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Literature summary for 3.1.26.5 extracted from
- Substrate recognition of pre-tRNA by ribonuclease P-subsite model of natural ribozyme originated from Escherichia coli (2009), Nucleic Acids Symp. Ser., 53, 35-36.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| pre-tRNA + H2O | a pre-tRNA is trapped on the CCA site and 5'-leader site first to form the Michaelis-complex. On this step, the shape of a substrate RNA is not recognized by the enzyme. After that, the T-arm site and the bottom half site cooperatively examine the shape of the substrate to achieve the transition state conformation. After the cleavage of the 5'-leader sequence, the enzyme-product complex turns to the non-transition state conformation, and the cleaved product is released from the enzyme | Escherichia coli | tRNA + RNA sequence | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ribonuclease P | - |
Escherichia coli |
| RNase P | - |
Escherichia coli |
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