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Literature summary for 6.1.1.24 extracted from
- The archaeal transamidosome for RNA-dependent glutamine biosynthesis (2010), Nucleic Acids Res., 38, 5774-5783.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| GatDE | a heterodimeric amidotransferase. In the presence of GatDE at 1.8 mM, the Glu-tRNAGlu activity of ND-GluRS decreases almost in half | Methanothermobacter thermautotrophicus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methanothermobacter thermautotrophicus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| native ND-GluRS by gel filtration | Methanothermobacter thermautotrophicus |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | ND-GluRS:GatDE complex formation and structure, detailed overview | Methanothermobacter thermautotrophicus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ND-GluRS | - |
Methanothermobacter thermautotrophicus |
| non-discriminating glutamyl-tRNA synthetase | - |
Methanothermobacter thermautotrophicus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Methanothermobacter thermautotrophicus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.2 | 7.5 | assay at | Methanothermobacter thermautotrophicus |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
GatDE | apparent KI of GatDE for ND-GluRS in the Glu-tRNAGlu reaction is 31 nM | Methanothermobacter thermautotrophicus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | ND-GluRS is a class I aminoacyl-tRNA synthetase | Methanothermobacter thermautotrophicus |
| additional information | ND-GluRS:GatDE complex formation and structure, detailed overview | Methanothermobacter thermautotrophicus |
| physiological function | for synthesis of Gln-tRNAGln, a two-step process is required: the non-discriminating glutamyl-tRNA synthetase, ND-GluRS, forms Glu-tRNAGln, while the heterodimeric amidotransferase GatDE converts this mischarged tRNA to Gln-tRNAGln. A similar complex for Gln-tRNAGln formation in Methanothermobacter thermautotrophicus that allows the mischarged Glu-tRNAGln made by the tRNA synthetase to be channeled to the amidotransferase. The association of archaeal ND-GluRS with GatDE sequesters the tRNA synthetase for Gln-tRNAGln formation, with GatDE reducing the affinity of ND-GluRS for tRNAGlu by at least 13fold. The archaeal complex does not require tRNA for its formation, is not stable through product (Gln-tRNAGln) formation, and has no major effect on the kinetics of tRNAGln glutamylation nor transamidation | Methanothermobacter thermautotrophicus |
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Release 2023.1 (January 2023)
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