|
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 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
|
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
|
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
|
On the processive mechanism of Escherichia coli DNA polymerase I. Quantitative assessment of processivity.
|
Cloned or native
|
Cloned in E. coli
|
|
|
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 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
|
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
|
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
|
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
|
|
