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Literature summary extracted from
- Characterization of a urea induced molten globule intermediate state of glutaminyl-tRNA synthetase from Escherichia coli (1995), Biochemistry, 34, 5242-5247.
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 6.1.1.18 | Escherichia coli | - |
- |
- |
Renatured (Commentary)
| EC Number | Renatured (Comment) | Organism |
|---|---|---|
| 6.1.1.18 | urea induces equilibrium denaturation of glutaminyl-tRNA synthetase, existence of a stable intermediate state at around 2 M urea, existence of an induced molten globule state in a large multidomain protein which is separated from the native and the denatured protein by high activation energy barriers | Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 6.1.1.18 | ATP + L-glutamine + tRNAGln | - |
Escherichia coli | AMP + diphosphate + L-glutaminyl-tRNAGln | - |
? |  |
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