EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.7.7.6 | D421A | mutation results in an enzyme with reduced activity and altered patterns of transcription | Escherichia phage T7 |
2.7.7.6 | D421T | mutation results in an enzyme with reduced activity and altered patterns of transcription | Escherichia phage T7 |
2.7.7.6 | E813A/D814A | significantly decreased elongation rate, the mutation changes the effect of diphosphate on the 3'-5'-exonuclease reaction, whose addition stimulates the production of UMP through hydrolysis rather than of UTP through diphosphorolysis. The mutation makes the 3'-exonuclease activity independent of TTP. The mutation changes the response of TEC to diphosphate: instead of causing diphosphorolysis it stimulates the exonuclease reaction | Escherichia coli |
2.7.7.6 | N458A | significantly decreased elongation rate | Escherichia coli |
2.7.7.6 | R1106A | significantly decreased elongation rate, enhanced exonuclease activity | Escherichia coli |
2.7.7.6 | R423A | mutation results in an enzyme with reduced activity and altered patterns of transcription | Escherichia phage T7 |
2.7.7.6 | R423K | mutation results in an enzyme with reduced activity and altered patterns of transcription | Escherichia phage T7 |
2.7.7.6 | R425K | mutation results in an enzyme with reduced activity and altered patterns of transcription | Escherichia phage T7 |
2.7.7.6 | W422A | mutation results in an enzyme that has nearly normal levels of activity and exhibits patterns of transcription that are similar to that of the wild-type enzyme | Escherichia phage T7 |
2.7.7.6 | W422F | mutation results in an enzyme that has nearly normal levels of activity and exhibits patterns of transcription that are similar to that of the wild-type enzyme | Escherichia phage T7 |
2.7.7.6 | W422R | mutation results in an enzyme that has nearly normal levels of activity and exhibits patterns of transcription that are similar to that of the wild-type enzyme | Escherichia phage T7 |
2.7.7.6 | W422S | mutation results in an enzyme that has nearly normal levels of activity and exhibitspatterns of transcription that arew similar to that of the wild-type enzyme | Escherichia phage T7 |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.7.7.6 | 0.0095 | - |
ATP | pH 7.9, 37°C, wild-type enzyme | Escherichia phage T7 | |
2.7.7.6 | 0.016 | - |
ATP | pH 7.9, 37°C, mutant enzyme W422A | Escherichia phage T7 | |
2.7.7.6 | 0.036 | - |
ATP | pH 7.9, 37°C, mutant enzyme Y427A | Escherichia phage T7 | |
2.7.7.6 | 0.067 | - |
ATP | pH 7.9, 37°C, mutant enzyme D421A | Escherichia phage T7 | |
2.7.7.6 | 0.137 | - |
ATP | pH 7.9, 37°C, mutant enzyme R423A | Escherichia phage T7 | |
2.7.7.6 | 0.282 | - |
ATP | pH 7.9, 37°C, mutant enzyme R425K | Escherichia phage T7 | |
2.7.7.6 | 0.384 | - |
ATP | pH 7.9, 37°C, mutant enzyme R425A | Escherichia phage T7 |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.7.7.6 | Mg2+ | the active center of the enzyme involves a symmetrical pair of Mg2+ ions that switch roles in synthesis and degradation. One ion is retained permanently and the other is recruited ad hoc for each act of catalysis. The weakly bound Mg2+ is stabilized in the active center in different modes depending on the type of reaction: during synthesis by the beta,gamma-phosphates of the incoming substrate and during hydrolysis by the phosphates of a non-base-paired nucleoside triphosphate | Escherichia coli |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.7.7.6 | Escherichia coli | - |
- |
- |
2.7.7.6 | Escherichia phage T7 | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.7.6 | ATP + RNAn | - |
Escherichia phage T7 | diphosphate + RNAn+1 | - |
? | |
2.7.7.6 | nucleoside triphosphate + RNAn | the enzyme requires DNA as template | Escherichia coli | diphosphate + RNAn+1 | - |
? | |
2.7.7.6 | nucleoside triphosphate + RNAn | the enzyme requires DNA as template | Escherichia phage T7 | diphosphate + RNAn+1 | - |
? |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.7.7.6 | 0.00065 | - |
ATP | pH 7.9, 37°C, mutant enzyme R425A | Escherichia phage T7 | |
2.7.7.6 | 0.0013 | - |
ATP | pH 7.9, 37°C, mutant enzyme R423A | Escherichia phage T7 | |
2.7.7.6 | 0.005 | - |
ATP | pH 7.9, 37°C, mutant enzyme D421A | Escherichia phage T7 | |
2.7.7.6 | 0.0135 | - |
ATP | pH 7.9, 37°C, mutant enzyme R425K | Escherichia phage T7 | |
2.7.7.6 | 0.253 | - |
ATP | pH 7.9, 37°C, mutant enzyme Y427A | Escherichia phage T7 | |
2.7.7.6 | 0.35 | - |
ATP | pH 7.9, 37°C, mutant enzyme W422A | Escherichia phage T7 | |
2.7.7.6 | 0.482 | - |
ATP | pH 7.9, 37°C, wild-type enzyme | Escherichia phage T7 |