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Literature summary for 2.7.7.6 extracted from
- Transient state kinetics of transcription elongation by T7 RNA polymerase (2006), J. Biol. Chem., 281, 35677-35685.
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| nucleoside triphosphate + RNAn | Escherichia phage T7 | the single subunit DNA-dependent RNA polymerase from bacteriophage T7 catalyzes both promoterdependent transcription initiation and promoter-independent elongation | diphosphate + RNAn+1 | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia phage T7 | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| nucleoside triphosphate + RNAn | the single subunit DNA-dependent RNA polymerase from bacteriophage T7 catalyzes both promoterdependent transcription initiation and promoter-independent elongation | Escherichia phage T7 | diphosphate + RNAn+1 | - |
? | |
| nucleoside triphosphate + RNAn | T7 RNAP undergoes a slow conformational change to form an elongation competent complex with the promoter-free substrate. The complex binds to a correct NTP and incorporates the nucleoside monophosphate into RNA primer very efficiently. In the presence of inorganic pyrophosphate, the elongation complex catalyzes the reverse pyrophosphorolysis reaction at a maximum rate of 0.8 per s | Escherichia phage T7 | diphosphate + RNAn+1 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | - |
Escherichia phage T7 |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| RNAP | - |
Escherichia phage T7 |
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