BRENDA - Enzyme Database
show all sequences of 6.1.1.24

A single glutamyl-tRNA synthetase aminoacylates tRNAGlu and tRNAGln in Bacillus subtilis and efficiently misacylates Escherichia coli tRNA1Gln in vitro

Lapointe, J.; Duplain, L.; Proulx, M.; J. Bacteriol. 165, 88-93 (1986)

Data extracted from this reference:

KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.00045
-
tRNAGln
homologous tRNAGln, in absence of regulatory factor beta
Bacillus subtilis
0.00065
-
tRNAGln
homologous tRNAGln, in presence of regulatory factor beta
Bacillus subtilis
0.00083
-
tRNAGlu
homologous tRNAGlu, in absence of regulatory factor beta
Bacillus subtilis
0.0014
-
tRNAGlu
homologous tRNAGlu, in presence of regulatory factor beta
Bacillus subtilis
0.0015
-
tRNAGln
tRNAGln
Bacillus subtilis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + L-glutamate + tRNAGlx
Bacillus subtilis
the enzyme is responsible for the in vivo aminoacylation of both tRNAGlu and tRNAGln in Bacillus subtilis
AMP + diphosphate + Glu-tRNAGlx
-
Bacillus subtilis
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bacillus subtilis
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + L-glutamate + tRNAGln
the enzyme aminoacylates tRNAGLU and tRNASGln in Bacillus subtilis and efficiently misacylates Escherichia coli tRNA1Gln in vitro
492293
Bacillus subtilis
AMP + diphosphate + Glu-tRNAGln
-
-
-
-
ATP + L-glutamate + tRNAGlu
the enzyme aminoacylates tRNAGlu and tRNAsGln in Bacillus subtilis and efficiently misacylates Escherichia coli tRNA1Gln in vitro, not tRNA2Gln from Escherichia coli or tRNAGlu from Escherichia coli
492293
Bacillus subtilis
AMP + diphosphate + Glu-tRNAGlu
-
492293
Bacillus subtilis
?
ATP + L-glutamate + tRNAGlu
the enzyme interacts with the G64-C50 or G64-U50 in the Tpsi stem of its tRNA substrate
492293
Bacillus subtilis
AMP + diphosphate + Glu-tRNAGlu
-
492293
Bacillus subtilis
?
ATP + L-glutamate + tRNAGlx
the enzyme is responsible for the in vivo aminoacylation of both tRNAGlu and tRNAGln in Bacillus subtilis
492293
Bacillus subtilis
AMP + diphosphate + Glu-tRNAGlx
-
492293
Bacillus subtilis
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.04
-
tRNAGln
homologous tRNAGln
Bacillus subtilis
0.05
-
tRNAGlu
homologous tRNAGlu
Bacillus subtilis
0.07
-
tRNAGln
tRNAGln from E. coli
Bacillus subtilis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.00045
-
tRNAGln
homologous tRNAGln, in absence of regulatory factor beta
Bacillus subtilis
0.00065
-
tRNAGln
homologous tRNAGln, in presence of regulatory factor beta
Bacillus subtilis
0.00083
-
tRNAGlu
homologous tRNAGlu, in absence of regulatory factor beta
Bacillus subtilis
0.0014
-
tRNAGlu
homologous tRNAGlu, in presence of regulatory factor beta
Bacillus subtilis
0.0015
-
tRNAGln
tRNAGln
Bacillus subtilis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + L-glutamate + tRNAGlx
Bacillus subtilis
the enzyme is responsible for the in vivo aminoacylation of both tRNAGlu and tRNAGln in Bacillus subtilis
AMP + diphosphate + Glu-tRNAGlx
-
Bacillus subtilis
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + L-glutamate + tRNAGln
the enzyme aminoacylates tRNAGLU and tRNASGln in Bacillus subtilis and efficiently misacylates Escherichia coli tRNA1Gln in vitro
492293
Bacillus subtilis
AMP + diphosphate + Glu-tRNAGln
-
-
-
-
ATP + L-glutamate + tRNAGlu
the enzyme aminoacylates tRNAGlu and tRNAsGln in Bacillus subtilis and efficiently misacylates Escherichia coli tRNA1Gln in vitro, not tRNA2Gln from Escherichia coli or tRNAGlu from Escherichia coli
492293
Bacillus subtilis
AMP + diphosphate + Glu-tRNAGlu
-
492293
Bacillus subtilis
?
ATP + L-glutamate + tRNAGlu
the enzyme interacts with the G64-C50 or G64-U50 in the Tpsi stem of its tRNA substrate
492293
Bacillus subtilis
AMP + diphosphate + Glu-tRNAGlu
-
492293
Bacillus subtilis
?
ATP + L-glutamate + tRNAGlx
the enzyme is responsible for the in vivo aminoacylation of both tRNAGlu and tRNAGln in Bacillus subtilis
492293
Bacillus subtilis
AMP + diphosphate + Glu-tRNAGlx
-
492293
Bacillus subtilis
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.04
-
tRNAGln
homologous tRNAGln
Bacillus subtilis
0.05
-
tRNAGlu
homologous tRNAGlu
Bacillus subtilis
0.07
-
tRNAGln
tRNAGln from E. coli
Bacillus subtilis
Other publictions for EC 6.1.1.24
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)
745335
Mailu
Plasmodium apicoplast Gln-tRN ...
Plasmodium falciparum
J. Biol. Chem.
290
29629-29641
2015
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1
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4
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1
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2
2
-
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-
728399
Liao
Trans-kingdom rescue of Gln-tR ...
Saccharomyces cerevisiae
Nucleic Acids Res.
40
9171-9181
2012
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713616
Ito
Structure of nondiscriminating ...
Thermotoga maritima
Acta Crystallogr. Sect. D
66
813-820
2010
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1
1
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1
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1
1
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714207
Rodriguez-Hernandez
Synthesis of Glu-tRNAGln by en ...
Escherichia coli, Methanothermobacter thermautotrophicus
Biochemistry
49
6727-6736
2010
-
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2
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6
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8
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1
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6
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6
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8
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2
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6
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1
1
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3
3
716371
Rampias
The archaeal transamidosome fo ...
Methanothermobacter thermautotrophicus
Nucleic Acids Res.
38
5774-5783
2010
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1
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5
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1
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1
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3
3
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716375
Nureki
Structure of an archaeal non-d ...
Methanothermobacter thermautotrophicus
Nucleic Acids Res.
38
7286-7297
2010
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-
1
1
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5
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2
2
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1
1
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693653
Blaise
Crystal structure of glutamyl- ...
Escherichia coli
J. Mol. Biol.
381
1224-1237
2008
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1
1
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3
1
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694903
Bullock
A rationally engineered misacy ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
105
7428-7433
2008
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1
1
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3
-
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2
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1
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2
1
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675400
Schulze
Crystal structure of a non-dis ...
Thermosynechococcus elongatus
J. Mol. Biol.
361
888-897
2006
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1
1
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5
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1
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2
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651337
Nunez
In vivo formation of glutamyl- ...
Acidithiobacillus ferrooxidans, Helicobacter pylori
FEBS Lett.
557
133-135
2004
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2
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659687
Baick
Growth inhibition of Escherich ...
Bacillus subtilis
J. Microbiol.
42
111-116
2004
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1
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659722
Lee
Divergent anticodon recognitio ...
Helicobacter pylori, Helicobacter pylori ATCC 700392
J. Mol. Biol.
344
1167-1174
2004
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2
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660346
Salazar
Coevolution of an aminoacyl-tR ...
Acidithiobacillus ferrooxidans, Acidithiobacillus ferrooxidans GluRS1, Acidithiobacillus ferrooxidans GluRS2, Helicobacter pylori, Helicobacter pylori GluRS2
Proc. Natl. Acad. Sci. USA
100
13863-13868
2003
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12
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12
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492290
Kim
Major identity element of glut ...
Bacillus subtilis
Mol. Cells
8
459-465
1998
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492295
Pelchat
Overproduction of the Bacillus ...
Bacillus subtilis
Can. J. Microbiol.
44
378-381
1998
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492292
Freist
Glutamyl-tRNA synthetase ...
Bacillus subtilis, Geobacillus stearothermophilus, Sinorhizobium meliloti
Biol. Chem.
378
1313-1329
1997
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3
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492291
Vothknecht
-
Charging of both, plastidial t ...
Tetradesmus obliquus
Z. Naturforsch. C
50
789-795
1995
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230
Schn
-
tRNA specificity of a mischarg ...
Hordeum vulgare
FEBS Lett.
228
241-244
1988
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492293
Lapointe
A single glutamyl-tRNA synthet ...
Bacillus subtilis
J. Bacteriol.
165
88-93
1986
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5
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1
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