BRENDA - Enzyme Database show
show all sequences of 6.3.5.7

Rational design of an evolutionary precursor of glutaminyl-tRNA synthetase

O'Donoghue, P.; Sheppard, K.; Nureki, O.; Soell, D.; Proc. Natl. Acad. Sci. USA 108, 20485-20490 (2011)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
additional information
activity of the engineered enzyme variants indicates that the acceptor stem loop is the principle discrimination element because insertion of this loop alone enhances the specificity of the archaeal enzyme toward tRNAGln2
Methanothermobacter thermautotrophicus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
aminoacylation kinetics of enzyme variants
Methanothermobacter thermautotrophicus
0.00133
-
tRNAGln2(CUG)
pH 7.2, 37°C
Methanothermobacter thermautotrophicus
0.00361
-
tRNAGlu
pH 7.2, 37°C
Methanothermobacter thermautotrophicus
0.00539
-
tRNAGln1(UUG)
pH 7.2, 37°C
Methanothermobacter thermautotrophicus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Methanothermobacter thermautotrophicus
-
-
-
Purification (Commentary)
Commentary
Organism
-
Methanothermobacter thermautotrophicus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + L-glutamate + tRNAGln1(UUG)
the enzyme is active toward the two tRNAGln isoacceptors, but with a significant catalytic preference for tRNAGln2(CUG). The less active tRNAGln1(UUG) responds to the less common CAA codon for Gln
728668
Methanothermobacter thermautotrophicus
AMP + diphosphate + L-glutamyl-tRNAGln1(UUG)
-
-
-
?
ATP + L-glutamate + tRNAGln2(CUG)
the enzyme is active toward the two tRNAGln isoacceptors, but with a significant catalytic preference for tRNAGln2(CUG). The less active tRNAGln1(UUG) responds to the less common CAA codon for Gln. The wild-type enzyme shows a 24fold catalytic preference for tRNAGln2 over tRNAGlu
728668
Methanothermobacter thermautotrophicus
AMP + diphosphate + L-glutamyl-tRNAGln2(CUG)
-
-
-
?
ATP + L-glutamate + tRNAGlu
-
728668
Methanothermobacter thermautotrophicus
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Methanothermobacter thermautotrophicus
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
aminoacylation kinetics of enzyme variants
Methanothermobacter thermautotrophicus
0.006
-
tRNAGln1(UUG)
pH 7.2, 37°C
Methanothermobacter thermautotrophicus
0.04
-
tRNAGlu
pH 7.2, 37°C
Methanothermobacter thermautotrophicus
0.41
-
tRNAGln2(CUG)
pH 7.2, 37°C
Methanothermobacter thermautotrophicus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.2
-
assay at
Methanothermobacter thermautotrophicus
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
activity of the engineered enzyme variants indicates that the acceptor stem loop is the principle discrimination element because insertion of this loop alone enhances the specificity of the archaeal enzyme toward tRNAGln2
Methanothermobacter thermautotrophicus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
aminoacylation kinetics of enzyme variants
Methanothermobacter thermautotrophicus
0.00133
-
tRNAGln2(CUG)
pH 7.2, 37°C
Methanothermobacter thermautotrophicus
0.00361
-
tRNAGlu
pH 7.2, 37°C
Methanothermobacter thermautotrophicus
0.00539
-
tRNAGln1(UUG)
pH 7.2, 37°C
Methanothermobacter thermautotrophicus
Purification (Commentary) (protein specific)
Commentary
Organism
-
Methanothermobacter thermautotrophicus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + L-glutamate + tRNAGln1(UUG)
the enzyme is active toward the two tRNAGln isoacceptors, but with a significant catalytic preference for tRNAGln2(CUG). The less active tRNAGln1(UUG) responds to the less common CAA codon for Gln
728668
Methanothermobacter thermautotrophicus
AMP + diphosphate + L-glutamyl-tRNAGln1(UUG)
-
-
-
?
ATP + L-glutamate + tRNAGln2(CUG)
the enzyme is active toward the two tRNAGln isoacceptors, but with a significant catalytic preference for tRNAGln2(CUG). The less active tRNAGln1(UUG) responds to the less common CAA codon for Gln. The wild-type enzyme shows a 24fold catalytic preference for tRNAGln2 over tRNAGlu
728668
Methanothermobacter thermautotrophicus
AMP + diphosphate + L-glutamyl-tRNAGln2(CUG)
-
-
-
?
ATP + L-glutamate + tRNAGlu
-
728668
Methanothermobacter thermautotrophicus
AMP + diphosphate + L-glutamyl-tRNAGlu
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Methanothermobacter thermautotrophicus
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
aminoacylation kinetics of enzyme variants
Methanothermobacter thermautotrophicus
0.006
-
tRNAGln1(UUG)
pH 7.2, 37°C
Methanothermobacter thermautotrophicus
0.04
-
tRNAGlu
pH 7.2, 37°C
Methanothermobacter thermautotrophicus
0.41
-
tRNAGln2(CUG)
pH 7.2, 37°C
Methanothermobacter thermautotrophicus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.2
-
assay at
Methanothermobacter thermautotrophicus
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
aminoacylation kinetics of enzyme variants
Methanothermobacter thermautotrophicus
1.1
-
tRNAGln1(UUG)
pH 7.2, 37°C
Methanothermobacter thermautotrophicus
11
-
tRNAGlu
pH 7.2, 37°C
Methanothermobacter thermautotrophicus
308
-
tRNAGln2(CUG)
pH 7.2, 37°C
Methanothermobacter thermautotrophicus
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
aminoacylation kinetics of enzyme variants
Methanothermobacter thermautotrophicus
1.1
-
tRNAGln1(UUG)
pH 7.2, 37°C
Methanothermobacter thermautotrophicus
11
-
tRNAGlu
pH 7.2, 37°C
Methanothermobacter thermautotrophicus
308
-
tRNAGln2(CUG)
pH 7.2, 37°C
Methanothermobacter thermautotrophicus
Other publictions for EC 6.3.5.7
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 ...
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290
29629-29641
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1
1
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745612
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3669-3677
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2
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744268
Echevarria
Glutamyl-tRNAGln amidotransfe ...
Mus musculus
Biochem. J.
460
91-101
2014
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4
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1
1
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745552
Hadd
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426
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2014
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4
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Thermotoga maritima
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425
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728391
Huot
Gln-tRNAGln synthesis in a dyn ...
Helicobacter pylori
Nucleic Acids Res.
39
9306-9315
2011
1
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3
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1
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2
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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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1
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1
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1
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1
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4
4
709508
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1
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714451
Balg
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18
7868-7872
2010
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7
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4
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1
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1
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716331
Ito
Two enzymes bound to one trans ...
Thermotoga maritima
Nature
467
612-616
2010
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1
1
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716371
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Methanothermobacter thermautotrophicus
Nucleic Acids Res.
38
5774-5783
2010
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3
3
706514
Nagao
Biogenesis of glutaminyl-mt tR ...
Homo sapiens
Proc. Natl. Acad. Sci. USA
106
16209-16214
2009
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692759
Balg
Inhibition of Helicobacter pyl ...
Helicobacter pylori
J. Am. Chem. Soc.
130
3264-3265
2008
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673689
Namgoong
Co-evolution of the archaeal t ...
Methanothermobacter thermautotrophicus
FEBS Lett.
581
309-314
2007
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674787
Sheppard
The Helicobacter pylori amidot ...
Helicobacter pylori
J. Biol. Chem.
282
11866-11873
2007
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3
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7
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2
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9
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662450
Feng
Gln-tRNAGln formation from Glu ...
Methanothermobacter thermautotrophicus
J. Biol. Chem.
280
8150-8155
2005
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1
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7
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7
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1
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492304
Harpel
Mutagenesis and mechanism-base ...
Streptococcus pyogenes
Biochemistry
41
6398-6407
2002
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3
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1
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1
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492305
Kwak
Expression, purification, and ...
Geobacillus stearothermophilus
Mol. Cells
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374-381
2002
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492302
Horiuchi
Mechanistic studies of reactio ...
Streptococcus pyogenes
Biochemistry
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2001
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492308
Salazar
A dual-specific Glu-tRNA(Gln) ...
Acidithiobacillus ferrooxidans
FEBS Lett.
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129-131
2001
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492303
Curnow
Glu-tRNAGln amidotransferase: ...
Bacillus subtilis
Proc. Natl. Acad. Sci. USA
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1997
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Vothknecht
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Charging of both, plastidial t ...
Tetradesmus obliquus
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Jahn
Purification and functional ch ...
Chlamydomonas reinhardtii
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8059-8064
1990
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Strauch
Characterization of the glutam ...
Bacillus subtilis
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1988
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492307
Zalkin
Glu-tRNAGln amidotransferase ...
Bacillus subtilis
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1985
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