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Literature summary for 2.7.7.49 extracted from
- Mechanistic differences in RNA-dependent DNA polymerization and fidelity between murine leukemia virus and HIV-1 reverse transcriptases (2005), J. Biol. Chem., 280, 12190-12200.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| murine leukemia virus | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| deoxynucleoside triphosphate + DNAn | due to its low dNTP binding affinity, the dNTP binding step becomes rate-limiting in the multiple rounds of the dNTP incorporation by MuLV RT. The active site of MuLV RT has an intrinsically low dNTP binding affinity, compared with HIV-1 RT. In addition, instead of the misinsertion step, the mismatch extension step, which varies between MuLV and HIV-1 RTs, contributes to their fidelity differences | murine leukemia virus | diphosphate + DNAn+1 | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| MuLV RT | - |
murine leukemia virus |
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Release 2023.1 (January 2023)
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