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Literature summary for 2.7.7.49 extracted from

  • Marko, R.A.; Liu, H.W.; Ablenas, C.J.; Ehteshami, M.; Goette, M.; Cosa, G.
    Binding kinetics and affinities of heterodimeric versus homodimeric HIV-1 reverse transcriptase on DNA-DNA substrates at the single-molecule level (2013), J. Phys. Chem. B, 117, 4560-4567.
    View publication on PubMed

Cloned(Commentary)

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 [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

Metals/Ions Comment Organism Structure
Mg2+ required Human immunodeficiency virus 1

Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus 1
-
-
-

Subunits

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

Synonyms Comment Organism
HIV-1 reverse transcriptase
-
Human immunodeficiency virus 1
HIV-1 RT
-
Human immunodeficiency virus 1

General Information

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