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Literature summary for 3.6.4.13 extracted from
- Establishing a mechanistic basis for the large kinetic steps of the NS3 helicase. (2009), J. Biol. Chem., 284, 2512-2521.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | low salt conditions enhance unwinding by monomeric NS3 | Hepacivirus C |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Hepacivirus C | P26663 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | unwinds RNA in a discontinuous manner, pausing after long apparent steps of unwinding. It is proposed that the large kinetic step size of NS3 unwinding reflects a delayed, periodic release of the separated RNA product strand from a secondary binding site that is located in the NTPase domain (domain II) of NS3 | Hepacivirus C | ADP + phosphate | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| DEx(H/D)RNA helicase | - |
Hepacivirus C |
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