Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of constructed a chimaeric protein, cGluGlnRS, consisting of the catalytic domain, GluRS, and the anticodon binding domain of Escherichia coli GlnRS. cGluGlnRS shows detectable activity of glutamylation of Escherichia coli tRNAGlu and is capable of complementing an Escherichia coli temperature-sensitive GluRS strain at non-permissive temperatures. Both cGluGlnRS and N-terminal residues 1-314 of GluRS bind Escherichia coli tRNAglu with native GluRS-like affinity, suggesting that the anticodon-binding domain in cGluGlnRS enhances kcat for glutamylation. The kcat value of cGluGlnRS is approx. 500fold lower than that of GluRS, whereas the Km value is only moderately higher at the same solution conditions | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0019 | - |
tRNAGlu | wild-type | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P04805 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-glutamate + tRNAGlu | - |
Escherichia coli | AMP + diphosphate + L-glutamyl-tRNAGlu | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0058 | - |
tRNAGlu | wild-type | Escherichia coli |