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Results for property: kcat

Detailed Results for Property

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

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Polymerase Kingdom Family Reference Result Context
T4 W213S Virus/Phage B DNA polymerase proofreading: active site switching catalyzed by the bacteriophage T4 DNA polymerase. 1.5 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: Mg++ (8mM), Temp (37°C)
T4 Virus/Phage B DNA polymerase proofreading: active site switching catalyzed by the bacteriophage T4 DNA polymerase. 145 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover (with heparin); Experimental conditions: Temp (37°C), Mg++ (8mM)
T4 Virus/Phage B DNA polymerase proofreading: active site switching catalyzed by the bacteriophage T4 DNA polymerase. 106 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Multiple Turnover (without heparin); Experimental conditions: Mg++ (8mM), Temp (37°C)
KF Y766S Eubacterium A Identification of residues critical for the polymerase activity of the Klenow fragment of DNA polymerase I from Escherichia coli. 0.8 /second Reaction: Nucleotide incorporation; Substrate: dNTPs; Technique: Rapid quench
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. 0.09 /second 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 The 3'-5' exonuclease of DNA polymerase I of Escherichia coli: contribution of each amino acid at the active site to the reaction. 0.12 /second Reaction: 3-5' Exonuclease; Technique: Steady State (ssDNA: poly(dA)); Experimental conditions: pH (pH 7.5), Mg++ (8mM), Temp (37°C)
Klenow fragment Eubacterium A Fingers-closing and other rapid conformational changes in DNA polymerase I (Klenow fragment) and their role in nucleotide selectivity. 140 /second Reaction: Nucleotide incorporation; Substrate: dNTPs; Technique: Stopped flow (FRET assay of fingers-closing); Experimental conditions: pH (pH 7.5), Mg++ (5mM), Temp (22°C)
KF E357A ? ? The 3'-5' exonuclease of DNA polymerase I of Escherichia coli: contribution of each amino acid at the active site to the reaction. 1.8E-06 /second Reaction: 3-5' Exonuclease; Technique: Steady State (dsDNA, assuming WT has rate 0.001/s); Experimental conditions: pH (pH 7.5), Mg++ (6mM), Temp (37°C)
KF L361A Eubacterium ? The 3'-5' exonuclease of DNA polymerase I of Escherichia coli: contribution of each amino acid at the active site to the reaction. 0.044 /second Reaction: 3-5' Exonuclease; Technique: Steady State (ssDNA, poly(dA)); Experimental conditions: pH (pH 7.5), Mg++ (8mM), Temp (37°C)
KF L361A Eubacterium ? The 3'-5' exonuclease of DNA polymerase I of Escherichia coli: contribution of each amino acid at the active site to the reaction. 4E-05 /second Reaction: 3-5' Exonuclease; Technique: Steady State (dsDNA, assuming WT has rate 0.001/s); Experimental conditions: pH (pH 7.5), Mg++ (6mM), Temp (37°C)
KF L361M Eubacterium ? The 3'-5' exonuclease of DNA polymerase I of Escherichia coli: contribution of each amino acid at the active site to the reaction. 8.3E-05 /second Reaction: 3-5' Exonuclease; Technique: Steady State (dsDNA, assuming WT has rate 0.001/s); Experimental conditions: pH (pH 7.5), Mg++ (6mM), Temp (37°C)
KF D424A 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. 1.3E-08 /second Reaction: 3-5' Exonuclease; Technique: Steady State (dsDNA, assuming WT has rate 0.001/s); Experimental conditions: pH (pH 7.5), Temp (37°C)
Terminal Transferase Unknown ? Terminal deoxynucleotidyl transferase indiscriminately incorporates ribonucleotides and deoxyribonucleotides. 76 /minute Reaction: Nucleotide incorporation; Substrate: rATP
Terminal Transferase Unknown ? Terminal deoxynucleotidyl transferase indiscriminately incorporates ribonucleotides and deoxyribonucleotides. 180 /minute Reaction: Nucleotide incorporation; Substrate: dATP
Terminal Transferase Unknown ? Terminal deoxynucleotidyl transferase indiscriminately incorporates ribonucleotides and deoxyribonucleotides. 147 /minute Reaction: Nucleotide incorporation; Substrate: dATP
Terminal Transferase Unknown ? Terminal deoxynucleotidyl transferase indiscriminately incorporates ribonucleotides and deoxyribonucleotides. 11.3 /minute Reaction: Nucleotide incorporation; Substrate: dATP
Bst LF Eubacterium A Crystal structure of a thermostable Bacillus DNA polymerase I large fragment at 2.1 A resolution. 191.2 /second Reaction: Nucleotide incorporation; Substrate: dNTPs; Technique: Filter binding (16.5 nM primed M13); Experimental conditions: Temp (65°C)
Taq pol I Eubacterium A Crystal structure of a thermostable Bacillus DNA polymerase I large fragment at 2.1 A resolution. 46.6 /second Reaction: Nucleotide incorporation; Substrate: dNTPs; Technique: Filter binding (16.5nM primed M13); Experimental conditions: Temp (72°C)
KF D424E 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. 0.01 /second Reaction: 3-5' Exonuclease; Technique: Steady State (ssDNA, poly(dA)); Experimental conditions: pH (pH 7.5), Mg++ (8mM), Temp (37°C)
KF D424E 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. 4E-05 /second Reaction: 3-5' Exonuclease; Technique: Steady State (dsDNA, assuming WT has rate 0.001/s); Experimental conditions: pH (pH 7.5), Mg++ (6mM), Temp (37°C)
KF D355A 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. 8.3E-08 /second Reaction: 3-5' Exonuclease; Technique: Steady State (dsDNA substrate, assuming WT has rate 0.001/s); Experimental conditions: pH (pH 7.5), Mg++ (6mM), Temp (37°C)
KF F473A ? ? The 3'-5' exonuclease of DNA polymerase I of Escherichia coli: contribution of each amino acid at the active site to the reaction. 2.9E-07 /second Reaction: 3-5' Exonuclease; Technique: Steady State (dsDNA, assuming WT has rate 0.001/s); Experimental conditions: pH (pH 7.5), Temp (37°C)
KF D424N 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. 2.5E-08 /second Reaction: 3-5' Exonuclease; Technique: Steady State (dsDNA, assuming WT has rate 0.001/s); Experimental conditions: pH (pH 7.5), Mg++ (6mM), Temp (37°C)
KF D510E ? ? The 3'-5' exonuclease of DNA polymerase I of Escherichia coli: contribution of each amino acid at the active site to the reaction. 5.6E-06 /second Reaction: 3-5' Exonuclease; Technique: Steady State (dsDNA, assuming WT has rate 0.001/s); Experimental conditions: pH (pH 7.5), Mg++ (6mM), Temp (37°C)
KF D501A ? ? The 3'-5' exonuclease of DNA polymerase I of Escherichia coli: contribution of each amino acid at the active site to the reaction. 7.5E-08 /second Reaction: 3-5' Exonuclease; Technique: Steady State (dsDNA, assuming WT has rate 0.001/s); Experimental conditions: pH (pH 7.5), Mg++ (6mM), Temp (37°C)
KF Y497F ? ? The 3'-5' exonuclease of DNA polymerase I of Escherichia coli: contribution of each amino acid at the active site to the reaction. 0.0019 /second Reaction: 3-5' Exonuclease; Technique: Steady State (ssDNA, poly(dA)); Experimental conditions: pH (pH 7.5), Mg++ (8mM), Temp (37°C)
KF Y497F ? ? The 3'-5' exonuclease of DNA polymerase I of Escherichia coli: contribution of each amino acid at the active site to the reaction. 4.3E-05 /second Reaction: 3-5' Exonuclease; Technique: Steady State (dsDNA, assuming WT has rate 0.001/s); Experimental conditions: pH (pH 7.5), Mg++ (6mM), Temp (37°C)
KF D510N ? ? The 3'-5' exonuclease of DNA polymerase I of Escherichia coli: contribution of each amino acid at the active site to the reaction. 0.0005 /second Reaction: 3-5' Exonuclease; Technique: Steady State (dsDNA, assuming WT has rate 0.001/s); Experimental conditions: pH (pH 7.5), Temp (37°C)
RB69 D114AE116A Virus/Phage B Kinetics of error generation in homologous B-family DNA polymerases. 270 /second Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Single Turnover (across template T)
RB69 D114AE116A Virus/Phage B Kinetics of error generation in homologous B-family DNA polymerases. 0.43 /second Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Single Turnover (across template F)
T4 Virus/Phage B Mutational and pH studies of the 3' --> 5' exonuclease activity of bacteriophage T4 DNA polymerase. 200 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Degradation of labeled single-stranded DNA
T4 D324A Virus/Phage B Mutational and pH studies of the 3' --> 5' exonuclease activity of bacteriophage T4 DNA polymerase. 0.01 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Degradation of labeled single-stranded DNA (9.5)
T4 Y320FD324A Virus/Phage B Mutational and pH studies of the 3' --> 5' exonuclease activity of bacteriophage T4 DNA polymerase. 0.1 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Degradation of labeled single-stranded DNA
T4 D112AE114A Virus/Phage B Kinetics of error generation in homologous B-family DNA polymerases. 361 /second Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Single Turnover (across template T)
T4 D112AE114A Virus/Phage B Kinetics of error generation in homologous B-family DNA polymerases. 3.24 /second Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Single Turnover (across template F)
T4 D324A Virus/Phage B Kinetics of error generation in homologous B-family DNA polymerases. 180 /second 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. 2.13 /second 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. 224 /second Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Single Turnover (across template T)
RB69 D327A Virus/Phage B Kinetics of error generation in homologous B-family DNA polymerases. 0.53 /second Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Single Turnover (across template F)
T4 D219A Virus/Phage B Kinetics of error generation in homologous B-family DNA polymerases. 402 /second 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. 3.36 /second Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Single Turnover (across template F)
T4 D219A Virus/Phage B Kinetics of error generation in homologous B-family DNA polymerases. 0.56 /second Reaction: Misincorporation; Substrate: dATP; Technique: Multiple Turnover (across template C)
T4 D219A Virus/Phage B Kinetics of error generation in homologous B-family DNA polymerases. 0.18 /second Reaction: Misincorporation; Substrate: dTTP; Technique: Multiple Turnover (across template T)
RB69 D222A Virus/Phage B Kinetics of error generation in homologous B-family DNA polymerases. 320 /second 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. 0.97 /second Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Single Turnover (across template F)
RB69 D222A Virus/Phage B Kinetics of error generation in homologous B-family DNA polymerases. 0.43 /second Reaction: Misincorporation; Substrate: dATP; Technique: Multiple Turnover (across template C)
RB69 D222A Virus/Phage B Kinetics of error generation in homologous B-family DNA polymerases. 0.04 /second Reaction: Misincorporation; Substrate: dTTP; Technique: Multiple Turnover (across template T)
Klenow fragment Eubacterium A Isolation, characterization, and kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3'-5' exonuclease activity. 5.8 /second Reaction: 3-5' Exonuclease; Substrate: DNA template
Klenow fragment Eubacterium A Isolation, characterization, and kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3'-5' exonuclease activity. 7.8 /second 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. 170 /second 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. 420 /second 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. 170 /second 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. 270 /second Reaction: 3-5' Exonuclease
T4 N388 Virus/Phage B Isolation, characterization, and kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3'-5' exonuclease activity. 170 /second 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. 3 /second Reaction: Nucleotide incorporation; Substrate: dATP
T4 Virus/Phage B Functional consequences and exonuclease kinetic parameters of point mutations in bacteriophage T4 DNA polymerase. 65.1 /second 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. 0.16 /second 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. 0.0078 /second 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. 0.0037 /second Reaction: 3-5' Exonuclease; Substrate: DNA template
T4 D112N Virus/Phage B Functional consequences and exonuclease kinetic parameters of point mutations in bacteriophage T4 DNA polymerase. 0.001 /second 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. 2 /second 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. 0.08 /second Reaction: 3-5' Exonuclease; Substrate: DNA template
T4 D219AD324A Virus/Phage B Functional consequences and exonuclease kinetic parameters of point mutations in bacteriophage T4 DNA polymerase. 0.0034 /second 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. 0.096 /second 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. 6E-05 /second 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. 0.0062 /second 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. 7E-05 /second Reaction: 3-5' Exonuclease; Substrate: DNA template
RB69 K302A Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.0011 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 6.5)
RB69 Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 0.004 /second 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. 0.011 /second 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. 0.77 /second 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. 0.041 /second 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. 0.001 /second 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. 0.09 /second Reaction: Misincorporation; Substrate: dTTP
RB69 K302A Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.0033 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 7)
RB69 K302A Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.01 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 7.5)
RB69 K302A Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.032 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 8)
RB69 K302A Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.11 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 8.5)
RB69 Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 0.013 /second 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. 0.14 /second 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. 0.015 /second 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. 220 /second 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. 200 /second Reaction: Nucleotide incorporation; Substrate: dCTP
RB69 Virus/Phage B The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 167 /second 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. 240 /second 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. 0.013 /second 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. 0.003 /second 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. 0.08 /second 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. 0.03 /second 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. 0.11 /second 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. 0.26 /second 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. 0.18 /second 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. 0.03 /second 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. 0.8 /second 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. 0.14 /second 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. 0.05 /second 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. 0.13 /second 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. 108 /second 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. 89 /second 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. 101 /second 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. 115 /second 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. 0.03 /second 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. 0.01 /second 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. 0.75 /second Reaction: Misincorporation; Substrate: dATP
RB69 E116A Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 3.9E-05 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 6.5)
RB69 E116A Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.00011 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 7)
RB69 E116A Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.00028 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 7.5)
RB69 E116A Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.00075 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 8)
RB69 E116A Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.00053 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 8.5)
RB69 Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 17 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover (Substrat: 3'-tailed duplex phosphorothioate)
RB69 Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 3 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 6.5)
RB69 Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 5 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 7)
RB69 Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 6.6 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 7.5)
RB69 Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 7.7 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 8)
RB69 Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 8.1 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 8.5)
RB69 Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 24 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover (Substrate: 3'-tailed duplex all-oxygen substrate)
T4 Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 130 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover (Substrate: 3'-tailed duplex all-oxygen substrate)
T4 Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 91 /second Reaction: 3-5' Exonuclease; Substrate: DNA template
T4 K229A Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.18 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover (Substrate: 3'-tailed duplex all-oxygen substrate)
T4 K229A Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.05 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover (Substrate: 3'-tailed duplex phosphorothioate substrate)
RB69 Y323F Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.14 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover (Substrate: 3'-tailed duplex all-oxygen substrate)
RB69 Y323F Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.00056 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 6.5)
RB69 Y323F Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.0018 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 7)
RB69 Y323F Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.0058 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 7.5)
RB69 Y323F Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.019 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 8)
RB69 Y323F Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.056 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 8.5)
RB69 Y323F Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.0013 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover (Substrate: 3'-tailed duplex phosphorothioate substrate)
T4 Y320F Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.12 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover (Substrate: 3'-tailed duplex all-oxygen substrate)
T4 Y320F Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.00096 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ( Substrate: 3'-tailed duplex phosphorothioate substrate)
T4 Y320A Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.075 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover (Substrate: 3'-tailed duplex all-oxygen substrate)
T4 Y320A Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.0085 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover (Substrate: 3'-tailed duplex phosphorothioate substrate)
T4 K299AY320F Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.013 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ( Substrate: 3'-tailed duplex phosphorothioate substrate)
T4 K299AY320F Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.0005 /second Reaction: 3-5' Exonuclease; Substrate: DNA template
RB69 K302AY323F Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.013 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover (Substrate: 3'-tailed duplex all-oxygen substrate)
RB69 K302AY323F Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.00081 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover (Substrate: 3'-tailed duplex phosphorothioate substrate)
RB69 K302AY323F Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.02 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover (Substrate: 3'-tailed duplex phosphorothioate substrate)
RB69 K302AY323F Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 2.1E-05 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 6.5)
RB69 K302AY323F Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 6.5E-05 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 7)
RB69 K302AY323F Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.0002 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 7.5)
RB69 K302AY323F Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.00064 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 8)
RB69 K302AY323F Virus/Phage B Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.002 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 8.5)
Klenow fragment Eubacterium A Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.02 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ( Substrate: 3'-tailed duplex phosphorothioate substrate)
Klenow fragment Eubacterium A Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.0017 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 6.5)
Klenow fragment Eubacterium A Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.0054 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 7)
Klenow fragment Eubacterium A Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.016 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 7.5)
Klenow fragment Eubacterium A Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.052 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 8)
Klenow fragment Eubacterium A Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.16 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 8.5)
Klenow fragment Eubacterium A Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. 0.33 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover (Substrate: 3'-tailed duplex all-oxygen substrate)
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. 0.58 /second Reaction: Nucleotide incorporation; Substrate: dCTP; 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. 0.055 /second Reaction: Nucleotide incorporation; Substrate: dCTP; 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. 0.0066 /second 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. 0.0025 /second 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. 0.00083 /second Reaction: Nucleotide incorporation; Substrate: dGTP; Technique: Steady State (O6-BzG)
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. 0.8 /second Reaction: Nucleotide incorporation; Substrate: dCTP; Technique: Steady State (Template G)
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. 0.47 /second Reaction: Nucleotide incorporation; Substrate: dCTP; Technique: Steady State
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. 0.34 /second Reaction: Nucleotide incorporation; Substrate: dCTP; 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. 0.5 /minute Reaction: Nucleotide incorporation; Substrate: dCTP; 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. 0.43 /minute Reaction: Nucleotide incorporation; Substrate: dTTP; Technique: Steady State
Human Pol gamma Eukaryote A Expression, purification, and initial kinetic characterization of the large subunit of the human mitochondrial DNA polymerase. 0.03 /second
Human Pol gamma Eukaryote A Expression, purification, and initial kinetic characterization of the large subunit of the human mitochondrial DNA polymerase. 0.18 /second Reaction: 3-5' Exonuclease; Substrate: DNA 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. 0.12 /minute Reaction: Nucleotide incorporation; Substrate: dGTP; 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. 0.77 /minute Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Steady State
Human Pol delta Eukaryote B Kinetic analysis of nucleotide incorporation by mammalian DNA polymerase delta. 0.36 /minute Reaction: Nucleotide incorporation; Substrate: dCTP; Technique: Steady State (With PCNA)
Human Pol delta Eukaryote B Kinetic analysis of nucleotide incorporation by mammalian DNA polymerase delta. 0.3 /minute Reaction: Nucleotide incorporation; Substrate: dCTP; Technique: Steady State (Without PCNA)
Bst LF Eubacterium A Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. 191.2 /second Reaction: Nucleotide incorporation; Substrate: dNTPs
Taq pol I Eubacterium A Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. 46.6 /second Reaction: Nucleotide incorporation; Substrate: dNTPs
Klenow fragment Eubacterium A Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. 5.2 /second Reaction: Nucleotide incorporation; Substrate: dNTPs
Human Pol eta Eukaryote Y Yeast DNA polymerase eta utilizes an induced-fit mechanism of nucleotide incorporation. 0.01 /second Reaction: Nucleotide incorporation; Substrate: dNTPs
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. 0.025 /second 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. 1.9 /second Reaction: Nucleotide incorporation; Substrate: dNTPs; 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. 0.071 /second Reaction: Nucleotide incorporation; Substrate: TTP analog; Technique: Rapid quench (RNA template)
GA-1 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. 2260 /minute Reaction: Nucleotide incorporation; Substrate: dNTPs
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. 0.3 /second Reaction: Nucleotide incorporation; Substrate: dTTP
Vent A488L Archaeon B Comparative kinetics of nucleotide analog incorporation by vent DNA polymerase. 0.47 /second Reaction: Nucleotide incorporation; Substrate: ddCTP; Technique: Rapid quench (burst conditions); 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. 13 /second Technique: Rapid quench (single turnover); 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. 0.63 /second Reaction: Pyrophosphorolysis; Substrate: DNA template; Technique: Rapid quench (single turnover); 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. 56 /second Reaction: Nucleotide incorporation; Substrate: dCTP; Technique: Rapid quench (single turnover); 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. 0.7 /second Reaction: Nucleotide incorporation; Substrate: rCTP; Technique: Rapid quench (single turnover); 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. 0.3 /second Reaction: Nucleotide incorporation; Substrate: ddCTP; Technique: Rapid quench (single turnover); 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. 13 /second Reaction: Nucleotide incorporation; Substrate: CTP analog; Technique: Rapid quench (single turnover); 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. 45 /second Reaction: Nucleotide incorporation; Substrate: dCTP; Technique: Rapid quench (burst conditions); Experimental conditions: Mg++ (2mM), pH (pH 8.8), Temp (60°C)
Human Pol lamba Eukaryote X Loop 1 modulates the fidelity of DNA polymerase {lambda} 0.012 /second Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Steady State
Human Pol lamba Eukaryote X Loop 1 modulates the fidelity of DNA polymerase {lambda} 0.00014 /second Reaction: Nucleotide incorporation; Substrate: dGTP; Technique: Steady State
FIV RT Virus/Phage RT Comparison of DNA polymerase activities between recombinant feline immunodeficiency and leukemia virus reverse transcriptases. 0.51 /second Reaction: Nucleotide incorporation; Substrate: dGTP
FIV RT Virus/Phage RT Comparison of DNA polymerase activities between recombinant feline immunodeficiency and leukemia virus reverse transcriptases. 0.21 /second Reaction: Nucleotide incorporation; Substrate: dATP
FIV RT Virus/Phage RT Comparison of DNA polymerase activities between recombinant feline immunodeficiency and leukemia virus reverse transcriptases. 0.28 /second Reaction: Nucleotide incorporation; Substrate: dTTP
FIV RT Virus/Phage RT Comparison of DNA polymerase activities between recombinant feline immunodeficiency and leukemia virus reverse transcriptases. 0.22 /second Reaction: Nucleotide incorporation; Substrate: dCTP
FeLV RT Virus/Phage RT Comparison of DNA polymerase activities between recombinant feline immunodeficiency and leukemia virus reverse transcriptases. 0.56 /second Reaction: Nucleotide incorporation; Substrate: dGTP
FeLV RT Virus/Phage RT Comparison of DNA polymerase activities between recombinant feline immunodeficiency and leukemia virus reverse transcriptases. 0.18 /second Reaction: Nucleotide incorporation; Substrate: dATP
FeLV RT Virus/Phage RT Comparison of DNA polymerase activities between recombinant feline immunodeficiency and leukemia virus reverse transcriptases. 0.17 /second Reaction: Nucleotide incorporation; Substrate: dTTP
FeLV RT Virus/Phage RT Comparison of DNA polymerase activities between recombinant feline immunodeficiency and leukemia virus reverse transcriptases. 0.15 /second Reaction: Nucleotide incorporation; Substrate: dCTP
Pfu Archaeon B DNA polymerases from hyperthermophiles. 560 /minute Reaction: Nucleotide incorporation; Substrate: dNTPs
Pfu (exo-) ? ? DNA polymerases from hyperthermophiles. 550 /minute Reaction: Nucleotide incorporation; Substrate: dNTPs
Vent Archaeon B DNA polymerases from hyperthermophiles. 1000 /minute Reaction: Nucleotide incorporation; Substrate: dNTPs
Taq pol I Eubacterium A DNA polymerases from hyperthermophiles. 2800 /minute Reaction: Nucleotide incorporation; Substrate: dNTPs
Bst LF Eubacterium A DNA polymerases from hyperthermophiles. 1.15E+04 /minute Reaction: Nucleotide incorporation; Substrate: dNTPs
Klenow fragment Eubacterium A DNA polymerases from hyperthermophiles. 310 /minute Reaction: Nucleotide incorporation; Substrate: dNTPs
Sce pol gamma Eukaryote A C-terminal extension of the yeast mitochondrial DNA polymerase determines the balance between synthesis and degradation. 69 /second Reaction: Nucleotide incorporation; Substrate: dNTPs; Technique: Gel shift
Sce pol gamma ∆175 Eukaryote A C-terminal extension of the yeast mitochondrial DNA polymerase determines the balance between synthesis and degradation. 74 /second Reaction: Nucleotide incorporation; Substrate: dNTPs; Technique: Gel shift
Sce pol gamma ∆216 Eukaryote A C-terminal extension of the yeast mitochondrial DNA polymerase determines the balance between synthesis and degradation. 65 /second Reaction: Nucleotide incorporation; Substrate: dNTPs; Technique: Gel shift

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