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Results for property: Kd

Detailed Results for Property

Use this page to examine all the the polymerases and references referring to the property: K<sub>d</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. 23nM Reaction: Polymerase-DNA interaction; Substrate: DNA template
T7 Virus/Phage A Pre-steady-state kinetic analysis of processive DNA replication including complete characterization of an exonuclease-deficient mutant. 18uM Reaction: Nucleotide incorporation; Substrate: dNTPs
T7 Virus/Phage A Expression, purification, and initial kinetic characterization of the large subunit of the human mitochondrial DNA polymerase. 18uM Reaction: Nucleotide incorporation; Substrate: dNTPs
T7 Virus/Phage A Expression, purification, and initial kinetic characterization of the large subunit of the human mitochondrial DNA polymerase. 18nM Reaction: Polymerase-DNA interaction; Substrate: DNA template
T7 Virus/Phage A Pre-steady-state kinetic analysis of processive DNA replication including complete characterization of an exonuclease-deficient mutant. 2000uM Reaction: Pyrophosphorolysis
RB69 Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 1715uM Reaction: Misincorporation; Substrate: dTTP
RB69 Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 2085uM Reaction: Misincorporation; Substrate: dCTP
RB69 Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 1986uM Reaction: Misincorporation; Substrate: dTTP
RB69 Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 1391uM Reaction: Misincorporation; Substrate: dTTP
RB69 Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 50uM Reaction: Nucleotide incorporation; Substrate: dATP
RB69 Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 909uM Reaction: Misincorporation; Substrate: dATP
RB69 Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 761uM Reaction: Misincorporation; Substrate: dGTP
RB69 Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 4500uM Reaction: Misincorporation; Substrate: dCTP
RB69 Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 725uM Reaction: Misincorporation; Substrate: dGTP
RB69 Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 3363uM Reaction: Misincorporation; Substrate: dCTP
RB69 Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 1800uM Reaction: Misincorporation; Substrate: dATP
RB69 Virus/Phage B Structure and enzymatic properties of a chimeric bacteriophage RB69 DNA polymerase and single-stranded DNA binding protein with increased processivity. 2.17nM
RB69 Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 784uM Reaction: Misincorporation; Substrate: dGTP
RB69 Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 811uM Reaction: Misincorporation; Substrate: dATP
RB69 Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 42uM Reaction: Nucleotide incorporation; Substrate: dTTP
RB69 Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 26uM Reaction: Nucleotide incorporation; Substrate: dGTP
RB69 Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 69uM Reaction: Nucleotide incorporation; Substrate: dCTP
RB69 Virus/Phage B Different behaviors in vivo of mutations in the beta hairpin loop of the DNA polymerases of the closely related phages T4 and RB69. 54nM Reaction: Polymerase-DNA interaction; Substrate: DNA template
Vent A488L Archaeon B Comparative kinetics of nucleotide analog incorporation by vent DNA polymerase. 24uM Reaction: Nucleotide incorporation; Substrate: CTP analog; Technique: Rapid quench ; Experimental conditions: Mg++ (2mM), pH (pH 8.8), Temp (60°C)
Vent A488L Archaeon B Comparative kinetics of nucleotide analog incorporation by vent DNA polymerase. 18uM Reaction: Nucleotide incorporation; Substrate: ddCTP; Technique: Rapid quench ; Experimental conditions: Mg++ (2mM), pH (pH 8.8), Temp (60°C)
Vent A488L Archaeon B Comparative kinetics of nucleotide analog incorporation by vent DNA polymerase. 77uM Reaction: Nucleotide incorporation; Substrate: dCTP; Technique: Rapid quench ; Experimental conditions: Mg++ (2mM), pH (pH 8.8), Temp (60°C)
Vent A488L Archaeon B Comparative kinetics of nucleotide analog incorporation by vent DNA polymerase. 360uM Reaction: Pyrophosphorolysis; Technique: Rapid quench ; Experimental conditions: Mg++ (2mM), pH (pH 8.8), Temp (60°C)
Vent A488L Archaeon B Comparative kinetics of nucleotide analog incorporation by vent DNA polymerase. 1100uM Reaction: Pyrophosphorolysis; Substrate: DNA template; Technique: Rapid quench ; Experimental conditions: Mg++ (2mM), pH (pH 8.8), Temp (60°C)
T4 D219A Virus/Phage B Function and assembly of the bacteriophage T4 DNA replication complex: interactions of the T4 polymerase with various model DNA constructs. 470nM Reaction: Polymerase-DNA interaction; Substrate: DNA template; Experimental conditions: pH (pH 7.5), Temp (20°C)
T4 D219A Virus/Phage B Kinetics of error generation in homologous B-family DNA polymerases. 13uM Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Single Turnover (across template T)
T4 D219A Virus/Phage B Kinetics of error generation in homologous B-family DNA polymerases. 934uM Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Single Turnover (across template F)
T4 D219A Virus/Phage B Construction and characterization of a bacteriophage T4 DNA polymerase deficient in 3'-->5' exonuclease activity. 40nM Reaction: 3-5' Exonuclease; Substrate: DNA template
T4 D219A Virus/Phage B Construction and characterization of a bacteriophage T4 DNA polymerase deficient in 3'-->5' exonuclease activity. 10uM Reaction: Nucleotide incorporation; Substrate: dATP
T4 D219A Virus/Phage B Function and assembly of the bacteriophage T4 DNA replication complex: interactions of the T4 polymerase with various model DNA constructs. 24nM Reaction: Polymerase-DNA interaction; Substrate: DNA template; Experimental conditions: pH (pH 7.5), Temp (20°C)
T4 D219A Virus/Phage B Function and assembly of the bacteriophage T4 DNA replication complex: interactions of the T4 polymerase with various model DNA constructs. 240nM Reaction: Polymerase-DNA interaction; Substrate: DNA template; Experimental conditions: pH (pH 7.5), Temp (20°C)
T4 D219A Virus/Phage B Function and assembly of the bacteriophage T4 DNA replication complex: interactions of the T4 polymerase with various model DNA constructs. 370nM Reaction: Polymerase-DNA interaction; Substrate: DNA template; Experimental conditions: pH (pH 7.5), Temp (20°C)
T4 D219A Virus/Phage B Function and assembly of the bacteriophage T4 DNA replication complex: interactions of the T4 polymerase with various model DNA constructs. 95nM Reaction: Polymerase-DNA interaction; Substrate: DNA template; Experimental conditions: pH (pH 7.5), Temp (20°C)
T4 D219A Virus/Phage B Function and assembly of the bacteriophage T4 DNA replication complex: interactions of the T4 polymerase with various model DNA constructs. 8nM Reaction: Polymerase-DNA interaction; Substrate: DNA template; Experimental conditions: pH (pH 7.5), Temp (20°C)
T4 D219A Virus/Phage B Function and assembly of the bacteriophage T4 DNA replication complex: interactions of the T4 polymerase with various model DNA constructs. 4nM Reaction: Polymerase-DNA interaction; Substrate: DNA template; Experimental conditions: pH (pH 7.5), Temp (20°C)
T4 Virus/Phage B Different behaviors in vivo of mutations in the beta hairpin loop of the DNA polymerases of the closely related phages T4 and RB69. 43nM Reaction: Polymerase-DNA interaction; Substrate: DNA template
T4 Virus/Phage B The dynamic processivity of the T4 DNA polymerase during replication. 145nM Reaction: Nucleotide incorporation; Substrate: dNTPs
RB69 D222AD327A Virus/Phage B Biochemical characterization of interactions between DNA polymerase and single-stranded DNA-binding protein in bacteriophage RB69. 353nM Reaction: Polymerase-DNA interaction; Substrate: DNA template; Technique: fluorescence titration (gp32 added)
RB69 D222AD327A Virus/Phage B Biochemical characterization of interactions between DNA polymerase and single-stranded DNA-binding protein in bacteriophage RB69. 124nM Reaction: Polymerase-DNA interaction; Substrate: DNA template; Technique: fluorescence titration
T4 G255S Virus/Phage B Different behaviors in vivo of mutations in the beta hairpin loop of the DNA polymerases of the closely related phages T4 and RB69. 24nM Reaction: Polymerase-DNA interaction
RB69 G258S Virus/Phage B Different behaviors in vivo of mutations in the beta hairpin loop of the DNA polymerases of the closely related phages T4 and RB69. 54nM Reaction: Polymerase-DNA interaction; Substrate: DNA template
T4 D112AE114A Virus/Phage B Kinetics of error generation in homologous B-family DNA polymerases. 11uM Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Single Turnover (across template T)
T4 D112AE114A Virus/Phage B Using 2-aminopurine fluorescence to detect base unstacking in the template strand during nucleotide incorporation by the bacteriophage T4 DNA polymerase. 10uM Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Rapid quench
T4 D112AE114A Virus/Phage B Using 2-aminopurine fluorescence to detect base unstacking in the template strand during nucleotide incorporation by the bacteriophage T4 DNA polymerase. 16.2uM Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Rapid quench
T4 D112AE114A Virus/Phage B Using 2-aminopurine fluorescence to measure incorporation of incorrect nucleotides by wild type and mutant bacteriophage T4 DNA polymerases. 31uM Reaction: Nucleotide incorporation; Substrate: dTTP; Technique: Rapid quench (opposite template A)
T4 D112AE114A Virus/Phage B Kinetics of error generation in homologous B-family DNA polymerases. 915uM Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Single Turnover (across template F)
T4 D112AE114A Virus/Phage B Dynamics of nucleotide incorporation: snapshots revealed by 2-aminopurine fluorescence studies. 31uM Reaction: Nucleotide incorporation; Substrate: dTTP; Technique: Rapid quench (across template 2AP)
T4 D324A Virus/Phage B Kinetics of error generation in homologous B-family DNA polymerases. 18uM Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Single Turnover (across template T)
T4 D324A Virus/Phage B Kinetics of error generation in homologous B-family DNA polymerases. 897uM Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Single Turnover (across template F)
RB69 D114AE116A Virus/Phage B Kinetics of error generation in homologous B-family DNA polymerases. 832uM Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Single Turnover (across template F)
RB69 D114AE116A Virus/Phage B Kinetics of error generation in homologous B-family DNA polymerases. 47uM Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Single Turnover (across template T)
RB69 D222A Virus/Phage B Kinetics of error generation in homologous B-family DNA polymerases. 42uM Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Single Turnover (across template T)
RB69 D222A Virus/Phage B Kinetics of error generation in homologous B-family DNA polymerases. 1767uM Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Single Turnover (across template F)
RB69 D327A Virus/Phage B Kinetics of error generation in homologous B-family DNA polymerases. 1210uM Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Single Turnover (across template F)
RB69 D327A Virus/Phage B Kinetics of error generation in homologous B-family DNA polymerases. 47uM Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Single Turnover (across template T)
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 1200uM Reaction: Polymerase - NTP interaction; Substrate: Deoxyadenosine 3’-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 144uM Reaction: Polymerase - NTP interaction; Substrate: 6-mercaptopurine ribonucleoside 5’-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 69uM Reaction: Polymerase - NTP interaction; Substrate: 6-methylmcrcaptopurinc ribonuclcosidc 5’-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 23uM Reaction: Polymerase - NTP interaction; Substrate: 4’-deoxy-4’-thioadenine ribonucleoside 5’-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 3000uM Reaction: Polymerase - NTP interaction; Substrate: 3'-O-methyl AMP; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 2600uM Reaction: Polymerase - NTP interaction; Substrate: 2’-deoxyadenosine; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 2800uM Reaction: Polymerase - NTP interaction; Substrate: Thymidine 5’-phosphonate ; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 3700uM Reaction: Polymerase - NTP interaction; Substrate: 2’,3’-dideoxythymidine 5’-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 167uM Reaction: Polymerase - NTP interaction; Substrate: Purine deoxyribonucleoside 5’-phosphate ; Technique: Equilibrium Dialysis ; Experimental conditions: pH (pH 7.4), PP (50mM)
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 87uM Reaction: Polymerase - NTP interaction; Substrate: 5-fluorouracil deoxyribonucleoside 5'-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: pH (pH 7.4), PP (50mM)
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 2600uM Reaction: Polymerase - NTP interaction; Substrate: Deoxycytidine 3’-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 3000uM Reaction: Polymerase - NTP interaction; Substrate: Thymidylyl-(5’,3’)-thymidine 5’-triphosphate ; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 2800uM Reaction: Polymerase - NTP interaction; Substrate: guanosine 5’-methane phosphonate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 4000uM Reaction: Polymerase - NTP interaction; Substrate: 3’-O-methyl-fluorouracil deoxyribonucleoside 5’-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 900uM Reaction: Polymerase - NTP interaction; Substrate: Nicotinamide ribonucleoside 5’-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 2300uM Reaction: Polymerase - NTP interaction; Substrate: Uracil xylonucleoside 5’-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 1000uM Reaction: Polymerase - NTP interaction; Substrate: Deoxy-guanosine 3’-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 3400uM Reaction: Polymerase - NTP interaction; Substrate: Thymidine 3’,5’-diphosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 4200uM Reaction: Polymerase - NTP interaction; Substrate: Barbituric acid ribonucleoside 5’-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 3000uM Reaction: Polymerase - NTP interaction; Substrate: Uracil lyxonucleoside 5’-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 35uM Reaction: Polymerase - NTP interaction; Substrate: AMP; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 2700uM Reaction: Polymerase - NTP interaction; Substrate: Adenine-3’-deoxylyxonucleoside 5’-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 3700uM Reaction: Polymerase - NTP interaction; Substrate: Uracil arabinonucleoside 5’-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 2600uM Reaction: Polymerase - NTP interaction; Substrate: Thymine arabinonucleoside 5’-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 1700uM Reaction: Polymerase - NTP interaction; Substrate: 2’,3’-dideoxyadenosine 5’-phosphate ; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 3000uM Reaction: Polymerase - NTP interaction; Substrate: Adenosine 5’-phosphite; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 2300uM Reaction: Polymerase - NTP interaction; Substrate: Adenine arabinonucleoside 5’-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 3000uM Reaction: Polymerase - NTP interaction; Substrate: Deoxythymidine 3’-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 62uM Reaction: Polymerase - NTP interaction; Substrate: Aristeromycin 6'-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: pH (pH 7.4), PP (50mM)
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 3100uM Reaction: Polymerase - NTP interaction; Substrate: 5'-fluorouracil arabinonucleoside 5'-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 3900uM Reaction: Polymerase - NTP interaction; Substrate: Adenine xylonucleoside 5’-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 3400uM Reaction: Polymerase - NTP interaction; Substrate: 2’,3’-dideoxy-2’,3’-didehydroadenosine 5’-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Eubacterium A Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 3900uM Reaction: Polymerase - NTP interaction; Substrate: Adenine-2’-deoxylyxonucleoside 5’-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Klenow fragment Eubacterium A Expression, purification, and initial kinetic characterization of the large subunit of the human mitochondrial DNA polymerase. 17uM Reaction: Nucleotide incorporation; Substrate: dNTPs
Klenow fragment Eubacterium A Expression, purification, and initial kinetic characterization of the large subunit of the human mitochondrial DNA polymerase. 5nM 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. 42nM Reaction: Polymerase-DNA interaction; Substrate: DNA template
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. 114uM Reaction: Nucleotide incorporation; Substrate: dCTP; Technique: Steady State (template G)
Human Pol eta Eukaryote Y Yeast DNA polymerase eta utilizes an induced-fit mechanism of nucleotide incorporation. 11nM Reaction: Polymerase-DNA interaction; Substrate: DNA template
Human Pol eta Eukaryote Y Yeast DNA polymerase eta utilizes an induced-fit mechanism of nucleotide incorporation. 2.4nM Reaction: Nucleotide incorporation; Substrate: dATP
Human Pol eta Eukaryote Y Yeast DNA polymerase eta utilizes an induced-fit mechanism of nucleotide incorporation. 13uM Reaction: Misincorporation; Substrate: dCTP
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. 190uM 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. 100uM Reaction: Nucleotide incorporation; Substrate: dCTP; Technique: Steady State
Human Pol gamma Eukaryote A Expression, purification, and initial kinetic characterization of the large subunit of the human mitochondrial DNA polymerase. 14uM Reaction: Nucleotide incorporation; Substrate: dTTP
Human Pol gamma Eukaryote A A novel processive mechanism for DNA synthesis revealed by structure, modeling and mutagenesis of the accessory subunit of human mitochondrial DNA polymerase. 10.2nM Reaction: Polymerase-DNA interaction; Substrate: DNA template
Human Pol gamma Eukaryote A Expression, purification, and initial kinetic characterization of the large subunit of the human mitochondrial DNA polymerase. 39nM Reaction: Polymerase-DNA interaction; Substrate: DNA template
Human Pol beta Eukaryote X Mismatched and matched dNTP incorporation by DNA polymerase beta proceed via analogous kinetic pathways. 489uM Reaction: Nucleotide incorporation; Substrate: dGTP; Technique: Steady State (T template)
Human Pol beta Eukaryote X Mismatched and matched dNTP incorporation by DNA polymerase beta proceed via analogous kinetic pathways. 6.8uM Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Steady State (T template)
Human Pol beta Eukaryote X Mismatched and matched dNTP incorporation by DNA polymerase beta proceed via analogous kinetic pathways. 2.2uM Reaction: Nucleotide incorporation; Substrate: dGTP; Technique: Steady State (C template)
Human Pol beta Eukaryote X Human DNA polymerases alpha and beta are able to incorporate anti-HIV deoxynucleotides into DNA. 2uM Reaction: Nucleotide incorporation; Substrate: ddCTP; 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. 810uM Reaction: Nucleotide incorporation; Substrate: TTP analog; Technique: Steady State (Activated DNA)
Human Pol beta Eukaryote X Hinge residue I174 is critical for proper dNTP selection by DNA polymerase beta. 590uM Reaction: Misincorporation; Substrate: dTTP; Technique: Single Turnover (G template)
Human Pol beta Eukaryote X Hinge residue I174 is critical for proper dNTP selection by DNA polymerase beta. 72uM Reaction: Misincorporation; Substrate: dATP; Technique: Single Turnover (G template)
Human Pol beta Eukaryote X Hinge residue I174 is critical for proper dNTP selection by DNA polymerase beta. 120uM Reaction: Misincorporation; Substrate: dGTP; Technique: Single Turnover (G template)
Human Pol beta Eukaryote X Mismatched and matched dNTP incorporation by DNA polymerase beta proceed via analogous kinetic pathways. 227uM Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Steady State (C template)
Human Pol beta Eukaryote X Hinge residue I174 is critical for proper dNTP selection by DNA polymerase beta. 9uM Reaction: Misincorporation; Substrate: dCTP; Technique: Single Turnover (G template)
HIV RT Virus/Phage RT Human immunodeficiency virus 1 reverse transcriptase. Template binding, processivity, strand displacement synthesis, and template switching. 2.3uM Reaction: Polymerase-DNA interaction; Substrate: RNA-DNA hybrid
HIV RT Virus/Phage RT Expression, purification, and initial kinetic characterization of the large subunit of the human mitochondrial DNA polymerase. 4.7nM Reaction: Polymerase-DNA interaction; Substrate: DNA template
HIV RT Virus/Phage RT Expression, purification, and initial kinetic characterization of the large subunit of the human mitochondrial DNA polymerase. 14uM Reaction: Nucleotide incorporation; Substrate: dNTPs
KF Y766S Eubacterium A Identification of residues critical for the polymerase activity of the Klenow fragment of DNA polymerase I from Escherichia coli. 20n/a Reaction: Polymerase-DNA interaction; Substrate: DNA template; Technique: DNase I Protection ; Experimental conditions: Mg++ (2mM), Temp (22°C), pH (pH 7.5)
RB69 L561A Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 537uM Reaction: Misincorporation; Substrate: dCTP
RB69 L561A Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 50uM Reaction: Nucleotide incorporation; Substrate: dCTP
RB69 L561A Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 2010uM Reaction: Misincorporation; Substrate: dCTP
RB69 L561A Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 251uM Reaction: Misincorporation; Substrate: dGTP
RB69 L561A Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 161uM Reaction: Misincorporation; Substrate: dGTP
RB69 L561A Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 310uM Reaction: Misincorporation; Substrate: dATP
RB69 L561A Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 368uM Reaction: Misincorporation; Substrate: dATP
RB69 L561A Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 228uM Reaction: Misincorporation; Substrate: dGTP
RB69 L561A Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 30uM Reaction: Nucleotide incorporation; Substrate: dATP
RB69 L561A Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 155uM Reaction: Misincorporation; Substrate: dATP
RB69 L561A Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 205uM Reaction: Misincorporation; Substrate: dTTP
RB69 L561A Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 51uM Reaction: Nucleotide incorporation; Substrate: dTTP
RB69 L561A Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 28uM Reaction: Misincorporation; Substrate: dTTP
RB69 L561A Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 17uM Reaction: Nucleotide incorporation; Substrate: dGTP
RB69 L561A Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 1467uM Reaction: Misincorporation; Substrate: dCTP
RB69 L561A Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 507uM Reaction: Misincorporation; Substrate: dTTP
Human Pol alpha Eukaryote B Human DNA polymerases alpha and beta are able to incorporate anti-HIV deoxynucleotides into DNA. 120uM Reaction: Nucleotide incorporation; Substrate: ddCTP; 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. 650uM Reaction: Nucleotide incorporation; Substrate: TTP analog; Technique: Steady State (Activated DNA)
Pol beta I260Q Eukaryote X Mismatched and matched dNTP incorporation by DNA polymerase beta proceed via analogous kinetic pathways. 49uM Reaction: Nucleotide incorporation; Substrate: dGTP; Technique: Steady State (T template)
Pol beta I260Q Eukaryote X Mismatched and matched dNTP incorporation by DNA polymerase beta proceed via analogous kinetic pathways. 2.2uM Reaction: Nucleotide incorporation; Substrate: dGTP; Technique: Steady State (C template )
Pol beta I260Q Eukaryote X Mismatched and matched dNTP incorporation by DNA polymerase beta proceed via analogous kinetic pathways. 45uM Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Steady State (C template)
Pol beta I260Q Eukaryote X Mismatched and matched dNTP incorporation by DNA polymerase beta proceed via analogous kinetic pathways. 7.1uM Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Steady State (T template)
T7 (exo-) Virus/Phage A Pre-steady-state kinetic analysis of processive DNA replication including complete characterization of an exonuclease-deficient mutant. 2000uM Reaction: Pyrophosphorolysis
T7 (exo-) Virus/Phage A Pre-steady-state kinetic analysis of processive DNA replication including complete characterization of an exonuclease-deficient mutant. 16nM Reaction: Polymerase-DNA interaction; Substrate: DNA template
T7 (exo-) Virus/Phage A Pre-steady-state kinetic analysis of processive DNA replication including complete characterization of an exonuclease-deficient mutant. 21uM Reaction: Nucleotide incorporation; Substrate: dNTPs
SsoDpo1 Archaeon B A trimeric DNA polymerase complex increases the native replication processivity. 542nM
SsoDpo1 Archaeon B A trimeric DNA polymerase complex increases the native replication processivity. 1.2uM
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. 1.5nM Reaction: Nucleotide incorporation; Substrate: dNTPs
RB69-SSO-F6 Virus/Phage ? Structure and enzymatic properties of a chimeric bacteriophage RB69 DNA polymerase and single-stranded DNA binding protein with increased processivity. 0.38nM
Eco Pol III Holoenzyme Eubacterium C The cycling of Escherichia coli DNA polymerase III holoenzyme in replication. 0.8uM Reaction: Polymerase - NTP interaction; Substrate: dATP

Version:20240424

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