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Literature summary for 3.6.4.13 extracted from
- Further characterization of the helicase activity of eIF4A. Substrate specificity (2001), J. Biol. Chem., 276, 12598-12608.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Oryctolagus cuniculus | P29562 | - |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| reticulocyte | - |
Oryctolagus cuniculus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | eIF4A may interact directly with double-stranded RNA, and recognition of helicase substrates occurs via chemical and/or structural features of the duplex. The initial rate and amplitude of duplex unwinding by eIF4A is dependent on the overall stability, rather than the length or sequence, of the duplex substrate. eIF4A helicase activity is minimally dependent on the length of the single-stranded region adjacent to the double-stranded region of the substrate. Interestingly, eIF4A is able to unwind blunt-ended duplexes. eIF4A helicase activity is also affected by substitution of 2'-OH (RNA) groups with 2'-H (DNA) or 2'-methoxyethyl groups | Oryctolagus cuniculus | ADP + phosphate | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| eIF4A | - |
Oryctolagus cuniculus |
| eIF4A helicase | - |
Oryctolagus cuniculus |
| eukaryotic initiation factor eIF 4A | - |
Oryctolagus cuniculus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Oryctolagus cuniculus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.2 | - |
assay at | Oryctolagus cuniculus |
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Release 2023.1 (January 2023)
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