...
Zymomonas mobilis
Helv. Chim. Acta
89
573-597
2006
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13
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658289
Todorov
The role of aspartic acid 143 ...
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679204
Stengl
Mechanism and substrate specif ...
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658379
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Elevated expression level of 6 ...
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2004
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644928
Brenk
Virtual screening for submicro ...
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2003
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644939
Goodenough-Lashua
tRNA-guanine transglycosylase ...
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2003
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644940
Kittendorf
An essential role for aspartat ...
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2003
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1
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658446
Brenk
Flexible adaptations in the st ...
Zymomonas mobilis
ChemBioChem
4
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2003
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4
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4
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4
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644931
Nonekowski
The Escherichia coli tRNA-guan ...
Escherichia coli, Pyrococcus horikoshii
J. Biol. Chem.
277
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2002
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644929
Ishiwata
Increased expression of queuos ...
Homo sapiens
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2001
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5
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1
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644933
Kittendorf
tRNA-guanine transglycosylase ...
Escherichia coli
Biochemistry
40
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2001
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4
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8
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8
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8
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8
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644937
Nonekowski
tRNA recognition by tRNA-guani ...
Escherichia coli
RNA
7
1432-1441
2001
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-
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644938
Kung
tRNA-guanine transglycosylase ...
Escherichia coli
RNA
6
233-244
2000
-
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-
-
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6
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644926
Kung
tRNA-guanine transglycosylase ...
Escherichia coli
FEBS Lett.
431
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1998
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644927
Romier
Slight sequence variations of ...
Caenorhabditis elegans, Haemophilus influenzae, Helicobacter pylori, Homo sapiens, Mus musculus, Shigella flexneri, Synechocystis sp., Thermotoga maritima
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Romier
Crystal structure of tRNA-guan ...
Zymomonas mobilis
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1996
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Deshpande
Cloning and characterization o ...
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326
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644932
Curnow
tRNA-guanine transglycosylase ...
Escherichia coli
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270
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644935
Hoops
Mechanism-based inactivation o ...
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Biochemistry
34
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1995
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644934
Reuter
Serine 90 is required for enzy ...
Escherichia coli
Biochemistry
33
7041-7046
1994
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644920
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tRNA-guanine transglycosylase ...
Escherichia coli
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231
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644919
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Transfer -RNA guanine transgly ...
Salmonella enterica subsp. enterica serovar Typhimurium
Period. Biol.
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321-326
1988
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644922
Haumont
Enzymatic formation of queuosi ...
Xenopus laevis
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168
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644921
Farkas
Substrate and inhibitor specif ...
Oryctolagus cuniculus
Biochim. Biophys. Acta
781
64-75
1984
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644924
Carbon
Site-directed in vitro replace ...
Xenopus laevis
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1983
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Walden
Purification and properties of ...
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257
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644925
Shindo-Okada
Transfer ribonucleic acid guan ...
Rattus norvegicus
Biochemistry
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Okada
Novel mechanism of post-transc ...
Escherichia coli
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Studies with a homogeneous enz ...
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