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Literature summary for 3.1.26.13 extracted from

  • Li, A.; Li, J.; Johnson, K.A.
    HIV-1 reverse transcriptase polymerase and RNase H (ribonuclease H) active sites work simultaneously and independently (2016), J. Biol. Chem., 291, 26566-26585 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.26.13

Protein Variants

Protein Variants Comment Organism
R72A site-directed mutagenesis, the mutant shows reduced activity compared to wild-type. The R72A mutation might impair the nucleotide-induced conformational change but does not affect the RNase H activity directly, kinetic parameters governing TTP binding and incorporation by the HIVRT mutant, overview. The mutation causes impaired TTP induced conformational change on RNase H activity Human immunodeficiency virus 1
W71A site-directed mutagenesis, the mutant is probably less rigidly locked on the substrate DNA/RNA hybrid, parameters governing TTP binding and incorporation by the HIVRT mutant, overview. The mutation causes impaired TTP induced conformational change on RNase H activity Human immunodeficiency virus 1
W71D site-directed mutagenesis, the mutant is probably less rigidly locked on the substrate DNA/RNA hybrid, parameters governing TTP binding and incorporation by the HIVRT mutant, overview. The mutation causes impaired TTP induced conformational change on RNase H activity Human immunodeficiency virus 1

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information RNase H activity is analysed using presteady-state kinetics using global data Human immunodeficiency virus 1

Metals/Ions

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Human immunodeficiency virus 1 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 ?
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 ?

Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus 1
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 HIV-1
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information 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 Human immunodeficiency virus 1 ?
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 ?
additional information usage of DNA/RNA hybrid substrates for enzyme activity assay. The majority of species represent the active form of RTx02DNA/RNA complexes that can perform both activities simultaneously. Efficient RNase H cleavage required at least four ribonucleotides downstream of the cutting site Human immunodeficiency virus 1 ?
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 ?

Synonyms

Synonyms Comment Organism
HIV-1 reverse transcriptase ribonuclease H
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 Human immunodeficiency virus 1
HIV-1 reverse transcriptase RNase H
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 Human immunodeficiency virus 1

General Information

General Information Comment Organism
physiological function HIV reverse transcriptase plays a central role in viral replication and requires coordination of both polymerase and RNaseH activities. HIV-1 reverse transcriptase polymerase and RNase H (ribonuclease H) active sites work simultaneously and independently Human immunodeficiency virus 1