Crystallization (Comment) | Organism |
---|---|
of enzyme complexed with its cognate tRNA | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
P555S | thermosensitive mutant, resulting in substitution of Pro 555 by Ser. Pro555Ser lowers the stability of the functional configuration of both the acylation and the amino acid activation sites but has no significant effect on substrate binding | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0006 | - |
tRNAAsp | wild-type enzyme | Escherichia coli | |
0.06 | - |
Asp | wild-type enzyme | Escherichia coli | |
0.09 | - |
ATP | wild-type enzyme | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
overproducing strain, wild-type and thermosensitive mutant, resulting in substitution of Pro555 by Ser | - |
Purification (Comment) | Organism |
---|---|
- |
Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-aspartate + tRNAAsp | - |
Escherichia coli | AMP + diphosphate + L-aspartyl-tRNAAsp | - |
? |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
thermosensitive mutant, resulting in substitution of Pro 555 by Ser | Escherichia coli |
42 | - |
half-life: 22 min for tRNA aminoacylation, 68 min for ATP/diphosphate exchange | Escherichia coli |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
2 | 8 | Asp | mutant enzyme | Escherichia coli | |
18 | - |
Asp | wild-type enzyme | Escherichia coli |