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Polymerase: Klenow fragment

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Polymerase Reference Property Result Context
Klenow fragment 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. Processivity 12bp
Klenow fragment The 3'-5' exonuclease of DNA polymerase I of Escherichia coli: contribution of each amino acid at the active site to the reaction. 3-5' Exonuclease (proofreading) Yes
Klenow fragment 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. KM 2.3uM Reaction: Nucleotide incorporation; Substrate: dNTPs; Technique: Filter binding ; Experimental conditions: Temp (72°C)
Klenow fragment Fidelity of DNA polymerases in DNA amplification. Nucleotide Substitution Rate 0.00013 errors/bp Technique: DGGE
Klenow fragment The 3'-5' exonuclease of DNA polymerase I of Escherichia coli: contribution of each amino acid at the active site to the reaction. Cloned or native Cloned in E. coli
Klenow fragment The 3'-5' exonuclease of DNA polymerase I of Escherichia coli: contribution of each amino acid at the active site to the reaction. Tagged No
Klenow fragment Structural elucidation of the binding and inhibitory properties of lanthanide (III) ions at the 3'-5' exonucleolytic active site of the Klenow fragment. Other Important Residues Eu3+ at exo site
Klenow fragment The 3'-5' exonuclease of DNA polymerase I of Escherichia coli: contribution of each amino acid at the active site to the reaction. Full length or truncated Full length
Klenow fragment Highly efficient incorporation of the fluorescent nucleotide analogs tC and tCO by Klenow fragment. Methods Featured Fluorescence Spectroscopy
Klenow fragment Highly efficient incorporation of the fluorescent nucleotide analogs tC and tCO by Klenow fragment. Incorporation of non-standard nucleotides 95% + Nucleotide analog: Fluorescent dNTPs
Klenow fragment Highly efficient incorporation of the fluorescent nucleotide analogs tC and tCO by Klenow fragment. Vmax 8.4 /minute Reaction: Nucleotide incorporation; Substrate: CTP analog; Technique: Steady State (dtCoTP fluor analogue); Experimental conditions: pH (pH 8.0), Mg++ (10mM), Temp (37°C)
Klenow fragment Highly efficient incorporation of the fluorescent nucleotide analogs tC and tCO by Klenow fragment. Vmax 5.4 /minute Reaction: Nucleotide incorporation; Substrate: CTP analog; Technique: Steady State (dtCTP fluor analogue); Experimental conditions: pH (pH 8.0), Mg++ (10mM), Temp (37°C)
Klenow fragment Highly efficient incorporation of the fluorescent nucleotide analogs tC and tCO by Klenow fragment. Vmax 8.4 /minute Reaction: Nucleotide incorporation; Substrate: dCTP; Technique: Steady State ; Experimental conditions: pH (pH 8.0), Mg++ (10mM), Temp (37°C)
Klenow fragment The 3'-5' exonuclease of DNA polymerase I of Escherichia coli: contribution of each amino acid at the active site to the reaction. Specific Activity 9000 units/mg Technique: Polymerase assay (poly[d(AT)]
Klenow fragment Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase. Nucleotide Substitution Rate 8E-05 errors/bp Technique: Sequencing
Klenow fragment The 3'-5' exonuclease of DNA polymerase I of Escherichia coli: contribution of each amino acid at the active site to the reaction. KM 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 The 3'-5' exonuclease of DNA polymerase I of Escherichia coli: contribution of each amino acid at the active site to the reaction. kcat 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 The 3'-5' exonuclease of DNA polymerase I of Escherichia coli: contribution of each amino acid at the active site to the reaction. kcat 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 Fingers-closing and other rapid conformational changes in DNA polymerase I (Klenow fragment) and their role in nucleotide selectivity. Methods Featured Fluorescence Spectroscopy
Klenow fragment Fingers-closing and other rapid conformational changes in DNA polymerase I (Klenow fragment) and their role in nucleotide selectivity. Cloned or native Cloned in E. coli
Klenow fragment Fingers-closing and other rapid conformational changes in DNA polymerase I (Klenow fragment) and their role in nucleotide selectivity. Tagged Yes
Klenow fragment Fingers-closing and other rapid conformational changes in DNA polymerase I (Klenow fragment) and their role in nucleotide selectivity. Tag Name N-His6
Klenow fragment Fingers-closing and other rapid conformational changes in DNA polymerase I (Klenow fragment) and their role in nucleotide selectivity. Full length or truncated Full length
Klenow fragment Fingers-closing and other rapid conformational changes in DNA polymerase I (Klenow fragment) and their role in nucleotide selectivity. kcat 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)
Klenow fragment Structure of DNA polymerase I Klenow fragment bound to duplex DNA. Residues Involved in Catalysis of 3-5' Exo D355, E357, D424, D501
Klenow fragment Structure of DNA polymerase I Klenow fragment bound to duplex DNA. Amino Acids Contacting Template N579, S582, D827, R835
Klenow fragment Structure of DNA polymerase I Klenow fragment bound to duplex DNA. Other Important Residues L361, Q419, R455, F473, Y497, H660, T609, E611, R631, K635, N675, N678
Klenow fragment Construction of a plasmid that overproduces the large proteolytic fragment (Klenow fragment) of DNA polymerase I of Escherichia coli. Cloned or native Cloned in E. coli
Klenow fragment Cocrystal structure of an editing complex of Klenow fragment with DNA. Residues Involved in Catalysis of 3-5' Exo D355, E357, D424, D501
Klenow fragment Cocrystal structure of an editing complex of Klenow fragment with DNA. Other Important Residues L361, Q419, R455, F473, Y497, H660
Klenow fragment Formation of 2-hydroxydeoxyadenosine triphosphate, an oxidatively damaged nucleotide, and its incorporation by DNA polymerases. Steady-state kinetics of the incorporation. KM 0.24uM Reaction: Nucleotide incorporation; Substrate: dNTPs; Technique: Steady State
Klenow fragment Identification of residues critical for the polymerase activity of the Klenow fragment of DNA polymerase I from Escherichia coli. Molecular Weight 6.8E+04 Dalton
Klenow fragment Identification of residues critical for the polymerase activity of the Klenow fragment of DNA polymerase I from Escherichia coli. 3-5' Exonuclease (proofreading) Yes
Klenow fragment The fidelity of DNA synthesis catalyzed by derivatives of Escherichia coli DNA polymerase I. 3-5' Exonuclease (proofreading) Yes
Klenow fragment The fidelity of DNA synthesis catalyzed by derivatives of Escherichia coli DNA polymerase I. Residues Involved in Catalysis of 3-5' Exo D424, D355, E357, D501
Klenow fragment The fidelity of DNA synthesis catalyzed by derivatives of Escherichia coli DNA polymerase I. Frameshift Error Rate 6E-07 errors/bp Technique: M13mp2 forward mutation assay (1 uM dNTP, error rate is upper limit (≤))
Klenow fragment The fidelity of DNA synthesis catalyzed by derivatives of Escherichia coli DNA polymerase I. Nucleotide Substitution Rate 5.8E-06 errors/bp Technique: M13mp2 forward mutation assay (1 uM dNTP)
Klenow fragment Genetic and crystallographic studies of the 3',5'-exonucleolytic site of DNA polymerase I. Cloned or native Cloned in E. coli
Klenow fragment Genetic and crystallographic studies of the 3',5'-exonucleolytic site of DNA polymerase I. Residues Involved in Catalysis of 3-5' Exo D355, E357, D424, D501
Klenow fragment Genetic and crystallographic studies of the 3',5'-exonucleolytic site of DNA polymerase I. Tagged No
Klenow fragment Genetic and crystallographic studies of the 3',5'-exonucleolytic site of DNA polymerase I. Full length or truncated Full length
Klenow fragment Genetic and crystallographic studies of the 3',5'-exonucleolytic site of DNA polymerase I. Other Important Residues 2 Mn ions show metal A and B positions
Klenow fragment Genetic and crystallographic studies of the 3',5'-exonucleolytic site of DNA polymerase I. Specific Activity 1.07E+04 units/mg Technique: Polymerase assay (poly[d(AT)]
Klenow fragment Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP. Cloned or native Cloned in E. coli
Klenow fragment Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP. Tagged No
Klenow fragment Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP. Full length or truncated Full length
Klenow fragment Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP. Other Important Residues dNMP-Zn interacts with D355, E357, T358, L361, D424, F473, Y497, D501
Klenow fragment Structural basis for the 3'-5' exonuclease activity of Escherichia coli DNA polymerase I: a two metal ion mechanism. Residues Involved in Catalysis of 3-5' Exo D355, E357, D424, D501
Klenow fragment Structural basis for the 3'-5' exonuclease activity of Escherichia coli DNA polymerase I: a two metal ion mechanism. Other Important Residues T358, L361, Q419, R455, F473, Y497, H660
Klenow fragment Crystal structures of the Klenow fragment of DNA polymerase I complexed with deoxynucleoside triphosphate and pyrophosphate. Amino Acids Contacting NTP R682, Q708, H734, R754, K758, F762, Y766, H881
Klenow fragment Selective elimination of the exonuclease activity of the deoxyribonucleic acid polymerase from Escherichia coli B by limited proteolysis. Molecular Weight 7E+04 Dalton Technique: Gel Filtration
Klenow fragment Selective elimination of the exonuclease activity of the deoxyribonucleic acid polymerase from Escherichia coli B by limited proteolysis. Cloned or native Native organism
Klenow fragment Selective elimination of the exonuclease activity of the deoxyribonucleic acid polymerase from Escherichia coli B by limited proteolysis. 5-3' Exonuclease No
Klenow fragment Selective elimination of the exonuclease activity of the deoxyribonucleic acid polymerase from Escherichia coli B by limited proteolysis. Tagged No
Klenow fragment Selective elimination of the exonuclease activity of the deoxyribonucleic acid polymerase from Escherichia coli B by limited proteolysis. Specific Activity 4300 units/mg Technique: Polymerase Assay (calf thymus DNA)
Klenow fragment Selective elimination of the exonuclease activity of the deoxyribonucleic acid polymerase from Escherichia coli B by limited proteolysis. Specific Activity 2 units/mg Technique: Exo activity (arbitrary units) (3H poly d(A-T))
Klenow fragment Isolation, characterization, and kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3'-5' exonuclease activity. KM 3uM Reaction: 3-5' Exonuclease; Substrate: DNA template
Klenow fragment Isolation, characterization, and kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3'-5' exonuclease activity. KM 160uM Reaction: 3-5' Exonuclease; Substrate: DNA template
Klenow fragment Isolation, characterization, and kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3'-5' exonuclease activity. kcat 5.8 /second Reaction: 3-5' Exonuclease; Substrate: DNA template
Klenow fragment Isolation, characterization, and kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3'-5' exonuclease activity. kcat 7.8 /second Reaction: 3-5' Exonuclease; Substrate: DNA template
Klenow fragment Formation of 2-hydroxydeoxyadenosine triphosphate, an oxidatively damaged nucleotide, and its incorporation by DNA polymerases. Steady-state kinetics of the incorporation. KM 1.8uM Reaction: Nucleotide incorporation; Substrate: ATP analog; Technique: Steady State
Klenow fragment Formation of 2-hydroxydeoxyadenosine triphosphate, an oxidatively damaged nucleotide, and its incorporation by DNA polymerases. Steady-state kinetics of the incorporation. Vmax 14 /minute Reaction: Nucleotide incorporation; Substrate: dNTPs; Technique: Steady State
Klenow fragment Formation of 2-hydroxydeoxyadenosine triphosphate, an oxidatively damaged nucleotide, and its incorporation by DNA polymerases. Steady-state kinetics of the incorporation. Vmax 23 /minute Reaction: Nucleotide incorporation; Substrate: ATP analog; Technique: Steady State
Klenow fragment Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. kcat 0.02 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ( Substrate: 3'-tailed duplex phosphorothioate substrate)
Klenow fragment Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. kcat 0.0017 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 6.5)
Klenow fragment Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. kcat 0.0054 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 7)
Klenow fragment Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. kcat 0.016 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 7.5)
Klenow fragment Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. kcat 0.052 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 8)
Klenow fragment Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. kcat 0.16 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 8.5)
Klenow fragment Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity. kcat 0.33 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover (Substrate: 3'-tailed duplex all-oxygen substrate)
Klenow fragment Enzymatic synthesis of deoxyribonucleic acid. 36. A proofreading function for the 3' leads to 5' exonuclease activity in deoxyribonucleic acid polymerases. Vmax 19 /minute Reaction: 3-5' Exonuclease; Substrate: DNA template; Experimental conditions: Temp (37°C)
Klenow fragment Enzymatic synthesis of deoxyribonucleic acid. 36. A proofreading function for the 3' leads to 5' exonuclease activity in deoxyribonucleic acid polymerases. Vmax 4.8 /minute Reaction: 3-5' Exonuclease; Substrate: DNA template; Experimental conditions: Temp (37°C)
Klenow fragment Expression, purification, and initial kinetic characterization of the large subunit of the human mitochondrial DNA polymerase. Processivity 250bp
Klenow fragment Expression, purification, and initial kinetic characterization of the large subunit of the human mitochondrial DNA polymerase. Vmax 50 /second Reaction: Nucleotide incorporation; Substrate: dNTPs
Klenow fragment Expression, purification, and initial kinetic characterization of the large subunit of the human mitochondrial DNA polymerase. Kd 5nM Reaction: Polymerase-DNA interaction; Substrate: DNA template
Klenow fragment Expression, purification, and initial kinetic characterization of the large subunit of the human mitochondrial DNA polymerase. Kd 17uM Reaction: Nucleotide incorporation; Substrate: dNTPs
Klenow fragment Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. Polymerase Catalytic Residue Amino Acids Asp705, Asp882, and Glu883
Klenow fragment Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. 3-5' Exonuclease (proofreading) Yes
Klenow fragment Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. Residues Involved in Catalysis of 3-5' Exo Asp355, Glu357, Asp424, and Asp501
Klenow fragment Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. Processivity 70bp
Klenow fragment Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. Specific Activity 5500 units/mg Technique: Polymerase Assay (M13 DNA)
Klenow fragment Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. Specific Activity 9700 units/mg Technique: Polymerase Assay (calf thymus DNA)
Klenow fragment Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. KM 2.3uM Reaction: Nucleotide incorporation; Substrate: dNTPs
Klenow fragment Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. KM 1.8nM Reaction: Polymerase-DNA interaction; Substrate: DNA template
Klenow fragment Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. kcat 5.2 /second Reaction: Nucleotide incorporation; Substrate: dNTPs
Klenow fragment The thioredoxin binding domain of bacteriophage T7 DNA polymerase confers processivity on Escherichia coli DNA polymerase I. Processivity 20bp
Klenow fragment The thioredoxin binding domain of bacteriophage T7 DNA polymerase confers processivity on Escherichia coli DNA polymerase I. Specific Activity 2200 Other Technique: Polymerase Assay (M13 DNA)
Klenow fragment A thumb subdomain mutant of the large fragment of Escherichia coli DNA polymerase I with reduced DNA binding affinity, processivity, and frameshift fidelity. Molecular Weight 6.8E+04 Dalton
Klenow fragment A thumb subdomain mutant of the large fragment of Escherichia coli DNA polymerase I with reduced DNA binding affinity, processivity, and frameshift fidelity. Cloned or native Native organism
Klenow fragment A thumb subdomain mutant of the large fragment of Escherichia coli DNA polymerase I with reduced DNA binding affinity, processivity, and frameshift fidelity. Tagged No
Klenow fragment A thumb subdomain mutant of the large fragment of Escherichia coli DNA polymerase I with reduced DNA binding affinity, processivity, and frameshift fidelity. Frameshift Error Rate 0.0102 errors/bp Technique: Reversion
Klenow fragment A thumb subdomain mutant of the large fragment of Escherichia coli DNA polymerase I with reduced DNA binding affinity, processivity, and frameshift fidelity. Overall Error Rate 4E-05 errors/bp
Klenow fragment A thumb subdomain mutant of the large fragment of Escherichia coli DNA polymerase I with reduced DNA binding affinity, processivity, and frameshift fidelity. Nucleotide Substitution Rate 0.00036 errors/bp Technique: Reversion
Klenow fragment A thumb subdomain mutant of the large fragment of Escherichia coli DNA polymerase I with reduced DNA binding affinity, processivity, and frameshift fidelity. Nucleotide Substitution Rate 0.0028 errors/bp Technique: Forward mutational
Klenow fragment A thumb subdomain mutant of the large fragment of Escherichia coli DNA polymerase I with reduced DNA binding affinity, processivity, and frameshift fidelity. Full length or truncated Full length
Klenow fragment A thumb subdomain mutant of the large fragment of Escherichia coli DNA polymerase I with reduced DNA binding affinity, processivity, and frameshift fidelity. KM 3.7uM Reaction: Nucleotide incorporation; Substrate: dTTP
Klenow fragment A thumb subdomain mutant of the large fragment of Escherichia coli DNA polymerase I with reduced DNA binding affinity, processivity, and frameshift fidelity. Kd 42nM Reaction: Polymerase-DNA interaction; Substrate: DNA template
Klenow fragment A thumb subdomain mutant of the large fragment of Escherichia coli DNA polymerase I with reduced DNA binding affinity, processivity, and frameshift fidelity. kcat 0.3 /second Reaction: Nucleotide incorporation; Substrate: dTTP
Klenow fragment Kinetics of DNA polymerase I (Klenow fragment exo-) activity on damaged DNA templates: effect of proximal and distal template damage on DNA synthesis. Template lesions Bypasses Reaction: Nucleotide incorporation; DNA lesion: 8-oxo-dG
Klenow fragment Identification of a new motif required for the 3'-5' exonuclease activity of Escherichia coli DNA polymerase I (Klenow fragment): the RRRY motif is necessary for the binding of single-stranded DNA substrate and the template strand of the mismatched duplex. 3-5' Exonuclease (proofreading) Yes
Klenow fragment Identification of a new motif required for the 3'-5' exonuclease activity of Escherichia coli DNA polymerase I (Klenow fragment): the RRRY motif is necessary for the binding of single-stranded DNA substrate and the template strand of the mismatched duplex. 5-3' Exonuclease Unspecified
Klenow fragment Synthesis of novel poly(dG)-poly(dG)-poly(dC) triplex structure by Klenow exo- fragment of DNA polymerase I. 3-5' Exonuclease (proofreading) Yes
Klenow fragment Synthesis of novel poly(dG)-poly(dG)-poly(dC) triplex structure by Klenow exo- fragment of DNA polymerase I. 5-3' Exonuclease Unspecified
Klenow fragment Contribution of polar residues of the J-helix in the 3'-5' exonuclease activity of Escherichia coli DNA polymerase I (Klenow fragment): Q677 regulates the removal of terminal mismatch. 3-5' Exonuclease (proofreading) Yes
Klenow fragment Contribution of polar residues of the J-helix in the 3'-5' exonuclease activity of Escherichia coli DNA polymerase I (Klenow fragment): Q677 regulates the removal of terminal mismatch. 5-3' Exonuclease Unspecified
Klenow fragment In vitro synthesis of uniform poly(dG)-poly(dC) by Klenow exo- fragment of polymerase I. 3-5' Exonuclease (proofreading) Yes
Klenow fragment In vitro synthesis of uniform poly(dG)-poly(dC) by Klenow exo- fragment of polymerase I. 5-3' Exonuclease No
Klenow fragment The proofreading 3'-->5' exonuclease activity of DNA polymerases: a kinetic barrier to translesion DNA synthesis. 3-5' Exonuclease (proofreading) Yes
Klenow fragment The proofreading 3'-->5' exonuclease activity of DNA polymerases: a kinetic barrier to translesion DNA synthesis. 5-3' Exonuclease No
Klenow fragment Miscoding potential of the N2-ethyl-2'-deoxyguanosine DNA adduct by the exonuclease-free Klenow fragment of Escherichia coli DNA polymerase I. 3-5' Exonuclease (proofreading) Yes
Klenow fragment Miscoding potential of the N2-ethyl-2'-deoxyguanosine DNA adduct by the exonuclease-free Klenow fragment of Escherichia coli DNA polymerase I. 5-3' Exonuclease No
Klenow fragment 3'-5' exonuclease of Klenow fragment: role of amino acid residues within the single-stranded DNA binding region in exonucleolysis and duplex DNA melting. 3-5' Exonuclease (proofreading) Yes
Klenow fragment 3'-5' exonuclease of Klenow fragment: role of amino acid residues within the single-stranded DNA binding region in exonucleolysis and duplex DNA melting. 5-3' Exonuclease No
Klenow fragment The mutational specificity of the Dbh lesion bypass polymerase and its implications. Overall Error Rate 0.00038 errors/bp
Klenow fragment Fidelity of DNA synthesis by the Thermus aquaticus DNA polymerase. 3-5' Exonuclease (proofreading) Yes
Klenow fragment Fidelity of DNA synthesis by the Thermus aquaticus DNA polymerase. Overall Error Rate 0.0044 errors/bp
Klenow fragment Fidelity of DNA synthesis by the Thermus aquaticus DNA polymerase. Nucleotide Substitution Rate 4E-05 errors/bp
Klenow fragment Fidelity of DNA synthesis by the Thermus aquaticus DNA polymerase. Full length or truncated Full length
Klenow fragment Polymerase-specific differences in the DNA intermediates of frameshift mutagenesis. In vitro synthesis errors of Escherichia coli DNA polymerase I and its large fragment derivative. Overall Error Rate 5.8E-05 errors/bp
Klenow fragment Fidelity of the reverse transcriptase of human immunodeficiency virus type 2. Reverse Transcriptase Activity No
Klenow fragment Fidelity of the reverse transcriptase of human immunodeficiency virus type 2. 3-5' Exonuclease (proofreading) Yes
Klenow fragment DNA polymerases from hyperthermophiles. Reverse Transcriptase Activity Yes
Klenow fragment DNA polymerases from hyperthermophiles. 3-5' Exonuclease (proofreading) Yes
Klenow fragment DNA polymerases from hyperthermophiles. 3-5' Exo Specific Activity 28 units/mg
Klenow fragment DNA polymerases from hyperthermophiles. 5-3' Exonuclease No
Klenow fragment DNA polymerases from hyperthermophiles. Processivity 7bp
Klenow fragment DNA polymerases from hyperthermophiles. Specific Activity 0.9 units/mg Technique: Polymerase Assay (calf thymus DNA)
Klenow fragment DNA polymerases from hyperthermophiles. Specific Activity 0.6 units/mg Technique: Polymerase Assay (M13 DNA)
Klenow fragment DNA polymerases from hyperthermophiles. KM 2.3uM Reaction: Nucleotide incorporation; Substrate: dNTPs
Klenow fragment DNA polymerases from hyperthermophiles. KM 1.8nM Reaction: Polymerase-DNA interaction; Substrate: DNA template
Klenow fragment DNA polymerases from hyperthermophiles. Strand Displacement Yes
Klenow fragment DNA polymerases from hyperthermophiles. kcat 310 /minute Reaction: Nucleotide incorporation; Substrate: dNTPs
Klenow fragment Analyzing fidelity of DNA polymerases. Frameshift Error Rate 8E-05 errors/bp Technique: Reversion
Klenow fragment Analyzing fidelity of DNA polymerases. Overall Error Rate 0.0052 errors/bp Technique: M13mp2 forward mutation assay
Klenow fragment Analyzing fidelity of DNA polymerases. Overall Error Rate 7.7E-05 errors/bp Technique: M13mp2 opal codon reversion assay
Klenow fragment Deoxyribonucleic acid polymerase: two distinct enzymes in one polypeptide. II. A proteolytic fragment containing the 5' leads to 3' exonuclease function. Restoration of intact enzyme functions from the two proteolytic fragments. Molecular Weight 7.6E+04 Dalton
Klenow fragment Deoxyribonucleic acid polymerase: two distinct enzymes in one polypeptide. II. A proteolytic fragment containing the 5' leads to 3' exonuclease function. Restoration of intact enzyme functions from the two proteolytic fragments. 3-5' Exonuclease (proofreading) Yes
Klenow fragment Deoxyribonucleic acid polymerase: two distinct enzymes in one polypeptide. II. A proteolytic fragment containing the 5' leads to 3' exonuclease function. Restoration of intact enzyme functions from the two proteolytic fragments. 5-3' Exonuclease No
Klenow fragment Deoxyribonucleic acid polymerase: two distinct enzymes in one polypeptide. I. A proteolytic fragment containing the polymerase and 3' leads to 5' exonuclease functions. Molecular Weight 7.6E+04 Dalton Technique: SDS-acrylamide gel electrophoresis
Klenow fragment Deoxyribonucleic acid polymerase: two distinct enzymes in one polypeptide. I. A proteolytic fragment containing the polymerase and 3' leads to 5' exonuclease functions. 3-5' Exonuclease (proofreading) Yes
Klenow fragment Deoxyribonucleic acid polymerase: two distinct enzymes in one polypeptide. I. A proteolytic fragment containing the polymerase and 3' leads to 5' exonuclease functions. 5-3' Exonuclease No
Klenow fragment Deoxyribonucleic acid polymerase: two distinct enzymes in one polypeptide. I. A proteolytic fragment containing the polymerase and 3' leads to 5' exonuclease functions. Specific Activity 1.534E+04 units/mg Technique: Polymerase Assay (calf thymus DNA)
Klenow fragment Deoxyribonucleic acid polymerase: two distinct enzymes in one polypeptide. I. A proteolytic fragment containing the polymerase and 3' leads to 5' exonuclease functions. Extinction Coefficient 0.93 at 278nm

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