Cloned (Comment) | Organism |
---|---|
expression of full length and C-terminal truncated GlnRS, lacking the the Yqey domain, and of the isolated Yqey protein, in Escherichia coli strain ER2566 | Deinococcus radiodurans |
Crystallization (Comment) | Organism |
---|---|
purified recombinant full-length GlnRS grown in microbatch in the presence of PEG 3350, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement | Deinococcus radiodurans |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | effect of the isolated Yqey domain on the kinetic properties of GlnRS, overview | Deinococcus radiodurans |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Deinococcus radiodurans |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-glutamine + tRNAGln | Deinococcus radiodurans | - |
AMP + diphosphate + L-glutaminyl-tRNAGln | - |
? | |
ATP + L-glutamine + tRNAGln | Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539 | - |
AMP + diphosphate + L-glutaminyl-tRNAGln | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Deinococcus radiodurans | P56926 | - |
- |
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539 | P56926 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
ATP + L-glutamine + tRNAGln = AMP + diphosphate + L-glutaminyl-tRNAGln | structurefunction relationship, overview | Deinococcus radiodurans |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-glutamine + tRNAGln | - |
Deinococcus radiodurans | AMP + diphosphate + L-glutaminyl-tRNAGln | - |
? | |
ATP + L-glutamine + tRNAGln | - |
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539 | AMP + diphosphate + L-glutaminyl-tRNAGln | - |
? | |
ATP + L-glutamine + tRNAGln(CUG) | - |
Deinococcus radiodurans | AMP + diphosphate + L-glutaminyl-tRNAGln(CUG) | - |
? | |
ATP + L-glutamine + tRNAGln(CUG) | - |
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539 | AMP + diphosphate + L-glutaminyl-tRNAGln(CUG) | - |
? | |
ATP + L-glutamine + tRNAGln(UUG) | - |
Deinococcus radiodurans | AMP + diphosphate + L-glutaminyl-tRNAGln(UUG) | - |
? | |
ATP + L-glutamine + tRNAGln(UUG) | - |
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539 | AMP + diphosphate + L-glutaminyl-tRNAGln(UUG) | - |
? | |
additional information | the Deinococcus radiodurans GlnRS is a structural hybrid between conventional GlnRS and AdT, EC 6.3.5.6, structurefunction relationship, the Yqey domain is involved in tRNAGln recognition and plays the role of an affinity enhancer of GlnRS for tRNAGln acting only in cis, overview | Deinococcus radiodurans | ? | - |
? | |
additional information | the Deinococcus radiodurans GlnRS is a structural hybrid between conventional GlnRS and AdT, EC 6.3.5.6, structurefunction relationship, the Yqey domain is involved in tRNAGln recognition and plays the role of an affinity enhancer of GlnRS for tRNAGln acting only in cis, overview | Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | the enzyme possesses a C-terminal extension of 215 residues appending the anticodon-binding domain, the Yqey domain, which constitutes a paralog of the Saccharomyces cerevisiae Yqey protein, structure-function relationship, the Yqey domain is involved in tRNAGln recognition and plays the role of an affinity enhancer of GlnRS for tRNAGln acting only in cis, overview | Deinococcus radiodurans |
Synonyms | Comment | Organism |
---|---|---|
GlnRS | - |
Deinococcus radiodurans |
Glutaminyl-tRNA synthetase | - |
Deinococcus radiodurans |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Deinococcus radiodurans |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.2 | - |
assay at | Deinococcus radiodurans |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Deinococcus radiodurans |