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Results for property: KM

Detailed Results for Property

Use this page to examine all the the polymerases and references referring to the property: K<sub>M</sub>.

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Polymerase Kingdom Family Reference Result Context
T7 Virus/Phage A Pre-steady-state kinetic analysis of processive DNA replication including complete characterization of an exonuclease-deficient mutant. 690nM Reaction: 3-5' Exonuclease; Substrate: DNA template
T7 Virus/Phage A Characterization of a DNA polymerase from the hyperthermophile archaea Thermococcus litoralis. Vent DNA polymerase, steady state kinetics, thermal stability, processivity, strand displacement, and exonuclease activities. 18uM Reaction: Nucleotide incorporation; Substrate: dNTPs; Technique: Filter binding ; Experimental conditions: Temp (72°C)
T7 Virus/Phage A Deoxyribonucleic acid polymerase of bacteriophage T7. Purification and properties of the phage-encoded subunit, the gene 5 protein. 48nM Reaction: 3-5' Exonuclease; Substrate: DNA template
9egN Archaeon B DNA polymerases from hyperthermophiles. 0.05nM Reaction: Polymerase-DNA interaction; Substrate: DNA template
9egN Archaeon B DNA polymerases from hyperthermophiles. 75uM Reaction: Nucleotide incorporation; Substrate: dNTPs
9egN Archaeon B Cloning of thermostable DNA polymerases from hyperthermophilic marine Archaea with emphasis on Thermococcus sp. 9 degrees N-7 and mutations affecting 3'-5' exonuclease activity. 75uM Reaction: Nucleotide incorporation; Substrate: dNTPs; Technique: Filter binding ; Experimental conditions: Temp (72°C)
Vent Archaeon B DNA polymerases from hyperthermophiles. 57uM Reaction: Nucleotide incorporation; Substrate: dNTPs
Vent Archaeon B DNA polymerases from hyperthermophiles. 0.1nM Reaction: Polymerase-DNA interaction; Substrate: DNA template
Vent Archaeon B Characterization of a DNA polymerase from the hyperthermophile archaea Thermococcus litoralis. Vent DNA polymerase, steady state kinetics, thermal stability, processivity, strand displacement, and exonuclease activities. 0.07uM Reaction: Polymerase-DNA interaction; Substrate: DNA template; Technique: Filter binding ; Experimental conditions: Temp (72°C)
Vent Archaeon B Characterization of a DNA polymerase from the hyperthermophile archaea Thermococcus litoralis. Vent DNA polymerase, steady state kinetics, thermal stability, processivity, strand displacement, and exonuclease activities. 41uM Reaction: Nucleotide incorporation; Technique: Filter binding ; Experimental conditions: Temp (72°C)
T4 D219A Virus/Phage B Functional consequences and exonuclease kinetic parameters of point mutations in bacteriophage T4 DNA polymerase. 0.3uM Reaction: 3-5' Exonuclease; Substrate: DNA template
T4 D219A Virus/Phage B Functional consequences and exonuclease kinetic parameters of point mutations in bacteriophage T4 DNA polymerase. 12.8uM Reaction: 3-5' Exonuclease; Substrate: DNA template
T4 Virus/Phage B Characterization of a DNA polymerase from the hyperthermophile archaea Thermococcus litoralis. Vent DNA polymerase, steady state kinetics, thermal stability, processivity, strand displacement, and exonuclease activities. 2uM Reaction: Nucleotide incorporation; Substrate: dNTPs; Technique: Filter binding ; Experimental conditions: Temp (72°C)
T4 Virus/Phage B Error induction and correction by mutant and wild type T4 DNA polymerases. Kinetic error discrimination mechanisms. 4.6uM Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Primer extension assay
T4 Virus/Phage B Error induction and correction by mutant and wild type T4 DNA polymerases. Kinetic error discrimination mechanisms. 25.9uM Reaction: Nucleotide incorporation; Substrate: n/a; Technique: Primer extension assay (2AP)
T4 Virus/Phage B Nuclease activity in a fragment of bacteriophage T4 deoxyribonucleic acid polymerase induced by the amber mutant am B22. 0.04uM Reaction: 3-5' Exonuclease; Substrate: DNA template
T4 Virus/Phage B Nuclease activity in a fragment of bacteriophage T4 deoxyribonucleic acid polymerase induced by the amber mutant am B22. 0.08uM Reaction: 3-5' Exonuclease; Substrate: DNA template
T4 Virus/Phage B Isolation, characterization, and kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3'-5' exonuclease activity. 1000uM Reaction: 3-5' Exonuclease; Substrate: DNA template
T4 Virus/Phage B Isolation, characterization, and kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3'-5' exonuclease activity. 7uM Reaction: 3-5' Exonuclease; Substrate: DNA template
T4 Virus/Phage B Functional consequences and exonuclease kinetic parameters of point mutations in bacteriophage T4 DNA polymerase. 6.9uM Reaction: 3-5' Exonuclease; Substrate: DNA template
T4 Virus/Phage B Functional consequences and exonuclease kinetic parameters of point mutations in bacteriophage T4 DNA polymerase. 0.4uM Reaction: 3-5' Exonuclease; Substrate: DNA template
T4 Virus/Phage B An antimutator deoxyribonucleic acid polymerase. I. Purification and properties of the enzyme. 17uM Reaction: Nucleotide incorporation; Substrate: dTTP; Experimental conditions: Temp (30°C)
T4 Virus/Phage B An antimutator deoxyribonucleic acid polymerase. I. Purification and properties of the enzyme. 17uM Reaction: Nucleotide incorporation; Substrate: dTTP; Experimental conditions: Temp (43°C)
T4 Virus/Phage B An antimutator deoxyribonucleic acid polymerase. I. Purification and properties of the enzyme. 47uM Reaction: 3-5' Exonuclease; Substrate: DNA template; Experimental conditions: Temp (30°C)
T4 Virus/Phage B T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template. 1600uM Reaction: Nucleotide incorporation; Substrate: dCTP; Experimental conditions: pH (pH 8.8), Temp (30°C)
T4 Virus/Phage B T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template. 1.9uM Reaction: Nucleotide incorporation; Substrate: dCTP; Experimental conditions: pH (pH 8.8), Temp (30°C)
T4 Virus/Phage B T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template. 17uM Reaction: Nucleotide incorporation; Substrate: dATP; Experimental conditions: pH (pH 8.8), Temp (30°C)
T4 Virus/Phage B T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template. 1.3uM Reaction: Nucleotide incorporation; Substrate: dATP; Experimental conditions: pH (pH 8.8), Temp (30°C)
T4 Virus/Phage B T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template. 6uM Reaction: Nucleotide incorporation; Substrate: dTTP; Experimental conditions: pH (pH 8.8), Temp (30°C)
T4 Virus/Phage B T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template. 1.8uM Reaction: Nucleotide incorporation; Substrate: dTTP; Experimental conditions: pH (pH 8.8), Temp (30°C)
T4 Virus/Phage B T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template. 190uM Reaction: Nucleotide incorporation; Substrate: dGTP; Experimental conditions: pH (pH 8.8), Temp (30°C)
T4 Virus/Phage B T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template. 1.3uM Reaction: Nucleotide incorporation; Substrate: dGTP; Experimental conditions: pH (pH 8.8), Temp (30°C)
T4 Virus/Phage B Molecular basis for substitution mutations. Effect of primer terminal and template residues on nucleotide selection by phage T4 DNA polymerase in vitro. 12.3uM Reaction: Nucleotide incorporation; Substrate: dCTP; Technique: Steady State (Template: poly (dG)-(dC))
T4 Virus/Phage B Molecular basis for substitution mutations. Effect of primer terminal and template residues on nucleotide selection by phage T4 DNA polymerase in vitro. 38uM Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Steady State (Template: poly(dA)-(dT))
T4 Virus/Phage B Molecular basis for substitution mutations. Effect of primer terminal and template residues on nucleotide selection by phage T4 DNA polymerase in vitro. 605uM Reaction: Misincorporation; Substrate: dGTP; Technique: Steady State (Template: poly(dA)-(dT))
T4 Virus/Phage B Molecular basis for substitution mutations. Effect of primer terminal and template residues on nucleotide selection by phage T4 DNA polymerase in vitro. 5950uM Reaction: Misincorporation; Substrate: dCTP; Technique: Steady State (Template: poly(dA)-(dT))
T4 Virus/Phage B Molecular basis for substitution mutations. Effect of primer terminal and template residues on nucleotide selection by phage T4 DNA polymerase in vitro. 1850uM Reaction: Misincorporation; Substrate: dATP; Technique: Steady State (Template: poly(dG)-(dC))
T4 Virus/Phage B Molecular basis for substitution mutations. Effect of primer terminal and template residues on nucleotide selection by phage T4 DNA polymerase in vitro. 4940uM Reaction: Misincorporation; Substrate: dTTP; Technique: Steady State (Template: poly(dG)-(dC))
T4 Virus/Phage B Molecular basis for substitution mutations. Effect of primer terminal and template residues on nucleotide selection by phage T4 DNA polymerase in vitro. 6.4uM Reaction: Nucleotide incorporation; Substrate: dGTP; Technique: Steady State (Template: poly(dG)-(dC))
T4 A737V Virus/Phage B An antimutator deoxyribonucleic acid polymerase. I. Purification and properties of the enzyme. 47uM Reaction: 3-5' Exonuclease; Substrate: DNA template; Experimental conditions: Temp (30°C)
T4 A737V Virus/Phage B An antimutator deoxyribonucleic acid polymerase. I. Purification and properties of the enzyme. 37uM Reaction: Nucleotide incorporation; Substrate: dTTP; Experimental conditions: Temp (30°C)
T4 A737V Virus/Phage B An antimutator deoxyribonucleic acid polymerase. I. Purification and properties of the enzyme. 138uM Reaction: Nucleotide incorporation; Substrate: dTTP; Experimental conditions: Temp (43°C)
T4 D112AE114A Virus/Phage B In search of a mutational hotspot. 1.01uM Reaction: Nucleotide incorporation; Substrate: dCTP
T4 D112AE114A Virus/Phage B In search of a mutational hotspot. 8.87uM Reaction: Misincorporation; Substrate: dATP
T4 D112AE114A Virus/Phage B In search of a mutational hotspot. 1.38uM Reaction: Misincorporation; Substrate: dATP
T4 D112AE114A Virus/Phage B In search of a mutational hotspot. 0.34uM Reaction: Misincorporation; Substrate: dATP
T4 D112AE114A Virus/Phage B In search of a mutational hotspot. 0.18uM Reaction: Nucleotide incorporation; Substrate: dATP
T4 D112AE114A Virus/Phage B In search of a mutational hotspot. 0.911uM Reaction: Nucleotide incorporation; Substrate: dCTP
T4 D112AE114A Virus/Phage B In search of a mutational hotspot. 0.32uM Reaction: Nucleotide incorporation; Substrate: dATP
T4 D112AE114A Virus/Phage B In search of a mutational hotspot. 8.24uM Reaction: Nucleotide incorporation; Substrate: dATP
T4 D112AE114A Virus/Phage B In search of a mutational hotspot. 0.683uM Reaction: Misincorporation; Substrate: dCTP
T4 D112AE114A Virus/Phage B In search of a mutational hotspot. 0.102uM Reaction: Nucleotide incorporation; Substrate: dATP
T4 D112AE114A Virus/Phage B In search of a mutational hotspot. 0.332uM Reaction: Misincorporation; Substrate: dCTP
T4 D112AE114A Virus/Phage B In search of a mutational hotspot. 0.11uM Reaction: Misincorporation; Substrate: dCTP
T4 D324A Virus/Phage B Functional consequences and exonuclease kinetic parameters of point mutations in bacteriophage T4 DNA polymerase. 0.4uM Reaction: 3-5' Exonuclease; Substrate: DNA template
T4 D324A Virus/Phage B Functional consequences and exonuclease kinetic parameters of point mutations in bacteriophage T4 DNA polymerase. 6.3uM Reaction: 3-5' Exonuclease; Substrate: DNA template
Eco Pol I Eubacterium A The steady state kinetic parameters and non-processivity of Escherichia coli deoxyribonucleic acid polymerase I. 1uM Reaction: Nucleotide incorporation; Substrate: dATP
Eco Pol I Eubacterium A Characterization of a DNA polymerase from the hyperthermophile archaea Thermococcus litoralis. Vent DNA polymerase, steady state kinetics, thermal stability, processivity, strand displacement, and exonuclease activities. 2uM Reaction: Nucleotide incorporation; Substrate: dNTPs; Technique: Filter binding ; Experimental conditions: Temp (72°C)
Eco Pol I Eubacterium A The steady state kinetic parameters and non-processivity of Escherichia coli deoxyribonucleic acid polymerase I. 2uM Reaction: Nucleotide incorporation; Substrate: dTTP
Eco Pol I Eubacterium A Short deoxyribonucleic acid repair patch length in Escherichia coli is determined by the processive mechanism of deoxyribonucleic acid polymerase I. 2uM Reaction: Nucleotide incorporation; Substrate: dNTPs
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. 28. The pyrophosphate exchange and pyrophosphorolysis reactions of deoxyribonucleic acid polymerase. 600nM Reaction: Pyrophosphorolysis; Substrate: DNA template; Experimental conditions: Temp (37°C)
Klenow fragment Eubacterium A DNA polymerases from hyperthermophiles. 1.8nM Reaction: Polymerase-DNA interaction; Substrate: DNA template
Klenow fragment Eubacterium A The 3'-5' exonuclease of DNA polymerase I of Escherichia coli: contribution of each amino acid at the active site to the reaction. 0.56uM Reaction: 3-5' Exonuclease; Technique: Steady State (ssDNA: poly(dT)); Experimental conditions: pH (pH 7.5), Mg++ (6mM), Temp (37°C)
Klenow fragment Eubacterium A Characterization of a DNA polymerase from the hyperthermophile archaea Thermococcus litoralis. Vent DNA polymerase, steady state kinetics, thermal stability, processivity, strand displacement, and exonuclease activities. 2.3uM Reaction: Nucleotide incorporation; Substrate: dNTPs; Technique: Filter binding ; Experimental conditions: Temp (72°C)
Klenow fragment Eubacterium A Formation of 2-hydroxydeoxyadenosine triphosphate, an oxidatively damaged nucleotide, and its incorporation by DNA polymerases. Steady-state kinetics of the incorporation. 1.8uM Reaction: Nucleotide incorporation; Substrate: ATP analog; Technique: Steady State
Klenow fragment Eubacterium A DNA polymerases from hyperthermophiles. 2.3uM Reaction: Nucleotide incorporation; Substrate: dNTPs
Klenow fragment Eubacterium A Isolation, characterization, and kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3'-5' exonuclease activity. 160uM Reaction: 3-5' Exonuclease; Substrate: DNA template
Klenow fragment Eubacterium A Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. 2.3uM Reaction: Nucleotide incorporation; Substrate: dNTPs
Klenow fragment Eubacterium A Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. 1.8nM Reaction: Polymerase-DNA interaction; Substrate: DNA template
Klenow fragment Eubacterium A A thumb subdomain mutant of the large fragment of Escherichia coli DNA polymerase I with reduced DNA binding affinity, processivity, and frameshift fidelity. 3.7uM Reaction: Nucleotide incorporation; Substrate: dTTP
Klenow fragment Eubacterium A Formation of 2-hydroxydeoxyadenosine triphosphate, an oxidatively damaged nucleotide, and its incorporation by DNA polymerases. Steady-state kinetics of the incorporation. 0.24uM Reaction: Nucleotide incorporation; Substrate: dNTPs; Technique: Steady State
Klenow fragment Eubacterium A Isolation, characterization, and kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3'-5' exonuclease activity. 3uM Reaction: 3-5' Exonuclease; Substrate: DNA template
T4 D112A Virus/Phage B Functional consequences and exonuclease kinetic parameters of point mutations in bacteriophage T4 DNA polymerase. 7.7uM Reaction: 3-5' Exonuclease; Substrate: DNA template
T4 D112A Virus/Phage B Functional consequences and exonuclease kinetic parameters of point mutations in bacteriophage T4 DNA polymerase. 1.6uM Reaction: 3-5' Exonuclease; Substrate: DNA template
Dpo4 Archaeon Y Molecular basis of selectivity of nucleoside triphosphate incorporation opposite O6-benzylguanine by sulfolobus solfataricus DNA polymerase Dpo4: steady-state and pre-steady-state kinetics and x-ray crystallography of correct and incorrect pairing. 3uM Reaction: Nucleotide incorporation; Substrate: dCTP; Technique: Steady State (dGTP)
Dpo4 Archaeon Y Kinetic analysis of correct nucleotide insertion by a Y-family DNA polymerase reveals conformational changes both prior to and following phosphodiester bond formation as detected by tryptophan fluorescence. 7.7uM Reaction: Nucleotide incorporation; Substrate: dCTP; Technique: Steady State (Template G)
Dpo4 Archaeon Y Molecular basis of selectivity of nucleoside triphosphate incorporation opposite O6-benzylguanine by sulfolobus solfataricus DNA polymerase Dpo4: steady-state and pre-steady-state kinetics and x-ray crystallography of correct and incorrect pairing. 600uM Reaction: Nucleotide incorporation; Substrate: dGTP; Technique: Steady State (O6-BzG)
Dpo4 Archaeon Y Molecular basis of selectivity of nucleoside triphosphate incorporation opposite O6-benzylguanine by sulfolobus solfataricus DNA polymerase Dpo4: steady-state and pre-steady-state kinetics and x-ray crystallography of correct and incorrect pairing. 1200uM Reaction: Nucleotide incorporation; Substrate: dTTP; Technique: Steady State (O6-BzG)
Dpo4 Archaeon Y Molecular basis of selectivity of nucleoside triphosphate incorporation opposite O6-benzylguanine by sulfolobus solfataricus DNA polymerase Dpo4: steady-state and pre-steady-state kinetics and x-ray crystallography of correct and incorrect pairing. 300uM Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Steady State (O6-BzG)
Dpo4 Archaeon Y Molecular basis of selectivity of nucleoside triphosphate incorporation opposite O6-benzylguanine by sulfolobus solfataricus DNA polymerase Dpo4: steady-state and pre-steady-state kinetics and x-ray crystallography of correct and incorrect pairing. 1400uM Reaction: Nucleotide incorporation; Substrate: dCTP; Technique: Steady State (O6-BzG)
Human Pol eta Eukaryote Y Amino acid substitutions at conserved tyrosine 52 alter fidelity and bypass efficiency of human DNA polymerase eta. 55n/a Reaction: Nucleotide incorporation; Substrate: dCTP
Human Pol eta Eukaryote Y Amino acid substitutions at conserved tyrosine 52 alter fidelity and bypass efficiency of human DNA polymerase eta. 38n/a Reaction: Nucleotide incorporation; Substrate: dTTP
Human Pol eta Eukaryote Y Amino acid substitutions at conserved tyrosine 52 alter fidelity and bypass efficiency of human DNA polymerase eta. 1.7n/a Reaction: Nucleotide incorporation; Substrate: dATP
Human Pol eta Eukaryote Y Amino acid substitutions at conserved tyrosine 52 alter fidelity and bypass efficiency of human DNA polymerase eta. 3.2n/a Reaction: Nucleotide incorporation; Substrate: dGTP
Dpo4 T239W Archaeon Y Kinetic analysis of correct nucleotide insertion by a Y-family DNA polymerase reveals conformational changes both prior to and following phosphodiester bond formation as detected by tryptophan fluorescence. 12uM Reaction: Nucleotide incorporation; Substrate: dCTP; Technique: Steady State
Dpo4 N188W Archaeon Y Kinetic analysis of correct nucleotide insertion by a Y-family DNA polymerase reveals conformational changes both prior to and following phosphodiester bond formation as detected by tryptophan fluorescence. 14uM Reaction: Nucleotide incorporation; Substrate: dCTP; Technique: Steady State
Human Pol beta Eukaryote X Human DNA polymerases alpha and beta are able to incorporate anti-HIV deoxynucleotides into DNA. 2.6uM Reaction: Nucleotide incorporation; Substrate: dTTP; Technique: Steady State (Standing start primer template)
Human Pol beta Eukaryote X Human DNA polymerases alpha and beta are able to incorporate anti-HIV deoxynucleotides into DNA. 2.3uM Reaction: Nucleotide incorporation; Substrate: dTTP; Technique: Steady State (Activated DNA)
Human Pol beta Eukaryote X Human DNA polymerases alpha and beta are able to incorporate anti-HIV deoxynucleotides into DNA. 1.7uM Reaction: Nucleotide incorporation; Substrate: dCTP; Technique: Steady State (Standing start primer template)
Human Pol beta Eukaryote X Human DNA polymerases alpha and beta are able to incorporate anti-HIV deoxynucleotides into DNA. 1.2uM Reaction: Nucleotide incorporation; Substrate: ddCTP; Technique: Steady State (Standing start primer template)
Human Pol beta Eukaryote X Human DNA polymerases alpha and beta are able to incorporate anti-HIV deoxynucleotides into DNA. 1.5uM Reaction: Nucleotide incorporation; Substrate: dCTP; Technique: Steady State (Activated DNA)
T5 Virus/Phage A Exonuclease associated with bacteriophage T5-Induced DNA polymerase. 21.9uM Reaction: 3-5' Exonuclease; Substrate: DNA template
Taq pol I Eubacterium A DNA polymerases from hyperthermophiles. 24uM Reaction: Nucleotide incorporation; Substrate: dNTPs
Taq pol I Eubacterium A DNA polymerases from hyperthermophiles. 4nM Reaction: Polymerase-DNA interaction; Substrate: DNA template
Taq pol I Eubacterium A Crystal structure of a thermostable Bacillus DNA polymerase I large fragment at 2.1 A resolution. 24uM Reaction: Nucleotide incorporation; Substrate: dNTPs; Technique: Filter binding ; Experimental conditions: Temp (72°C)
Taq pol I Eubacterium A Crystal structure of a thermostable Bacillus DNA polymerase I large fragment at 2.1 A resolution. 3.5nM Reaction: Polymerase-DNA interaction; Substrate: DNA template; Technique: Filter binding ; Experimental conditions: Temp (72°C)
Taq pol I Eubacterium A Characterization of a DNA polymerase from the hyperthermophile archaea Thermococcus litoralis. Vent DNA polymerase, steady state kinetics, thermal stability, processivity, strand displacement, and exonuclease activities. 16uM Reaction: Nucleotide incorporation; Substrate: dNTPs; Technique: Filter binding ; Experimental conditions: Temp (72°C)
Taq pol I Eubacterium A Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. 3.5nM Reaction: Polymerase-DNA interaction; Substrate: DNA template
Taq pol I Eubacterium A Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. 24uM Reaction: Nucleotide incorporation; Substrate: dNTPs
HIV RT Virus/Phage RT Steady state kinetics and inhibition of HIV-1 reverse transcriptase by a non-nucleoside dipyridodiazepinone, BI-RG-587, using a heteropolymeric template. 10nM Reaction: Nucleotide incorporation; Substrate: dCTP; Technique: Steady State
HIV RT Virus/Phage RT Human immunodeficiency virus reverse transcriptase. Substrate and inhibitor kinetics with thymidine 5'-triphosphate and 3'-azido-3'-deoxythymidine 5'-triphosphate. 0.082uM Reaction: Nucleotide incorporation; Substrate: dTTP; Technique: Rapid quench (RNA template)
HIV RT Virus/Phage RT Human immunodeficiency virus reverse transcriptase. Substrate and inhibitor kinetics with thymidine 5'-triphosphate and 3'-azido-3'-deoxythymidine 5'-triphosphate. 10uM Reaction: Nucleotide incorporation; Substrate: dNTPs; Technique: Rapid quench (RNA template)
HIV RT Virus/Phage RT Steady state kinetics and inhibition of HIV-1 reverse transcriptase by a non-nucleoside dipyridodiazepinone, BI-RG-587, using a heteropolymeric template. 100nM Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Steady State
HIV RT Virus/Phage RT Steady state kinetics and inhibition of HIV-1 reverse transcriptase by a non-nucleoside dipyridodiazepinone, BI-RG-587, using a heteropolymeric template. 20nM Reaction: Nucleotide incorporation; Substrate: dGTP; Technique: Steady State
HIV RT Virus/Phage RT Human immunodeficiency virus 1 reverse transcriptase. Template binding, processivity, strand displacement synthesis, and template switching. 10uM Reaction: Nucleotide incorporation; Substrate: dTTP
HIV RT Virus/Phage RT Steady state kinetics and inhibition of HIV-1 reverse transcriptase by a non-nucleoside dipyridodiazepinone, BI-RG-587, using a heteropolymeric template. 40nM Reaction: Nucleotide incorporation; Substrate: dTTP; Technique: Steady State
HIV RT Virus/Phage RT Human immunodeficiency virus reverse transcriptase. Substrate and inhibitor kinetics with thymidine 5'-triphosphate and 3'-azido-3'-deoxythymidine 5'-triphosphate. 0.19uM Reaction: Nucleotide incorporation; Substrate: TTP analog; Technique: Rapid quench
Pfu Archaeon B DNA polymerases from hyperthermophiles. 0.7nM Reaction: Polymerase-DNA interaction; Substrate: DNA template
Pfu Archaeon B DNA polymerases from hyperthermophiles. 16uM Reaction: Nucleotide incorporation; Substrate: dNTPs
Human Pol lamba Eukaryote X Loop 1 modulates the fidelity of DNA polymerase {lambda} 0.39uM Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Steady State
Human Pol lamba Eukaryote X DNA polymerase lambda, a novel DNA repair enzyme in human cells. 0.5uM Reaction: Nucleotide incorporation; Substrate: dNTPs
Human Pol lamba Eukaryote X Loop 1 modulates the fidelity of DNA polymerase {lambda} 7.4uM Reaction: Nucleotide incorporation; Substrate: dGTP; Technique: Steady State
PGBD Pol I Archaeon B DNA polymerases from hyperthermophiles. 50uM Reaction: Nucleotide incorporation; Substrate: dNTPs
PGBD Pol I Archaeon B DNA polymerases from hyperthermophiles. 0.01nM Reaction: Polymerase-DNA interaction; Substrate: DNA template
Bst Eubacterium A DNA polymerase from mesophilic and thermophilic bacteria. III. Lack of fidelity in the replication of synthetic polydeoxyribonucleotides by DNA polymerase from Bacillus licheniformis and Bacillus stearothermophilus. 90uM Reaction: Nucleotide incorporation; Substrate: dNTPs
Bst LF Eubacterium A DNA polymerases from hyperthermophiles. 13uM Reaction: Nucleotide incorporation; Substrate: dNTPs
Bst LF Eubacterium A Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. 3.4nM Reaction: Polymerase-DNA interaction; Substrate: DNA template
Bst LF Eubacterium A Crystal structure of a thermostable Bacillus DNA polymerase I large fragment at 2.1 A resolution. 3.4nM Reaction: Polymerase-DNA interaction; Substrate: DNA template; Technique: Filter binding ; Experimental conditions: Temp (65°C)
Bst LF Eubacterium A Crystal structure of a thermostable Bacillus DNA polymerase I large fragment at 2.1 A resolution. 13uM Reaction: Nucleotide incorporation; Substrate: dNTPs; Technique: Filter binding ; Experimental conditions: Temp (65°C)
Bst LF Eubacterium A Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. 13uM Reaction: Nucleotide incorporation; Substrate: dNTPs
Bst LF Eubacterium A DNA polymerases from hyperthermophiles. 4.2nM Reaction: Polymerase-DNA interaction; Substrate: DNA template
KF Y766S Eubacterium A Identification of residues critical for the polymerase activity of the Klenow fragment of DNA polymerase I from Escherichia coli. 6.4uM Reaction: Nucleotide incorporation; Substrate: dNTPs; Technique: Rapid quench
AMV Virus/Phage RT RNA-dependent DNA polymerase activity of RNA tumor virus. VI. Processive mode of action of avian myeloblastosis virus polymerase. 10uM Reaction: Nucleotide incorporation; Substrate: dNTPs
Terminal Transferase Unknown ? Terminal deoxynucleotidyl transferase indiscriminately incorporates ribonucleotides and deoxyribonucleotides. 300uM Reaction: Nucleotide incorporation; Substrate: dATP
Terminal Transferase Unknown ? Terminal deoxynucleotidyl transferase indiscriminately incorporates ribonucleotides and deoxyribonucleotides. 5.9uM Reaction: Nucleotide incorporation; Substrate: dATP
Terminal Transferase Unknown ? Terminal deoxynucleotidyl transferase indiscriminately incorporates ribonucleotides and deoxyribonucleotides. 368uM Reaction: Nucleotide incorporation; Substrate: rATP
Terminal Transferase Unknown ? Terminal deoxynucleotidyl transferase indiscriminately incorporates ribonucleotides and deoxyribonucleotides. 15.9uM Reaction: Nucleotide incorporation; Substrate: dATP
T4 Q731am Virus/Phage B Nuclease activity in a fragment of bacteriophage T4 deoxyribonucleic acid polymerase induced by the amber mutant am B22. 0.38uM Reaction: 3-5' Exonuclease; Substrate: DNA template
T4 Q731am Virus/Phage B Nuclease activity in a fragment of bacteriophage T4 deoxyribonucleic acid polymerase induced by the amber mutant am B22. 0.71uM Reaction: 3-5' Exonuclease; Substrate: DNA template
Bli DNA polymerase Eubacterium A DNA polymerase from mesophilic and thermophilic bacteria. III. Lack of fidelity in the replication of synthetic polydeoxyribonucleotides by DNA polymerase from Bacillus licheniformis and Bacillus stearothermophilus. 70uM Reaction: Nucleotide incorporation; Substrate: dNTPs
Human Pol alpha Eukaryote B Enzymological characterization of DNA polymerase alpha. Basic catalytic properties processivity, and gap utilization of the homogeneous enzyme from human KB cells. 39uM Reaction: Polymerase-DNA interaction; Substrate: DNA template
Human Pol alpha Eukaryote B Enzymological characterization of DNA polymerase alpha. Basic catalytic properties processivity, and gap utilization of the homogeneous enzyme from human KB cells. 44uM Reaction: Polymerase-DNA interaction; Substrate: DNA template
Human Pol alpha Eukaryote B Enzymological characterization of DNA polymerase alpha. Basic catalytic properties processivity, and gap utilization of the homogeneous enzyme from human KB cells. 4uM Reaction: Nucleotide incorporation; Substrate: dTTP
Human Pol alpha Eukaryote B Enzymological characterization of DNA polymerase alpha. Basic catalytic properties processivity, and gap utilization of the homogeneous enzyme from human KB cells. 2.3uM Reaction: Nucleotide incorporation; Substrate: dCTP
Human Pol alpha Eukaryote B Enzymological characterization of DNA polymerase alpha. Basic catalytic properties processivity, and gap utilization of the homogeneous enzyme from human KB cells. 1.2uM Reaction: Nucleotide incorporation; Substrate: dGTP
Human Pol alpha Eukaryote B Enzymological characterization of DNA polymerase alpha. Basic catalytic properties processivity, and gap utilization of the homogeneous enzyme from human KB cells. 3uM Reaction: Nucleotide incorporation; Substrate: dATP
Human Pol alpha Eukaryote B Human DNA polymerases alpha and beta are able to incorporate anti-HIV deoxynucleotides into DNA. 1.5uM Reaction: Nucleotide incorporation; Substrate: dTTP; Technique: Steady State (Activated DNA)
Human Pol alpha Eukaryote B Human DNA polymerases alpha and beta are able to incorporate anti-HIV deoxynucleotides into DNA. 1.8uM Reaction: Nucleotide incorporation; Substrate: dCTP; Technique: Steady State (activated DNA)
Human Pol alpha Eukaryote B Human DNA polymerases alpha and beta are able to incorporate anti-HIV deoxynucleotides into DNA. 110uM Reaction: Nucleotide incorporation; Substrate: TTP analog; Technique: Steady State (Running start primer template)
Human Pol alpha Eukaryote B Human DNA polymerases alpha and beta are able to incorporate anti-HIV deoxynucleotides into DNA. 1.4uM Reaction: Nucleotide incorporation; Substrate: dTTP; Technique: Steady State (Running start primer template)
Human Pol alpha Eukaryote B Human DNA polymerases alpha and beta are able to incorporate anti-HIV deoxynucleotides into DNA. 2.1uM Reaction: Nucleotide incorporation; Substrate: dCTP; Technique: Steady State (Running start primer template)
Human Pol alpha Eukaryote B DNA polymerase insertion fidelity. Gel assay for site-specific kinetics. 3.7uM Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Gel shift
Human Pol alpha Eukaryote B DNA polymerase insertion fidelity. Gel assay for site-specific kinetics. 4200uM Reaction: Nucleotide incorporation; Substrate: dGTP; Technique: Gel shift
Human Pol alpha Eukaryote B DNA polymerase insertion fidelity. Gel assay for site-specific kinetics. 1E+04uM Reaction: Nucleotide incorporation; Substrate: dTTP; Technique: Gel shift
Human Pol alpha Eukaryote B DNA polymerase insertion fidelity. Gel assay for site-specific kinetics. 1E+04uM Reaction: Nucleotide incorporation; Substrate: dCTP; Technique: Gel shift
Human Pol alpha Eukaryote B DNA polymerase insertion fidelity. Gel assay for site-specific kinetics. 35uM Reaction: Nucleotide incorporation; Substrate: ATP analog; Technique: Gel shift
Human Pol alpha Eukaryote B Formation of 2-hydroxydeoxyadenosine triphosphate, an oxidatively damaged nucleotide, and its incorporation by DNA polymerases. Steady-state kinetics of the incorporation. 89uM Reaction: Nucleotide incorporation; Substrate: ATP analog; Technique: Steady State
Human Pol alpha Eukaryote B Formation of 2-hydroxydeoxyadenosine triphosphate, an oxidatively damaged nucleotide, and its incorporation by DNA polymerases. Steady-state kinetics of the incorporation. 0.2uM Reaction: Nucleotide incorporation; Substrate: dNTPs; Technique: Steady State
Human Pol delta Eukaryote B Abundant ribonucleotide incorporation into DNA by yeast replicative polymerases. 71uM Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Steady State
Human Pol delta Eukaryote B Kinetic analysis of nucleotide incorporation by mammalian DNA polymerase delta. 1.2uM Reaction: Nucleotide incorporation; Substrate: dCTP; Technique: Steady State (Without PCNA)
Human Pol delta Eukaryote B Kinetic analysis of nucleotide incorporation by mammalian DNA polymerase delta. 0.067uM Reaction: Nucleotide incorporation; Substrate: dCTP; Technique: Steady State (With PCNA)
Human Pol epsilon Eukaryote B Characterization of a large form of DNA polymerase delta from HeLa cells that is insensitive to proliferating cell nuclear antigen. 3uM Reaction: Polymerase-DNA interaction; Substrate: DNA template
Human Pol epsilon Eukaryote B Characterization of a large form of DNA polymerase delta from HeLa cells that is insensitive to proliferating cell nuclear antigen. 2.5uM Reaction: Nucleotide incorporation; Substrate: dTTP
Human Pol epsilon Eukaryote B Characterization of a large form of DNA polymerase delta from HeLa cells that is insensitive to proliferating cell nuclear antigen. 4.7uM Reaction: Nucleotide incorporation; Substrate: dNTPs
T4 D219AD324A Virus/Phage B Functional consequences and exonuclease kinetic parameters of point mutations in bacteriophage T4 DNA polymerase. 6.7uM Reaction: 3-5' Exonuclease; Substrate: DNA template
Sce Pol alpha Eukaryote B Purification and characterization of DNA polymerase II from the yeast Saccharomyces cerevisiae. Identification of the catalytic core and a possible holoenzyme form of the enzyme. 3.8uM Reaction: Nucleotide incorporation; Substrate: dNTPs
Sce Pol alpha Eukaryote B Purification and characterization of the 180- and 86-kilodalton subunits of the Saccharomyces cerevisiae DNA primase-DNA polymerase protein complex. The 180-kilodalton subunit has both DNA polymerase and 3'----5'-exonuclease activities. 7uM Reaction: Nucleotide incorporation; Substrate: dATP; Experimental conditions: Mg++ (1mM)
Sce Pol alpha Eukaryote B Purification and characterization of DNA polymerase II from the yeast Saccharomyces cerevisiae. Identification of the catalytic core and a possible holoenzyme form of the enzyme. 63nM Reaction: Polymerase-DNA interaction; Substrate: DNA template
T4 N698 Virus/Phage B Isolation, characterization, and kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3'-5' exonuclease activity. 3300uM Reaction: 3-5' Exonuclease; Substrate: DNA template
T4 N698 Virus/Phage B Isolation, characterization, and kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3'-5' exonuclease activity. 110uM Reaction: 3-5' Exonuclease; Substrate: DNA template
T4 N388 Virus/Phage B Isolation, characterization, and kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3'-5' exonuclease activity. 3800uM Reaction: 3-5' Exonuclease; Substrate: DNA template
T4 N388 Virus/Phage B Isolation, characterization, and kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3'-5' exonuclease activity. 1000uM Substrate: DNA template
T4 D112N Virus/Phage B Functional consequences and exonuclease kinetic parameters of point mutations in bacteriophage T4 DNA polymerase. 4uM Reaction: 3-5' Exonuclease; Substrate: DNA template
T4 E114A Virus/Phage B Functional consequences and exonuclease kinetic parameters of point mutations in bacteriophage T4 DNA polymerase. 2uM Reaction: 3-5' Exonuclease; Substrate: DNA template
T4 E114A Virus/Phage B Functional consequences and exonuclease kinetic parameters of point mutations in bacteriophage T4 DNA polymerase. 5uM Reaction: 3-5' Exonuclease; Substrate: DNA template
Pol eta Y52E Eukaryote Y Amino acid substitutions at conserved tyrosine 52 alter fidelity and bypass efficiency of human DNA polymerase eta. 448n/a Reaction: Nucleotide incorporation; Substrate: dCTP
Pol eta Y52E Eukaryote Y Amino acid substitutions at conserved tyrosine 52 alter fidelity and bypass efficiency of human DNA polymerase eta. 3.93n/a Reaction: Nucleotide incorporation; Substrate: dATP
Pol eta Y52E Eukaryote Y Amino acid substitutions at conserved tyrosine 52 alter fidelity and bypass efficiency of human DNA polymerase eta. 32n/a Reaction: Nucleotide incorporation; Substrate: dGTP
Pol eta Y52E Eukaryote Y Amino acid substitutions at conserved tyrosine 52 alter fidelity and bypass efficiency of human DNA polymerase eta. 3129n/a Reaction: Nucleotide incorporation; Substrate: dTTP
T7 (exo-) Virus/Phage A Pre-steady-state kinetic analysis of processive DNA replication including complete characterization of an exonuclease-deficient mutant. 800nM Reaction: 3-5' Exonuclease; Substrate: DNA template
Sce Pol II Eukaryote B Purification and characterization of DNA polymerase II from the yeast Saccharomyces cerevisiae. Identification of the catalytic core and a possible holoenzyme form of the enzyme. 6.2uM Reaction: Nucleotide incorporation; Substrate: dNTPs
Nf Virus/Phage B Functional characterization of highly processive protein-primed DNA polymerases from phages Nf and GA-1, endowed with a potent strand displacement capacity. 0.6uM Reaction: Nucleotide incorporation; Substrate: dNTPs
Sce Pol II* Eukaryote ? Purification and characterization of DNA polymerase II from the yeast Saccharomyces cerevisiae. Identification of the catalytic core and a possible holoenzyme form of the enzyme. 26nM Reaction: Polymerase-DNA interaction; Substrate: DNA template
Sce Pol II* Eukaryote ? Purification and characterization of DNA polymerase II from the yeast Saccharomyces cerevisiae. Identification of the catalytic core and a possible holoenzyme form of the enzyme. 7.5uM Reaction: Nucleotide incorporation; Substrate: dNTPs
FeLV RT Virus/Phage RT Comparison of DNA polymerase activities between recombinant feline immunodeficiency and leukemia virus reverse transcriptases. 2.546uM Reaction: Nucleotide incorporation; Substrate: dTTP
FeLV RT Virus/Phage RT Comparison of DNA polymerase activities between recombinant feline immunodeficiency and leukemia virus reverse transcriptases. 0.936uM Reaction: Nucleotide incorporation; Substrate: dGTP
FeLV RT Virus/Phage RT Comparison of DNA polymerase activities between recombinant feline immunodeficiency and leukemia virus reverse transcriptases. 1.481n/a Reaction: Nucleotide incorporation; Substrate: dCTP
FeLV RT Virus/Phage RT Comparison of DNA polymerase activities between recombinant feline immunodeficiency and leukemia virus reverse transcriptases. 4.674uM Reaction: Nucleotide incorporation; Substrate: dATP
FIV RT Virus/Phage RT Comparison of DNA polymerase activities between recombinant feline immunodeficiency and leukemia virus reverse transcriptases. 0.028uM Reaction: Nucleotide incorporation; Substrate: dCTP
FIV RT Virus/Phage RT Comparison of DNA polymerase activities between recombinant feline immunodeficiency and leukemia virus reverse transcriptases. 0.081uM Reaction: Nucleotide incorporation; Substrate: dATP
FIV RT Virus/Phage RT Comparison of DNA polymerase activities between recombinant feline immunodeficiency and leukemia virus reverse transcriptases. 0.06uM Reaction: Nucleotide incorporation; Substrate: dGTP
FIV RT Virus/Phage RT Comparison of DNA polymerase activities between recombinant feline immunodeficiency and leukemia virus reverse transcriptases. 0.051uM Reaction: Nucleotide incorporation; Substrate: dTTP
Pfu (exo-) ? ? DNA polymerases from hyperthermophiles. 12uM Reaction: Nucleotide incorporation; Substrate: dNTPs
Pfu (exo-) ? ? DNA polymerases from hyperthermophiles. 0.5nM Reaction: Polymerase-DNA interaction; Substrate: DNA template
Eco Pol III* Eubacterium C DNA polymerase 3 star requires ATP to start synthesis on a primed DNA. 8uM Reaction: Polymerase - NTP interaction; Substrate: dATP
Eco Pol III Holoenzyme Eubacterium C ATP activation of DNA polymerase III holoenzyme of Escherichia coli. I. ATP-dependent formation of an initiation complex with a primed template. 10uM Reaction: Nucleotide incorporation; Substrate: dNTPs; Experimental conditions: ATP (100µM)

Version:20241218

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