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Literature summary for 3.1.26.13 extracted from

  • Luczkowiak, J.; Matamoros, T.; Menendez-Arias, L.
    Template-primer binding affinity and RNase H cleavage specificity contribute to the strand transfer efficiency of HIV-1 reverse transcriptase (2018), J. Biol. Chem., 293, 13351-13363 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
D443N RNase H inactivating mutation, the mutant is devoid of strand transfer activity Human immunodeficiency virus type 1 group M subtype B
D443N site-directed mutagenesis, the mutant shows increased dissociation rate constant (koff) compared to wild-type Human immunodeficiency virus type 1 group O subtype B
E478Q RNase H inactivating mutation, the mutant is devoid of strand transfer activity Human immunodeficiency virus type 1 group M subtype B
E478Q site-directed mutagenesis, the mutant shows increased dissociation rate constant (koff) compared to wild-type Human immunodeficiency virus type 1 group O subtype B
F61A site-directed mutagenesis, the mutant shows increased dissociation rate constant (koff) compared to wild-type Human immunodeficiency virus type 1 group O subtype B
K358R/A359G/S360A the mutant shows highly increased strand transfer efficiency compared to wild-type Human immunodeficiency virus type 1 group O subtype B
K65R/E478Q site-directed mutagenesis, the mutant shows increased dissociation rate constant (koff) compared to wild-type Human immunodeficiency virus type 1 group O subtype B
L92P site-directed mutagenesis, the mutant shows increased dissociation rate constant (koff) compared to wild-type Human immunodeficiency virus type 1 group O subtype B
L92P/D443N site-directed mutagenesis, the mutant shows decreased dissociation rate constant (koff) compared to wild-type Human immunodeficiency virus type 1 group O subtype B
L92P/E478Q site-directed mutagenesis, the mutant shows increased dissociation rate constant (koff) compared to wild-type Human immunodeficiency virus type 1 group O subtype B
additional information the kinetics of wild-type and mutant enzymes are determined with the RNA/DNA template-primer R33B/20A. Rates of nontemplated nucleotide addition of wild-type and mutant HIV-1 RTs using blunt-ended DNA/DNA substrates, overview. Non-templated nucleotide addition and strand transfer are mechanistically independent Human immunodeficiency virus type 1 group O subtype B
T355A/Q357M site-directed mutagenesis, the mutant shows increased dissociation rate constant (koff) compared to wild-type Human immunodeficiency virus type 1 group O subtype B
T355A/Q357MK358R/A359G/S360A the mutant shows highly increased strand transfer efficiency compared to wild-type Human immunodeficiency virus type 1 group O subtype B
V148I site-directed mutagenesis, the mutant shows increased dissociation rate constant (koff) compared to wild-type Human immunodeficiency virus type 1 group O subtype B
V148I/K358R/A359G/S360A the mutant shows highly increased strand transfer efficiency compared to wild-type Human immunodeficiency virus type 1 group O subtype B

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics of wild-type and mutant enzymes are determined with the RNA/DNA template-primer R33B/20A Human immunodeficiency virus type 1 group O subtype B
additional information
-
additional information kinetics of wild-type enzyme are determined with the RNA/DNA template-primer R33B/20A Human immunodeficiency virus type 1 group M subtype B

Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus type 1 group M subtype B P03366 HIV-1
-
Human immunodeficiency virus type 1 group M subtype B BH10 P03366 HIV-1
-
Human immunodeficiency virus type 1 group O subtype B
-
HIV-1
-
Human immunodeficiency virus type 1 group O subtype B
-
HIV-1ESP49
-
Human immunodeficiency virus type 1 group O subtype B ESP49
-
HIV-1
-
Human immunodeficiency virus type 1 group O subtype B ESP49
-
HIV-1ESP49
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information activities of wild-type and mutant enzymes are determined with the RNA/DNA template-primer R33B/20A, comparison of HIV-1 group O subtype B ESP49 and HIV-1 group M subtype B BH10 Human immunodeficiency virus type 1 group O subtype B ?
-
?
additional information activity of wild-type enzyme is determined with the RNA/DNA template-primer R33B/20A, comparison of HIV-1 group O subtype B ESP49 and HIV-1 group M subtype B BH10 Human immunodeficiency virus type 1 group M subtype B ?
-
?
additional information activities of wild-type and mutant enzymes are determined with the RNA/DNA template-primer R33B/20A, comparison of HIV-1 group O subtype B ESP49 and HIV-1 group M subtype B BH10 Human immunodeficiency virus type 1 group O subtype B ESP49 ?
-
?
additional information activity of wild-type enzyme is determined with the RNA/DNA template-primer R33B/20A, comparison of HIV-1 group O subtype B ESP49 and HIV-1 group M subtype B BH10 Human immunodeficiency virus type 1 group M subtype B BH10 ?
-
?

Synonyms

Synonyms Comment Organism
RNase H
-
Human immunodeficiency virus type 1 group M subtype B
RNase H
-
Human immunodeficiency virus type 1 group O subtype B

General Information

General Information Comment Organism
malfunction the substitution of Pro for Leu-92 renders an HIV-1 reverse transcriptase without strand transfer activity but retaining wild-type DNA polymerase and RNase H activities. Introduction of L92P produces a 3-4fold increase in the dissociation equilibrium constant (Kd) for DNA/DNA template-primers, suggesting that the strand transfer defect is a consequence of impaired nucleic acid binding Human immunodeficiency virus type 1 group O subtype B
additional information nucleotide analogues can enhance strand transfer by slowing DNA polymerization kinetics. Contribution of dissociation rate constants (koff) to the strand transfer efficiency of HIV-1 RTs, overview Human immunodeficiency virus type 1 group M subtype B
additional information nucleotide analogues can enhance strand transfer by slowing DNA polymerization kinetics. Contribution of dissociation rate constants (koff) to the strand transfer efficiency of HIV-1 RTs, overview Human immunodeficiency virus type 1 group O subtype B
physiological function template-primer binding affinity and RNase H cleavage specificity contribute to the strand transfer efficiency of HIV-1 reverse transcriptase Human immunodeficiency virus type 1 group M subtype B
physiological function template-primer binding affinity and RNase H cleavage specificity contribute to the strand transfer efficiency of HIV-1 reverse transcriptase Human immunodeficiency virus type 1 group O subtype B