Protein Variants | Comment | Organism |
---|---|---|
K631R | the fraction of catalytically active E form is 38% compared to 100% for the wild-type enzyme. The synthesis of long transcripts is markedly diminished for the mutant due to decreasing processivity | Escherichia phage T7 |
Y639F | the fraction of catalytically active E form is 32% compared to 100% for the wild-type enzyme | Escherichia phage T7 |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | - |
Escherichia phage T7 |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia phage T7 | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
nucleoside triphosphate + RNAn | the enzyme requires DNA as template | Escherichia phage T7 | diphosphate + RNAn+1 | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | existence of two possible conformers: E and EĀ that are in rapid equilibrium. Both forms can form the quarternary complex, but only the E form is capable of catalyzing phosphodiester bond formation | Escherichia phage T7 |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | - |
Escherichia phage T7 |