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Polymerase: Eco Pol I

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Polymerase Reference Property Result Context
Eco Pol I On the processive mechanism of Escherichia coli DNA polymerase I. Quantitative assessment of processivity. Cloned or native Cloned in E. coli
Eco Pol I 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. Full length or truncated Full length
Eco Pol I 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 97bp
Eco Pol I 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 2uM Reaction: Nucleotide incorporation; Substrate: dNTPs; Technique: Filter binding ; Experimental conditions: Temp (72°C)
Eco Pol I On the processive mechanism of Escherichia coli DNA polymerase I. Quantitative assessment of processivity. Tagged No
Eco Pol I On the processive mechanism of Escherichia coli DNA polymerase I. Quantitative assessment of processivity. Full length or truncated Full length
Eco Pol I On the processive mechanism of Escherichia coli DNA polymerase I. Quantitative assessment of processivity. Processivity 188bp
Eco Pol I On the fidelity of DNA replication. The accuracy of T4 DNA polymerases in copying phi X174 DNA in vitro. Nucleotide Substitution Rate 9.01E-06 errors/bp Technique: Reversion (1 mM dNTP)
Eco Pol I On the fidelity of DNA replication. The accuracy of T4 DNA polymerases in copying phi X174 DNA in vitro. Processivity 3040bp
Eco Pol I On the processive mechanism of Escherichia coli DNA polymerase I. Quantitative assessment of processivity. Nick Extension Yes, unspecified mechanism
Eco Pol I On the processive mechanism of Escherichia coli DNA polymerase I. Quantitative assessment of processivity. Gap Filling Yes
Eco Pol I Second-strand cDNA synthesis with E. coli DNA polymerase I and RNase H: the fate of information at the mRNA 5' terminus and the effect of E. coli DNA ligase. RNase H Yes
Eco Pol I The steady state kinetic parameters and non-processivity of Escherichia coli deoxyribonucleic acid polymerase I. 3-5' Exonuclease (proofreading) Yes
Eco Pol I The steady state kinetic parameters and non-processivity of Escherichia coli deoxyribonucleic acid polymerase I. 5-3' Exonuclease Yes
Eco Pol I The steady state kinetic parameters and non-processivity of Escherichia coli deoxyribonucleic acid polymerase I. Full length or truncated Full length
Eco Pol I The steady state kinetic parameters and non-processivity of Escherichia coli deoxyribonucleic acid polymerase I. Specific Activity 1.5E+04 units/mg
Eco Pol I The steady state kinetic parameters and non-processivity of Escherichia coli deoxyribonucleic acid polymerase I. KM 1uM Reaction: Nucleotide incorporation; Substrate: dATP
Eco Pol I The steady state kinetic parameters and non-processivity of Escherichia coli deoxyribonucleic acid polymerase I. KM 2uM Reaction: Nucleotide incorporation; Substrate: dTTP
Eco Pol I Incorporation of reporter-labeled nucleotides by DNA polymerases. 3-5' Exonuclease (proofreading) No
Eco Pol I Incorporation of reporter-labeled nucleotides by DNA polymerases. Cloned or native Unspecified
Eco Pol I Incorporation of reporter-labeled nucleotides by DNA polymerases. 5-3' Exonuclease Unspecified
Eco Pol I Incorporation of reporter-labeled nucleotides by DNA polymerases. Tagged Unspecified
Eco Pol I Incorporation of reporter-labeled nucleotides by DNA polymerases. Full length or truncated Unspecified
Eco Pol I Incorporation of reporter-labeled nucleotides by DNA polymerases. Application name PCR
Eco Pol I Characterization of DNA polymerase I*, a form of DNA polymerase I found in Escherichia coli expressing SOS functions. 3-5' Exonuclease (proofreading) Yes
Eco Pol I Characterization of DNA polymerase I*, a form of DNA polymerase I found in Escherichia coli expressing SOS functions. Cloned or native Native organism
Eco Pol I Characterization of DNA polymerase I*, a form of DNA polymerase I found in Escherichia coli expressing SOS functions. 5-3' Exonuclease Yes
Eco Pol I Characterization of DNA polymerase I*, a form of DNA polymerase I found in Escherichia coli expressing SOS functions. Full length or truncated Full length
Eco Pol I Characterization of DNA polymerase I*, a form of DNA polymerase I found in Escherichia coli expressing SOS functions. Processivity 6bp
Eco Pol I Characterization of DNA polymerase I*, a form of DNA polymerase I found in Escherichia coli expressing SOS functions. Specific Activity 25 units/mg
Eco Pol I Kinetic analysis of Escherichia coli deoxyribonucleic acid polymerase I. Vmax 3.4 /second Reaction: Nucleotide incorporation; Substrate: dGTP
Eco Pol I Kinetic analysis of Escherichia coli deoxyribonucleic acid polymerase I. Vmax 3.8 /second Reaction: Nucleotide incorporation; Substrate: dTTP
Eco Pol I Kinetic analysis of Escherichia coli deoxyribonucleic acid polymerase I. Vmax 1.32 /second Reaction: Nucleotide incorporation; Substrate: dTTP
Eco Pol I Kinetic analysis of Escherichia coli deoxyribonucleic acid polymerase I. Vmax 2.5 /second Reaction: Nucleotide incorporation; Substrate: dATP
Eco Pol I Kinetic analysis of Escherichia coli deoxyribonucleic acid polymerase I. Vmax 0.11 /second Reaction: Nucleotide incorporation; Substrate: dCTP
Eco Pol I Escherichia coli thioredoxin confers processivity on the DNA polymerase activity of the gene 5 protein of bacteriophage T7. Full length or truncated Full length
Eco Pol I Escherichia coli thioredoxin confers processivity on the DNA polymerase activity of the gene 5 protein of bacteriophage T7. Specific Activity 9800 units/mg Technique: Polymerase Assay (calf thymus DNA)
Eco Pol I Escherichia coli thioredoxin confers processivity on the DNA polymerase activity of the gene 5 protein of bacteriophage T7. Specific Activity 2.8E+04 units/mg Technique: Polymerase Assay (M13 DNA)
Eco Pol I Short deoxyribonucleic acid repair patch length in Escherichia coli is determined by the processive mechanism of deoxyribonucleic acid polymerase I. Cloned or native Native organism
Eco Pol I Short deoxyribonucleic acid repair patch length in Escherichia coli is determined by the processive mechanism of deoxyribonucleic acid polymerase I. 5-3' Exonuclease Yes
Eco Pol I Short deoxyribonucleic acid repair patch length in Escherichia coli is determined by the processive mechanism of deoxyribonucleic acid polymerase I. Tagged No
Eco Pol I Short deoxyribonucleic acid repair patch length in Escherichia coli is determined by the processive mechanism of deoxyribonucleic acid polymerase I. Full length or truncated Full length
Eco Pol I Short deoxyribonucleic acid repair patch length in Escherichia coli is determined by the processive mechanism of deoxyribonucleic acid polymerase I. Processivity 20bp
Eco Pol I Short deoxyribonucleic acid repair patch length in Escherichia coli is determined by the processive mechanism of deoxyribonucleic acid polymerase I. KM 2uM Reaction: Nucleotide incorporation; Substrate: dNTPs
Eco Pol I Short deoxyribonucleic acid repair patch length in Escherichia coli is determined by the processive mechanism of deoxyribonucleic acid polymerase I. Nick Extension Yes, via strand displacement
Eco Pol I Processive DNA synthesis by DNA polymerase II mediated by DNA polymerase III accessory proteins. Molecular Weight 1.03E+05 Dalton
Eco Pol I Processive DNA synthesis by DNA polymerase II mediated by DNA polymerase III accessory proteins. 3-5' Exonuclease (proofreading) Yes
Eco Pol I Processive DNA synthesis by DNA polymerase II mediated by DNA polymerase III accessory proteins. Cloned or native Native organism
Eco Pol I Processive DNA synthesis by DNA polymerase II mediated by DNA polymerase III accessory proteins. 5-3' Exonuclease Yes
Eco Pol I Processive DNA synthesis by DNA polymerase II mediated by DNA polymerase III accessory proteins. Template lesions Bypasses Reaction: Nucleotide incorporation; DNA lesion: Apurinic/Apyrimidinic (AP) site
Eco Pol I Processive DNA synthesis by DNA polymerase II mediated by DNA polymerase III accessory proteins. Full length or truncated Full length
Eco Pol I Thermostable DNA polymerases. Molecular Weight 1.03E+05 Dalton
Eco Pol I Thermostable DNA polymerases. 3-5' Exonuclease (proofreading) Yes
Eco Pol I Thermostable DNA polymerases. 5-3' Exonuclease Yes
Eco Pol I Thermostable DNA polymerases. Full length or truncated Full length
Eco Pol I 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 7.1E-05 errors/bp Technique: Blue/white screening
Eco Pol I Highly mutagenic replication by DNA polymerase V (UmuC) provides a mechanistic basis for SOS untargeted mutagenesis. Overall Error Rate 0.00138 errors/bp
Eco Pol I Highly mutagenic replication by DNA polymerase V (UmuC) provides a mechanistic basis for SOS untargeted mutagenesis. Overall Error Rate 0.00078 errors/bp
Eco Pol I Pre-steady-state kinetic studies of the fidelity of Sulfolobus solfataricus P2 DNA polymerase IV. Overall Error Rate 0.00017 errors/bp
Eco Pol I Pre-steady-state kinetic studies of the fidelity of Sulfolobus solfataricus P2 DNA polymerase IV. Overall Error Rate 0.00053 errors/bp
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXVI. Physical and chemical studies of a homogeneous deoxyribonucleic acid polymerase. Molecular Weight 1.09E+05 Dalton Technique: Sedimentation Equilibrium
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXVI. Physical and chemical studies of a homogeneous deoxyribonucleic acid polymerase. Tagged No
Eco Pol I Enzymic synthesis of deoxyribonucleic acid. Optimal pH pH 8.7
Eco Pol I Enzymic synthesis of deoxyribonucleic acid. Percent/Fold Effect 97 % decrease Reaction: Nucleotide incorporation; Substrate: dNTPs; Experimental conditions: NaCl (0.2 mg/mL)
Eco Pol I Enzymic synthesis of deoxyribonucleic acid. Percent/Fold Effect 30 % increase Reaction: Nucleotide incorporation; Substrate: dNTPs; Experimental conditions: pH (pH 8.7)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XII. A polymer of deoxyguanylate and deoxycytidylate. Optimal pH pH 7.5
Eco Pol I ENZYMATIC SYNTHESIS OF DEOXYRIBONUCLEIC ACID, XVI. OLIGONUCLEOTIDES AS TEMPLATES AND THE MECHANISM OF THEIR REPLICATION. Other Important Residues deoxyadenylate and deoxythymidylate [(AT)3 to (AT)7]
Eco Pol I ENZYMATIC SYNTHESIS OF DEOXYRIBONUCLEIC ACID, XVI. OLIGONUCLEOTIDES AS TEMPLATES AND THE MECHANISM OF THEIR REPLICATION. Percent/Fold Effect 50 % decrease Reaction: Nucleotide incorporation; Substrate: dNTPs; Experimental conditions: Temp (20°C)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. II. General properties of the reaction. Percent/Fold Effect 38.5 % decrease Reaction: Pyrophosphorolysis; Substrate: DNA template; Experimental conditions: CTP (.005µM), GTP (.005µM), ATP (0µM), TTP (0µM)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. II. General properties of the reaction. Percent/Fold Effect 99.9 % decrease Reaction: Nucleotide incorporation; Substrate: dNTPs; Experimental conditions: CTP (.005µM), GTP (0µM), ATP (0µM), TTP (0µM)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. II. General properties of the reaction. Percent/Fold Effect 95 % decrease Reaction: Nucleotide incorporation; Substrate: dNTPs; Experimental conditions: Mg++ (0mM)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. II. General properties of the reaction. Percent/Fold Effect 94.5 % decrease Reaction: Pyrophosphorolysis; Substrate: DNA template; Experimental conditions: CTP (0µM), GTP (0µM), ATP (0µM), TTP (0µM)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. II. General properties of the reaction. Percent/Fold Effect 0 % decrease Reaction: Nucleotide incorporation; Substrate: dNTPs; Experimental conditions: PP (.016mM)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. II. General properties of the reaction. Percent/Fold Effect 94 % decrease Reaction: Pyrophosphorolysis; Substrate: DNA template; Experimental conditions: NTPs (0mM)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. II. General properties of the reaction. Percent/Fold Effect 99.5 % decrease Reaction: Nucleotide incorporation; Substrate: dNTPs; Experimental conditions: CTP (.005µM), GTP (.005µM), ATP (0µM), TTP (.005µM)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. II. General properties of the reaction. Percent/Fold Effect 67.5 % decrease Reaction: Pyrophosphorolysis; Substrate: DNA template; Experimental conditions: CTP (.005µM), GTP (0µM), ATP (0µM), TTP (0µM)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. II. General properties of the reaction. Percent/Fold Effect 99.8 % decrease Reaction: Nucleotide incorporation; Substrate: dNTPs; Experimental conditions: CTP (.005µM), GTP (.005µM), ATP (0µM), TTP (0µM)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. II. General properties of the reaction. Percent/Fold Effect 50 % decrease Reaction: Nucleotide incorporation; Substrate: dNTPs; Experimental conditions: PP (3mM)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. II. General properties of the reaction. Percent/Fold Effect 33 % decrease Reaction: Pyrophosphorolysis; Substrate: DNA template; Experimental conditions: CTP (.005µM), GTP (.005µM), ATP (0µM), TTP (.005µM)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. I. Preparation of substrates and partial purification of an enzyme from Escherichia coli. Optimal pH pH 8.7
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. I. Preparation of substrates and partial purification of an enzyme from Escherichia coli. Percent/Fold Effect 97 % decrease Reaction: Nucleotide incorporation; Substrate: dNTPs; Experimental conditions: NaCl (200mM)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. I. Preparation of substrates and partial purification of an enzyme from Escherichia coli. Percent/Fold Effect 90 % decrease Reaction: Nucleotide incorporation; Substrate: dNTPs; Experimental conditions: KF (50mM)
Eco Pol I ENZYMATIC SYNTHESIS OF DEOXYRIBONUCLEIC ACID. XIV. FURTHER PURIFICATION AND PROPERTIES OF DEOXYRIBONUCLEIC ACID POLYMERASE OF ESCHERICHIA COLI. 3-5' Exonuclease (proofreading) Unspecified
Eco Pol I ENZYMATIC SYNTHESIS OF DEOXYRIBONUCLEIC ACID. XIV. FURTHER PURIFICATION AND PROPERTIES OF DEOXYRIBONUCLEIC ACID POLYMERASE OF ESCHERICHIA COLI. 5-3' Exonuclease Unspecified
Eco Pol I ENZYMATIC SYNTHESIS OF DEOXYRIBONUCLEIC ACID. XIV. FURTHER PURIFICATION AND PROPERTIES OF DEOXYRIBONUCLEIC ACID POLYMERASE OF ESCHERICHIA COLI. Optimal pH pH 7.4
Eco Pol I ENZYMATIC SYNTHESIS OF DEOXYRIBONUCLEIC ACID. XIV. FURTHER PURIFICATION AND PROPERTIES OF DEOXYRIBONUCLEIC ACID POLYMERASE OF ESCHERICHIA COLI. Specific Activity 1.88E+04 units/mg Technique: Polymerase Assay (calf thymus DNA)
Eco Pol I ENZYMATIC SYNTHESIS OF DEOXYRIBONUCLEIC ACID. XIV. FURTHER PURIFICATION AND PROPERTIES OF DEOXYRIBONUCLEIC ACID POLYMERASE OF ESCHERICHIA COLI. Percent/Fold Effect 30 % decrease Reaction: Nucleotide incorporation; Substrate: dNTPs; Experimental conditions: pH (pH 7)
Eco Pol I ENZYMATIC SYNTHESIS OF DEOXYRIBONUCLEIC ACID. XIV. FURTHER PURIFICATION AND PROPERTIES OF DEOXYRIBONUCLEIC ACID POLYMERASE OF ESCHERICHIA COLI. Percent/Fold Effect 30 % decrease Reaction: Nucleotide incorporation; Substrate: dNTPs; Experimental conditions: pH (pH 7.8)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXVII. Chemical modifications of deoxyribonucleic acid polymerase. 3-5' Exonuclease (proofreading) Unspecified
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXVII. Chemical modifications of deoxyribonucleic acid polymerase. Cloned or native Cloned in E. coli
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXVII. Chemical modifications of deoxyribonucleic acid polymerase. 5-3' Exonuclease Yes
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXVII. Chemical modifications of deoxyribonucleic acid polymerase. Tagged Yes
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXVII. Chemical modifications of deoxyribonucleic acid polymerase. Tag Name Hg(II)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXVII. Chemical modifications of deoxyribonucleic acid polymerase. Percent/Fold Effect 920 % increase Reaction: 5-3' Exonuclease; Substrate: DNA template; Experimental conditions: Hg(II) (1000mM), pH (pH 7.4)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXVII. Chemical modifications of deoxyribonucleic acid polymerase. Percent/Fold Effect 98 % decrease Reaction: Pyrophosphorolysis; Substrate: DNA template; Experimental conditions: Hg(II) (1000mM), pH (pH 7.4)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXVII. Chemical modifications of deoxyribonucleic acid polymerase. Percent/Fold Effect 99.9 % decrease Reaction: Nucleotide incorporation; Substrate: dNTPs; Experimental conditions: Hg(II) (1000mM), pH (pH 7.4)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXVII. Chemical modifications of deoxyribonucleic acid polymerase. Percent/Fold Effect 80 % decrease Reaction: 5-3' Exonuclease; Substrate: DNA template; Experimental conditions: Hg(II) (1000mM), pH (pH 8.76), Temp (37°C)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXVII. Chemical modifications of deoxyribonucleic acid polymerase. Percent/Fold Effect 42 % decrease Reaction: 5-3' Exonuclease; Substrate: DNA template; Experimental conditions: Hg(II) (1000mM), Temp (37°C), pH (pH 6.5)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXXI. Binding of deoxyribonucleic acid to deoxyribonucleic acid polymerase. 5-3' Exonuclease Unspecified
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXXI. Binding of deoxyribonucleic acid to deoxyribonucleic acid polymerase. Specific Activity 1.8E+04 units/mg
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXXII. Replication of duplex deoxyribonucleic acid by polymerase at a single strand break. 3-5' Exonuclease (proofreading) Yes
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXXII. Replication of duplex deoxyribonucleic acid by polymerase at a single strand break. 5-3' Exonuclease Yes
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXXII. Replication of duplex deoxyribonucleic acid by polymerase at a single strand break. Optimal pH pH 7.4
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXXII. Replication of duplex deoxyribonucleic acid by polymerase at a single strand break. Specific Activity 1.8E+04 units/mg
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXXII. Replication of duplex deoxyribonucleic acid by polymerase at a single strand break. Nick Extension Yes, via exo activity
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXXII. Replication of duplex deoxyribonucleic acid by polymerase at a single strand break. Strand Displacement Yes
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 3-5' Exonuclease (proofreading) Yes
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. 5-3' Exonuclease Yes
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Extinction Coefficient 9.26x10^4 M^-1 cm^-1 at 280nm
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Kd 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 Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Kd 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 Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Kd 2600uM Reaction: Polymerase - NTP interaction; Substrate: Deoxycytidine 3’-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Kd 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 Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Kd 167uM Reaction: Polymerase - NTP interaction; Substrate: Purine deoxyribonucleoside 5’-phosphate ; Technique: Equilibrium Dialysis ; Experimental conditions: pH (pH 7.4), PP (50mM)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Kd 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 Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Kd 2800uM Reaction: Polymerase - NTP interaction; Substrate: Thymidine 5’-phosphonate ; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Kd 2600uM Reaction: Polymerase - NTP interaction; Substrate: 2’-deoxyadenosine; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Kd 3000uM Reaction: Polymerase - NTP interaction; Substrate: 3'-O-methyl AMP; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Kd 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 Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Kd 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 Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Kd 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 Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Kd 1200uM Reaction: Polymerase - NTP interaction; Substrate: Deoxyadenosine 3’-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Kd 3900uM Reaction: Polymerase - NTP interaction; Substrate: Adenine-2’-deoxylyxonucleoside 5’-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Kd 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 Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Kd 3900uM Reaction: Polymerase - NTP interaction; Substrate: Adenine xylonucleoside 5’-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Kd 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 Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Kd 62uM Reaction: Polymerase - NTP interaction; Substrate: Aristeromycin 6'-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: pH (pH 7.4), PP (50mM)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Kd 3000uM Reaction: Polymerase - NTP interaction; Substrate: Deoxythymidine 3’-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Kd 2300uM Reaction: Polymerase - NTP interaction; Substrate: Adenine arabinonucleoside 5’-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Kd 3000uM Reaction: Polymerase - NTP interaction; Substrate: Adenosine 5’-phosphite; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Kd 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 Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Kd 2600uM Reaction: Polymerase - NTP interaction; Substrate: Thymine arabinonucleoside 5’-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Kd 3700uM Reaction: Polymerase - NTP interaction; Substrate: Uracil arabinonucleoside 5’-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Kd 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 Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Kd 35uM Reaction: Polymerase - NTP interaction; Substrate: AMP; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Kd 3000uM Reaction: Polymerase - NTP interaction; Substrate: Uracil lyxonucleoside 5’-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Kd 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 Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Kd 3400uM Reaction: Polymerase - NTP interaction; Substrate: Thymidine 3’,5’-diphosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Kd 1000uM Reaction: Polymerase - NTP interaction; Substrate: Deoxy-guanosine 3’-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Kd 2300uM Reaction: Polymerase - NTP interaction; Substrate: Uracil xylonucleoside 5’-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Kd 900uM Reaction: Polymerase - NTP interaction; Substrate: Nicotinamide ribonucleoside 5’-phosphate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. XXXV. A 3'-hydroxylribonucleotide binding site of Escherichia coli deoxyribonucleic acid polymerase. Kd 2800uM Reaction: Polymerase - NTP interaction; Substrate: guanosine 5’-methane phosphonate; Technique: Equilibrium Dialysis ; Experimental conditions: PP (50mM), pH (pH 7.4)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. 28. The pyrophosphate exchange and pyrophosphorolysis reactions of deoxyribonucleic acid polymerase. KM 600nM Reaction: Pyrophosphorolysis; Substrate: DNA template; Experimental conditions: Temp (37°C)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. 28. The pyrophosphate exchange and pyrophosphorolysis reactions of deoxyribonucleic acid polymerase. Ki 0.7mM Reaction: Nucleotide incorporation; Inhibitor: [PP]; Substrate: dNTPs; Experimental conditions: Temp (37°C)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. 28. The pyrophosphate exchange and pyrophosphorolysis reactions of deoxyribonucleic acid polymerase. Percent/Fold Effect 50 % decrease Reaction: Nucleotide incorporation; Substrate: dNTPs; Experimental conditions: PP (1mM)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. 28. The pyrophosphate exchange and pyrophosphorolysis reactions of deoxyribonucleic acid polymerase. Percent/Fold Effect 85 % increase Reaction: Nucleotide incorporation; Substrate: dNTPs; Experimental conditions: PP (2mM)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. 28. The pyrophosphate exchange and pyrophosphorolysis reactions of deoxyribonucleic acid polymerase. Percent/Fold Effect 0 % decrease Reaction: Pyrophosphorolysis; Substrate: DNA template; Experimental conditions: pH (pH 6.5), Temp (37°C)
Eco Pol I Enzymatic synthesis of deoxyribonucleic acid. 28. The pyrophosphate exchange and pyrophosphorolysis reactions of deoxyribonucleic acid polymerase. Percent/Fold Effect 95 % decrease Reaction: Pyrophosphorolysis; Substrate: DNA template; Experimental conditions: pH (pH 9), Temp (37°C)
Eco Pol I 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 1.09E+05 Dalton
Eco Pol I 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
Eco Pol I 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 Yes
Eco Pol I 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. Specific Activity 4500 units/mg Technique: Polymerase Assay (calf thymus DNA)
Eco Pol I 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. Percent/Fold Effect 9.75 fold increase Reaction: 5-3' Exonuclease; Substrate: DNA template; Experimental conditions: TTP (.5mM)
Eco Pol I 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 1.09E+05 Dalton
Eco Pol I 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
Eco Pol I 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 Yes
Eco Pol I 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 4500 units/mg Technique: Polymerase Assay (calf thymus DNA)
Eco Pol I 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 0.85 at 278nm

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