Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
deoxynucleoside triphosphate + DNAn | murine leukemia virus | - |
diphosphate + DNAn+1 | - |
? | |
deoxynucleoside triphosphate + DNAn | bovine immunodeficiency virus | - |
diphosphate + DNAn+1 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
bovine immunodeficiency virus | - |
- |
- |
Human immunodeficiency virus 1 | - |
- |
- |
murine leukemia virus | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
deoxynucleoside triphosphate + DNAn | - |
murine leukemia virus | diphosphate + DNAn+1 | - |
? | |
deoxynucleoside triphosphate + DNAn | - |
Human immunodeficiency virus 1 | diphosphate + DNAn+1 | - |
? | |
deoxynucleoside triphosphate + DNAn | - |
bovine immunodeficiency virus | diphosphate + DNAn+1 | - |
? | |
additional information | reverse transcriptases perform template switches when there is a very short (two-nucleotide) complementarity between the 3' ends of the primer (donor) strand and the DNA or RNA template acceptor strands. Combined two-step clamp/DNA polymerase activity, where the initial clamp is followed by DNA synthesis, overview | murine leukemia virus | ? | - |
? | |
additional information | reverse transcriptases perform template switches when there is a very short (two-nucleotide) complementarity between the 3' ends of the primer (donor) strand and the DNA or RNA template acceptor strands. Combined two-step clamp/DNA polymerase activity, where the initial clamp is followed by DNA synthesis, overview | Human immunodeficiency virus 1 | ? | - |
? | |
additional information | reverse transcriptases perform template switches when there is a very short (two-nucleotide) complementarity between the 3' ends of the primer (donor) strand and the DNA or RNA template acceptor strands. Combined two-step clamp/DNA polymerase activity, where the initial clamp is followed by DNA synthesis, overview | bovine immunodeficiency virus | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
reverse transcriptase | - |
murine leukemia virus |
reverse transcriptase | - |
Human immunodeficiency virus 1 |
reverse transcriptase | - |
bovine immunodeficiency virus |
General Information | Comment | Organism |
---|---|---|
additional information | the BIV reverse transcriptase is not stringent in the reaction parameters for clamp activity, such as the minimal complementarity length between the primer and functional template termini that sustains stable clamps, the effects of gaps between the two template strands on the clamp activity of the tested RTs, the effects of template end phosphorylations on the RT-associated clamp activities, and clamp activity with a long hairpin double-stranded primer comprising both the primer and the complementary non-functional template strands, overview. BIV is active with a single-nucleotide clamp substrate although its activity is substantially lower relative to the two-nucleotide clamp. The enzyme from BIV is able to stabilize even a single-nucleotide complementarity between the duplexed P/T2 | bovine immunodeficiency virus |
additional information | the HIV-1 reverse transcriptase is stringent in the reaction parameters for clamp activity, such as the minimal complementarity length between the primer and functional template termini that sustains stable clamps, the effects of gaps between the two template strands on the clamp activity of the tested RTs, the effects of template end phosphorylations on the RT-associated clamp activities, and clamp activity with a long hairpin double-stranded primer comprising both the primer and the complementary non-functional template strands, overview. HIV-1 RT loses all apparent activity when tested with a single-nucleotide clamp substrate. The enzyme from HIV is not able to stabilize a single-nucleotide complementarity between the duplexed P/T2 | Human immunodeficiency virus 1 |
additional information | the MLV reverse transcriptase is stringent in the reaction parameters for clamp activity, such as the minimal complementarity length between the primer and functional template termini that sustains stable clamps, the effects of gaps between the two template strands on the clamp activity of the tested RTs, the effects of template end phosphorylations on the RT-associated clamp activities, and clamp activity with a long hairpin double-stranded primer comprising both the primer and the complementary non-functional template strands, overview. MLV RT loses all apparent activity when tested with s single-nucleotide clamp substrate. The enzyme from MIV is not able to stabilize a single-nucleotide complementarity between the duplexed P/T2 | murine leukemia virus |