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