EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   3.1.13.2 | RNA/DNA hybrid + H2O |
Cy3-labeled 43-nt RNA strand (5'-GGUCUCUCUGGUUAGACCAGAUCUGAGCCUGGGAGCUCUCUGG-3') annealed to a 53-nt DNA strand (5'-CCCTAGTTAGCCAGAGAGCTCCCAGGCTCAGATCTGGTCTAACCAGAGAGACC-3') |
Human immunodeficiency virus 1 |
? |
- |
? |
| 3.1.13.2 | RNA/DNA hybrid + H2O |
Cy3-labeled 43-nt RNA strand (5'-GGUCUCUCUGGUUAGACCAGAUCUGAGCCUGGGAGCUCUCUGG-3') annealed to a 53-nt DNA strand (5'-CCCTAGTTAGCCAGAGAGCTCCCAGGCTCAGATCTGGTCTAACCAGAGAGACC-3') |
Simian immunodeficiency virus |
? |
- |
? |
| 3.1.13.2 | RNA/DNA hybrid + H2O |
Cy3-labeled 43-nt RNA strand (5'-GGUCUCUCUGGUUAGACCAGAUCUGAGCCUGGGAGCUCUCUGG-3') annealed to a 53-nt DNA strand (5'-CCCTAGTTAGCCAGAGAGCTCCCAGGCTCAGATCTGGTCTAACCAGAGAGACC-3') |
Human immunodeficiency virus 2 |
? |
- |
? |
| 3.1.13.2 | RNA/DNA hybrid + H2O |
i.e. 18 nucleotide 3'-fluorescein-labeled RNA annealed to a complementary 18 nucleotide 5'-dabsyl-modified DNA, RNase H catalysis by the retroviral enzyme appears to involve a two-metal ion mechanism. Unlike cellular RNases H, the retroviral RNase H displays three different modes of cleavage: internal, 3'-end-DNA-directed, and 5'-end-RNA-directed, all three modes of cleavage appear to have essential roles in reverse transcription, overview, substrate binding structure, overview |
Human immunodeficiency virus 1 |
? |
- |
? |
| 3.1.13.2 | RNA/DNA hybrid + H2O |
RNase H catalysis by the retroviral enzyme appears to involve a two-metal ion mechanism. Unlike cellular RNases H, the retroviral RNase H displays three different modes of cleavage: internal,3'-end-DNA-directed, and 5'-end-RNA-directed, all three modes of cleavage appear to have essential roles in reverse transcription, overview |
Moloney murine leukemia virus |
? |
- |
? |
| 3.1.13.2 | RNA/DNA hybrid + H2O |
secondary structure and substrate binding, overview |
Moloney murine leukemia virus |
? |
- |
? |
| 3.1.13.2 | single-stranded RNA + H2O |
- |
Human immunodeficiency virus 1 |
? |
- |
? |
