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Literature summary for 3.1.26.13 extracted from
- Enzymatic analysis of two HIV-1 reverse transcriptase mutants with mutations in carboxyl-terminal amino acid residues conserved among retroviral ribonucleases H (1993), J. Biol. Chem., 268, 2674-2683.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Human immunodeficiency virus 1 |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| N494D | mutant closely resembles the wild-type RNase H, exhibits an endonuclease activity and a processive RNase H activity, gives rise to small RNA hydrolysis products, and acts in concert with the reverse transcriptase | Human immunodeficiency virus 1 |
| Q475E | mutant exhibits a retarded endonuclease activity and an impaired 3'-5' processive RNA cleavage activity, gives rise to predominantly larger RNA hydrolysis products, is less processive in the presence of competitor substrate, and is defective in its ability to hydrolyze the polypurine tract and homopolymeric hybrids | Human immunodeficiency virus 1 |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Human immunodeficiency virus 1 | - |
- |
- |
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Release 2023.1 (January 2023)
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