Crystallization (Comment) | Organism |
---|---|
cocrystallization of the purified enzyme with tRNAGln and inhibitor QSI, X-ray diffraction structure determination at 2.4 A resolution and analysis | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
5'-O-[N-(L-glutaminyl)sulfamoyl] adenosine | i.e. QSI, glutaminyl-adenylate analogue, competitive to glutamine | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-glutamine + tRNAGln | Escherichia coli | - |
AMP + diphosphate + L-glutaminyl-tRNAGln | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P00962 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
ATP + L-glutamine + tRNAGln = AMP + diphosphate + L-glutaminyl-tRNAGln | aminoacylation reaction mechanism, substrate binding sites, Tyr211 and a water molecule are responsible for recognition of both hydrogen atoms of the nitrogen of glutamine sidechain, which is esstial for substrate recognition | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-glutamine + tRNAGln | - |
Escherichia coli | AMP + diphosphate + L-glutaminyl-tRNAGln | - |
? |
Synonyms | Comment | Organism |
---|---|---|
GlnRS | - |
Escherichia coli |
Glutaminyl-tRNA synthetase | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Escherichia coli |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0013 | - |
5'-O-[N-(L-glutaminyl)sulfamoyl] adenosine | pH 7.0, 37°C | Escherichia coli |