BRENDA - Enzyme Database
show all sequences of 6.1.1.17

ATP binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding

Sekine, S.; Nureki, O.; Dubois, D.Y.; Bernier, S.; Chenevert, R.; Lapointe, J.; Vassylyev, D.G.; Yokoyama, S.; EMBO J. 22, 676-688 (2003)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
crystallization of the enzyme in different complexes: 1. non-productively complexed with ATP and L-glutamate, 2. with ATP, 3. with tRNAGlu and ATP, 4. with tRNAGlu and the glutamyl-AMP analogue glutamol-AMP, hanging-drop method, 0.008 ml of 5.0 mg/ml protein in 10 mM Na-MOPS, pH 6.5, 5 mM MgCl2, 2.5 mM 2-mercaptoethanol, 1% PEG 6000, 1-2 mM ATP and/or 2 mM glutamate and/or 0.5 mM glutamol-AMP, plus 1 ml reservoir solution containing 10% PEG 6000 at 4 or 20°C, 3 days or more, X-ray diffraction structure determination at 1.8 A resolution, molecular replacement, and analysis
Thermus thermophilus
Inhibitors
Inhibitors
Commentary
Organism
Structure
glutamol-AMP
competitive inhibition
Thermus thermophilus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Thermus thermophilus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + L-glutamate + tRNAGlu
Thermus thermophilus
-
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Thermus thermophilus
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Thermus thermophilus
P27000
-
-
Reaction
Reaction
Commentary
Organism
ATP + L-glutamate + tRNAGlu = AMP + diphosphate + L-glutamyl-tRNAGlu
catalytic site structure, substrate binding and reaction mechanism
Thermus thermophilus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + L-glutamate + tRNAGlu
-
651000
Thermus thermophilus
AMP + diphosphate + L-glutamyl-tRNAGlu
-
651000
Thermus thermophilus
?
ATP + L-glutamate + tRNAGlu
tRNAGlu binding causes conformational changes in the enzyme, glutamine binding mechanism, in presence or absence of tRNA
651000
Thermus thermophilus
AMP + diphosphate + L-glutamyl-tRNAGlu
-
651000
Thermus thermophilus
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
65
-
assay at
Thermus thermophilus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Thermus thermophilus
Cofactor
Cofactor
Commentary
Organism
Structure
ATP
binding mechanism, in presence or absence of tRNA
Thermus thermophilus
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.0012
-
glutamol-AMP
pH 7.5, 65°C
Thermus thermophilus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
ATP
binding mechanism, in presence or absence of tRNA
Thermus thermophilus
Crystallization (Commentary) (protein specific)
Crystallization
Organism
crystallization of the enzyme in different complexes: 1. non-productively complexed with ATP and L-glutamate, 2. with ATP, 3. with tRNAGlu and ATP, 4. with tRNAGlu and the glutamyl-AMP analogue glutamol-AMP, hanging-drop method, 0.008 ml of 5.0 mg/ml protein in 10 mM Na-MOPS, pH 6.5, 5 mM MgCl2, 2.5 mM 2-mercaptoethanol, 1% PEG 6000, 1-2 mM ATP and/or 2 mM glutamate and/or 0.5 mM glutamol-AMP, plus 1 ml reservoir solution containing 10% PEG 6000 at 4 or 20°C, 3 days or more, X-ray diffraction structure determination at 1.8 A resolution, molecular replacement, and analysis
Thermus thermophilus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
glutamol-AMP
competitive inhibition
Thermus thermophilus
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.0012
-
glutamol-AMP
pH 7.5, 65°C
Thermus thermophilus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Thermus thermophilus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + L-glutamate + tRNAGlu
Thermus thermophilus
-
AMP + diphosphate + L-glutamyl-tRNAGlu
-
Thermus thermophilus
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + L-glutamate + tRNAGlu
-
651000
Thermus thermophilus
AMP + diphosphate + L-glutamyl-tRNAGlu
-
651000
Thermus thermophilus
?
ATP + L-glutamate + tRNAGlu
tRNAGlu binding causes conformational changes in the enzyme, glutamine binding mechanism, in presence or absence of tRNA
651000
Thermus thermophilus
AMP + diphosphate + L-glutamyl-tRNAGlu
-
651000
Thermus thermophilus
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
65
-
assay at
Thermus thermophilus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Thermus thermophilus
Other publictions for EC 6.1.1.17
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)
745339
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10824-10835
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1
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2
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745867
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6
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5
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3
2
2
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2
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2
7
7
2
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744531
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745395
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Pseudomonas aeruginosa, Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
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20
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1
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1
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1
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1
1
746179
Blais
tRNAGlu increases the affinit ...
Escherichia coli
PLoS ONE
10
e0121043
2015
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1
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2
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743955
Chongdar
Preliminary X-ray crystallogr ...
Escherichia coli
Acta Crystallogr. Sect. F
70
922-927
2014
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1
1
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1
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6
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745552
Hadd
Coevolution of specificity de ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 / S288c
J. Mol. Biol.
426
3619-3633
2014
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4
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2
2
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2
2
727963
Mailu
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Plasmodium falciparum
J. Biol. Chem.
288
32539-32552
2013
1
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1
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2
6
1
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2
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6
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6
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1
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6
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6
6
728154
Grant
The structure of yeast glutami ...
Methanobacterium thermoautotrophicus
J. Mol. Biol.
425
2480-2493
2013
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727429
Pedroni
Babesia bovis: a bipartite sig ...
Babesia bovis
Exp. Parasitol.
131
261-266
2012
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2
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1
1
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4
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1
1
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728668
O'Donoghue
Rational design of an evolutio ...
Methanothermobacter thermautotrophicus
Proc. Natl. Acad. Sci. USA
108
20485-20490
2011
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1
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4
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3
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3
3
705182
Black Pyrkosz
Exit strategies for charged tR ...
Thermus thermophilus
J. Mol. Biol.
397
1350-1371
2010
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713616
Ito
Structure of nondiscriminating ...
Thermotoga maritima, Thermotoga maritima TM1351
Acta Crystallogr. Sect. D
66
813-820
2010
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1
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1
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714031
Katz
Redox status affects the catal ...
Acidithiobacillus ferrooxidans
Biochem. Biophys. Res. Commun.
398
51-55
2010
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1
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2
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2
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2
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1
1
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1
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3
3
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714451
Balg
Inhibition of Helicobacter pyl ...
Helicobacter pylori
Bioorg. Med. Chem.
18
7868-7872
2010
-
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7
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4
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7
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7
7
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1
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702120
Saha
A chimaeric glutamyl:glutaminy ...
Escherichia coli
Biochem. J.
417
449-455
2009
-
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1
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1
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5
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702746
Paul
Glutamyl tRNA synthetases and ...
Schizosaccharomyces pombe
Biosci. Biotechnol. Biochem.
73
1339-1347
2009
-
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2
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1
1
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703636
Paravisi
Kinetic and mechanistic charac ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
FEBS J.
276
1398-1417
2009
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1
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1
2
3
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1
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3
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1
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3
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703714
Dasgupta
The role of the catalytic doma ...
Escherichia coli
FEBS Lett.
583
2114-2120
2009
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1
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1
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705976
Chang
Recognition of tRNAGln by Heli ...
Helicobacter pylori
Nucleic Acids Res.
37
6942-6949
2009
-
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706514
Nagao
Biogenesis of glutaminyl-mt tR ...
Homo sapiens
Proc. Natl. Acad. Sci. USA
106
16209-16214
2009
-
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2
1
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2
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2
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Regulation of a glutamyl-tRNA ...
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Structures of the interacting ...
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Luque
Regulated expression of glutam ...
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Structural basis of yeast amin ...
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Sekine
Structural bases of transfer R ...
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Role of Arc1p in the modulatio ...
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Glutamylsulfamoyladenosine and ...
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2005
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Blaise
A minimalist glutamyl-tRNA syn ...
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Dubois
An aminoacyl-tRNA synthetase-l ...
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Proc. Natl. Acad. Sci. USA
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2004
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660376
Salazar
A truncated aminoacyl-tRNA syn ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
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7536-7541
2004
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Sekine
ATP binding by glutamyl-tRNA s ...
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653391
Santoro
An archaebacteria-derived glut ...
Aeropyrum pernix, Archaeoglobus fulgidus, Methanocaldococcus jannaschii, Methanococcus thermoautotrophicum, Methanosarcina mazei, Pyrococcus horikoshii, Saccharolobus solfataricus
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Salazar
Coevolution of an aminoacyl-tR ...
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Pelchat
In vivo and in vitro processin ...
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Major identity element of glut ...
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Cloning of the cDNA for glutam ...
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The catalytic mechanism of the ...
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The Monomeric glutamyl-tRNA sy ...
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Kern
The glutamyl-tRNA synthetase o ...
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501-515
1979
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4
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218
Kern
Glutamyl transfer ribonucleic ...
Escherichia coli
Biochemistry
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5819-5826
1979
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Monomeric structure of glutamy ...
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1978
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Lapointe
Glutamyl transfer ribonucleic ...
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4966-4974
1972
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3
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212
Lapointe
Glutamyl transfer ribonucleic ...
Escherichia coli
J. Biol. Chem.
247
4975-4981
1972
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213
Lapointe
Glutamyl transfer ribonucleic ...
Escherichia coli
J. Biol. Chem.
247
4982-4985
1972
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7
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1
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7
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214
Lea
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Stereospecificity of glutamyl- ...
Caesalpinia bondue, Hemerocallis fulva, Vigna radiata var. radiata
Phytochemistry
11
2129-2138
1972
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3
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8
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1
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10
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3
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8
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