Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 6.3.5.7 extracted from

  • O'Donoghue, P.; Sheppard, K.; Nureki, O.; Soell, D.
    Rational design of an evolutionary precursor of glutaminyl-tRNA synthetase (2011), Proc. Natl. Acad. Sci. USA, 108, 20485-20490.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.3.5.7

Protein Variants

Protein Variants Comment 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 Comment 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 UniProt Comment Textmining
Methanothermobacter thermautotrophicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Methanothermobacter thermautotrophicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 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 Methanothermobacter thermautotrophicus AMP + diphosphate + L-glutamyl-tRNAGln2(CUG)
-
 ?
ATP + L-glutamate + tRNAGlu
-
 Methanothermobacter thermautotrophicus AMP + diphosphate + L-glutamyl-tRNAGlu
-
 ?

Synonyms

Synonyms Comment Organism
GluRS
-
 Methanothermobacter thermautotrophicus
nondiscriminating GluRS
-
 Methanothermobacter thermautotrophicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Methanothermobacter thermautotrophicus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment 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 Comment 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 Comment 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