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Literature summary for 6.1.1.18 extracted from
- Synthesis of beta-ketophosphonate analogs of glutamyl and glutaminyl adenylate, and selective inhibition of the corresponding bacterial aminoacyl-tRNA synthetases (2007), Bioorg. Med. Chem., 15, 295-304.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Glu-AMS | - |
Escherichia coli |  |
| glutaminyl-beta-ketophosphonate-adenosine | i.e. Gln-KPA, selective, competitive inhibition of GlnRS, contrast, Gln-KPA inhibits GlnRS by binding competitively but weakly at two distinct sites on the enzyme, the glutamine and the AMP modules of Gln-KPA, connected by the beta-ketophosphonate linker, cannot bind GlnRS simultaneously, and that one Gln-KPA molecule binds the AMP-binding site of GlnRS through its AMP module, whereas another Gln-KPA molecule binds the glutamine-binding site through its glutamine module, mechanism, overview | Escherichia coli | |
| glutamyl-beta-ketophosphonate-adenosine | i.e. Glu-KPA, competitive inhibition, non-cognate, binds weakly at one site on the monomeric enzyme | Escherichia coli | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | - |
Escherichia coli | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 64200 | - |
1 * 64200, recombinant His6-tagged GlnRS, SDS-PAGE | Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-glutamine + tRNAGln | Escherichia coli | - |
AMP + diphosphate + L-glutaminyl-tRNAGln | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-glutamine + tRNAGln | - |
Escherichia coli | AMP + diphosphate + L-glutaminyl-tRNAGln | - |
r | |
| ATP + L-glutamine + tRNAGln | a two-step reaction | Escherichia coli | AMP + diphosphate + L-glutaminyl-tRNAGln | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 64200, recombinant His6-tagged GlnRS, SDS-PAGE | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GlnRS | - |
Escherichia coli |
| Glutaminyl-tRNA synthetase | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.2 | - |
assay at | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Escherichia coli | |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | inhibition kinetics | Escherichia coli | |
| 0.65 | - |
glutaminyl-beta-ketophosphonate-adenosine | pH 7.2, 37°C, versus L-glutamine | Escherichia coli | |
| 2.8 | - |
glutamyl-beta-ketophosphonate-adenosine | pH 7.2, 37°C, versus L-glutamine | Escherichia coli | |
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