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Literature summary for 6.1.1.12 extracted from

  • Martin, F.; Barends, S.; Eriani, G.
    Single amino acid changes in AspRS reveal alternative routes for expanding its tRNA repertoire in vivo (2004), Nucleic Acids Res., 32, 4081-4089.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.1.1.12

Protein Variants

Protein Variants Comment Organism
A471T mutant enzyme is still able to aminoacylate the native tRNAAsp in vivo at a level sufficient to complement the defective strain CS143 Escherichia coli
D29N mutant enzyme is still able to aminoacylate the native tRNAAsp in vivo at a level sufficient to complement the defective strain CS143 Escherichia coli
E118K mutant enzyme is still able to aminoacylate the native tRNAAsp in vivo at a level sufficient to complement the defective strain CS143. 6.5fold increase in aminoacylation rate and 3fold decrease in amino acid activation reaction Escherichia coli
E93K mutant enzyme is still able to aminoacylate the native tRNAAsp in vivo at a level sufficient to complement the defective strain CS143 Escherichia coli
G90S mutant enzyme is still able to aminoacylate the native tRNAAsp in vivo at a level sufficient to complement the defective strain CS143 Escherichia coli
G90V mutant enzyme is still able to aminoacylate the native tRNAAsp in vivo at a level sufficient to complement the defective strain CS143 Escherichia coli
L30F mutant enzyme is still able to aminoacylate the native tRNAAsp in vivo at a level sufficient to complement the defective strain CS143 Escherichia coli
R383C mutant enzyme is still able to aminoacylate the native tRNAAsp in vivo at a level sufficient to complement the defective strain CS143 Escherichia coli
T89I mutant enzyme is still able to aminoacylate the native tRNAAsp in vivo at a level sufficient to complement the defective strain CS143 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.05
-
 ATP pH 7.5, 37°C, aminoacylation of tRNAAsp(QUC), mutant enzyme E93K Escherichia coli
0.091
-
 ATP pH 7.5, 37°C, aminoacylation of tRNAAsp(QUC), wild-type enzyme Escherichia coli
0.092
-
 ATP pH 7.5, 37°C, aminoacylation of tRNAAsp(QUC), mutant enzyme L30F Escherichia coli
0.1
-
 ATP pH 7.5, 37°C, aminoacylation of tRNAAsp(QUC), mutant enzyme E118K Escherichia coli
1.11
-
 ATP pH 7.5, 37°C, aminoacylation of tRNAAsp(QUC), mutant enzyme A471T Escherichia coli
1.2
-
 aspartate pH 7.5, 37°C, aminoacylation of tRNAAsp(QUC), mutant enzyme E118K Escherichia coli
1.3
-
 aspartate pH 7.5, 37°C, aminoacylation of tRNAAsp(QUC), mutant enzyme A471T Escherichia coli
1.3
-
 aspartate pH 7.5, 37°C, aminoacylation of tRNAAsp(QUC), wild-type enzyme Escherichia coli
1.4
-
 aspartate pH 7.5, 37°C, aminoacylation of tRNAAsp(QUC), mutant enzyme E93K Escherichia coli
1.4
-
 aspartate pH 7.5, 37°C, aminoacylation of tRNAAsp(QUC), mutant enzyme L30F Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-aspartate + tRNAAsp
-
 Escherichia coli AMP + diphosphate + L-aspartyl-tRNAAsp
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.05
-
 tRNAAsp pH 7.5, 37°C, aminoacylation of tRNAAsp(QUC), mutant enzyme E93K Escherichia coli
8
-
 tRNAAsp pH 7.5, 37°C, aminoacylation of tRNAAsp(QUC), mutant enzyme A471T Escherichia coli
12
-
 tRNAAsp pH 7.5, 37°C, aminoacylation of tRNAAsp(QUC), mutant enzyme L30F Escherichia coli
12
-
 tRNAAsp pH 7.5, 37°C, aminoacylation of tRNAAsp(QUC), wild-type enzyme Escherichia coli
79
-
 tRNAAsp pH 7.5, 37°C, aminoacylation of tRNAAsp(QUC), mutant enzyme E118K Escherichia coli