EC Number   |
Natural Substrates |
|---|
   3.1.26.13 | more |
5'end-directed RNase H of reverse transcriptase |
| 3.1.26.13 | more |
HIV-1 reverse transcriptase has two enzymatic functions, DNA polymerase and RNase H activities |
| 3.1.26.13 | more |
Moloney murine leukemia virus reverse transcriptase, M-MuLV RT, is a domain structured enzyme that has the N-terminally located DNA polymerization activity and C-terminally located RNase H activity, which interferes with the efficient synthesis of long cDNA molecules |
| 3.1.26.13 | more |
Moloney murine leukemia virus reverse transcriptase, MMLV RT, shows DNA polymerization activity and RNase H activity. Stabilization of the reverse transcriptase activity by eliminating the RNase H activity, overview |
| 3.1.26.13 | more |
retroviral reverse transcriptase also possesses a ribonuclease H activity, an enzyme which cleaves the RNA strand of RNA/DNA hetroduplex |
| 3.1.26.13 | more |
RNase H functions as an endonuclease that specifically cleaves the RNA moiety of RNA/DNA hybrids, substrate binding and reaction mechanism, overview |
| 3.1.26.13 | more |
conserved residues in the connection subdomain and C-terminal ribonuclease H, RNase H, domain of HIV-1 RT contact the nascent DNA primer and modulate the trajectory of the template relative to the RNase H catalytic center. Within the RNase H domain, these residues include Thr473, Glu475, Lys476, Tyr501, and Ile505, while His539 and Asn474 interact with the scissile phosphate of the RNA template,m substrate recognition and binding, overview |
| 3.1.26.13 | more |
a DNA/RNA hybrid can simultaneously engage both active sites. Of the tested interconverting reverse transcriptase-DNA/RNA species, 43% are active for both sites simultaneously, 27% show only polymerase activity, and the remaining 30% are nonproductive. A string of at least 4-6 nucleotides downstream of the cleaving site is required for efficient RNA cleavage. During processive nucleotide incorporation, sequential rounds of RNA cleavage occur each time after about 6 nucleotides are incorporated, during processive primer extension, diphosphate release is rate-limiting. Although polymerization is efficient and processive, RNase H is inefficient and periodic. This combination allows the two catalytic centers of HIVRT to work simultaneously at similar speeds without being tightly coupled |
| 3.1.26.13 | more |
HIV RNase H cleaves viral RNA at multiple stages of reverse transcription with at least three distinct modes: random internal cleavages, DNA 3' end-directed and polymerase dependent cleavages, and RNA 5' end-directed cleavages. A biochemical assay uses the HTS-1 RNA/DNA substrate to specifically probe random internal cleavage, which is believed to be the dominant mode of RNA cutting |
| 3.1.26.13 | RNA-DNA duplex + H2O |
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