EC Number   |
Inhibitors |
Structure |
|---|
   5.6.2.3 | (5'R)-8,5'-cyclo-2'-deoxyguanosine |
the enzyme is strongly inhibited by (5'R)-8,5'-cyclo-2'-deoxyguanosine in the non-translocating strand |
   |
| 5.6.2.3 | (5'S)-8,5'-cyclo-2'-deoxyguanosine |
the enzyme is strongly inhibited by (5'S)-8,5'-cyclo-2'-deoxyguanosine in the non-translocating strand. At 40 nM enzyme, less than 10% of the forked duplex with (5'S)-8,5'-cyclo-2'-deoxyguanosine in the nontranslocating strand is unwound compared to 60% of the control forked duplex or the substrate with (5'S)-8,5'-cyclo-2'-deoxyguanosine in the translocating strand |
|
| 5.6.2.3 | adenosine 5 O-(3-thiotriphosphate) |
inhibits ATP hydrolysis activity by more than 98% |
|
| 5.6.2.3 | ADP |
at a concentration of 2 mM ATP, DNA helicase activity is inhibited 30% by 2 mM ADP |
|
| 5.6.2.3 | ATP |
substrate with optimal concentration range between 1 and 2 mM. At high concentrations inhibition of activity can be observed |
|
| 5.6.2.3 | ATPgammaS |
- |
|
| 5.6.2.3 | ATPgammaS |
at a concentration of 2 mM ATP, DNA helicase activity is inhibited 38 and 73% by 0.2 and 2 mM ATPgammaS, respectively |
|
| 5.6.2.3 | benzoquinoquinoxaline |
BQQ, inhibits ChlR1 triplex DNA unwinding activity |
|
| 5.6.2.3 | dATP |
substrate with optimal concentration range between 1 and 2 mM. At high concentrations inhibition of activity can be observed |
|
| 5.6.2.3 | double-strand DNA binding protein |
- |
|
