Cloned (Comment) | Organism |
---|---|
recombinant expression of HIV-1 RTp66/p51 heterodimers, expression of RTp66 subunit in Escherichia coli strain M15 in the absence of HIV-1 protease. The lack of protease allows for the expression of RTp66 without a subsequent cleavage to generate RTp51 | Human immunodeficiency virus 1 |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | dissociation/association rate constants and equilibrium dissociation constants for the three dimeric enzyme forms and their nucleic acid substrates | Human immunodeficiency virus 1 |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Human immunodeficiency virus 1 |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Human immunodeficiency virus 1 | - |
- |
- |
Subunits | Comment | Organism |
---|---|---|
dimer | while the biologically relevant form of RT is the p66-p51 heterodimer, two recombinant homodimer forms of RT, p66-p66 and p51p51, are also catalytically active | Human immunodeficiency virus 1 |
Synonyms | Comment | Organism |
---|---|---|
HIV-1 reverse transcriptase | - |
Human immunodeficiency virus 1 |
HIV-1 RT | - |
Human immunodeficiency virus 1 |
General Information | Comment | Organism |
---|---|---|
additional information | while the biologically relevant form of RT is the p66-p51 heterodimer, two recombinant homodimer forms of RT, p66-p66 and p51-p51, are also catalytically active. The apparent binding affinity of p51-p51 for its DNA substrate is to a great extent time-dependent when compared to that of p66-p66 and p66-p51, and is more likely determined by the dimer dissociation into its constituent monomers rather than the intrinsic binding affinity of dimeric enzyme | Human immunodeficiency virus 1 |
physiological function | during viral replication, HIV-1 reverse transcriptase plays a pivotal role in converting genomic RNA into proviral DNA | Human immunodeficiency virus 1 |