show help

Results for:

Polymerase: T4

Welcome to the results summary page

This page presents all the results for a polymerase, property or reference. To find more information about a polymerase or reference, follow the relevant link.

Using Polbase tables:

Sorting:

Tables may be sorted by clicking on any of the column titles. A second click reverses the sort order. <Ctrl> + click on the column titles to sort by more than one column (e.g. family then name).

Filtering:

It is also possible to filter the table by typing into the search box above the table. This will instantly hide lines from the table that do not contain your search text.

Help icons:

The show help symbol in the upper-right corner of the page links to this help text. The question mark icon is used everywhere to indicate that help is available.

Polymerase Reference Property Result Context
T4 DNA polymerase proofreading: active site switching catalyzed by the bacteriophage T4 DNA polymerase. kcat 145 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover (with heparin); Experimental conditions: Temp (37°C), Mg++ (8mM)
T4 DNA polymerase proofreading: active site switching catalyzed by the bacteriophage T4 DNA polymerase. kcat 106 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Multiple Turnover (without heparin); Experimental conditions: Mg++ (8mM), Temp (37°C)
T4 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
T4 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)
T4 Fidelity of DNA polymerases in DNA amplification. Nucleotide Substitution Rate 3E-06 errors/bp Technique: DGGE
T4 On the fidelity of DNA replication. The accuracy of T4 DNA polymerases in copying phi X174 DNA in vitro. Nucleotide Substitution Rate 1E-06 errors/bp Technique: Reversion (1 mM dNTP)
T4 On the fidelity of DNA replication. The accuracy of T4 DNA polymerases in copying phi X174 DNA in vitro. Processivity 1840bp
T4 Gel kinetic analysis of DNA polymerase fidelity in the presence of proofreading using bacteriophage T4 DNA polymerase. Nucleotide Substitution Rate 1E-06 errors/bp Technique: Gel kinetic assay (dCMP-A mismatch)
T4 Gel kinetic analysis of DNA polymerase fidelity in the presence of proofreading using bacteriophage T4 DNA polymerase. Nucleotide Substitution Rate 1E-05 errors/bp Technique: Gel kinetic assay (dGMP-A mismatch)
T4 Gel kinetic analysis of DNA polymerase fidelity in the presence of proofreading using bacteriophage T4 DNA polymerase. Nucleotide Substitution Rate 1E-08 errors/bp Technique: Gel kinetic assay (dAMP-A mismatch)
T4 Gel kinetic analysis of DNA polymerase fidelity in the presence of proofreading using bacteriophage T4 DNA polymerase. Nucleotide Substitution Rate 0.0002 errors/bp Technique: Gel kinetic assay (dTMP-T mismatch)
T4 Stopped-flow fluorescence study of precatalytic primer strand base-unstacking transitions in the exonuclease cleft of bacteriophage T4 DNA polymerase. Methods Featured Fluorescence Spectroscopy
T4 Error induction and correction by mutant and wild type T4 DNA polymerases. Kinetic error discrimination mechanisms. KM 4.6uM Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Primer extension assay
T4 Error induction and correction by mutant and wild type T4 DNA polymerases. Kinetic error discrimination mechanisms. KM 25.9uM Reaction: Nucleotide incorporation; Substrate: n/a; Technique: Primer extension assay (2AP)
T4 Efficient in vitro replication of double-stranded DNA templates by a purified T4 bacteriophage replication system. Vmax 500 /second Reaction: Nucleotide incorporation; Substrate: dNTPs
T4 Efficient in vitro replication of double-stranded DNA templates by a purified T4 bacteriophage replication system. Nucleotide incorporation accessory protein(s) gp 32, gp 45, gp 44/62, gp 41
T4 The 3'-5' proofreading exonuclease of bacteriophage T4 DNA polymerase is stimulated by other T4 DNA replication proteins. Exonuclease accessory protein(s) gp 45, gp 44/62, gp 32
T4 Using 2-aminopurine fluorescence to detect bacteriophage T4 DNA polymerase-DNA complexes that are important for primer extension and proofreading reactions. Methods Featured Fluorescence Spectroscopy
T4 Mutational and pH studies of the 3' --> 5' exonuclease activity of bacteriophage T4 DNA polymerase. kcat 200 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Degradation of labeled single-stranded DNA
T4 Exonuclease-polymerase active site partitioning of primer-template DNA strands and equilibrium Mg2+ binding properties of bacteriophage T4 DNA polymerase. Methods Featured Fluorescence Spectroscopy
T4 Nuclease activity in a fragment of bacteriophage T4 deoxyribonucleic acid polymerase induced by the amber mutant am B22. KM 0.04uM Reaction: 3-5' Exonuclease; Substrate: DNA template
T4 Nuclease activity in a fragment of bacteriophage T4 deoxyribonucleic acid polymerase induced by the amber mutant am B22. KM 0.08uM Reaction: 3-5' Exonuclease; Substrate: DNA template
T4 Nuclease activity in a fragment of bacteriophage T4 deoxyribonucleic acid polymerase induced by the amber mutant am B22. Vmax 91 /minute Reaction: 3-5' Exonuclease
T4 Nuclease activity in a fragment of bacteriophage T4 deoxyribonucleic acid polymerase induced by the amber mutant am B22. Vmax 2.2 /minute Reaction: 3-5' Exonuclease; Technique: Steady State (substrate: E. coli DNA, heat denatured)
T4 Different behaviors in vivo of mutations in the beta hairpin loop of the DNA polymerases of the closely related phages T4 and RB69. Kd 43nM Reaction: Polymerase-DNA interaction; Substrate: DNA template
T4 On the exonuclease activity of phage T4 deoxyribonucleic acid polymerase. Molecular Weight 1.15E+05 Dalton
T4 On the exonuclease activity of phage T4 deoxyribonucleic acid polymerase. 3-5' Exonuclease (proofreading) Yes
T4 On the exonuclease activity of phage T4 deoxyribonucleic acid polymerase. Cloned or native Native organism
T4 On the exonuclease activity of phage T4 deoxyribonucleic acid polymerase. Tagged No
T4 On the exonuclease activity of phage T4 deoxyribonucleic acid polymerase. Full length or truncated Full length
T4 On the exonuclease activity of phage T4 deoxyribonucleic acid polymerase. Specific Activity 2.3E+04 units/mg
T4 Isolation, characterization, and kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3'-5' exonuclease activity. 3-5' Exonuclease (proofreading) Yes
T4 Isolation, characterization, and kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3'-5' exonuclease activity. KM 1000uM Reaction: 3-5' Exonuclease; Substrate: DNA template
T4 Isolation, characterization, and kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3'-5' exonuclease activity. KM 7uM Reaction: 3-5' Exonuclease; Substrate: DNA template
T4 Isolation, characterization, and kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3'-5' exonuclease activity. kcat 170 /second Reaction: 3-5' Exonuclease; Substrate: DNA template
T4 Isolation, characterization, and kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3'-5' exonuclease activity. kcat 420 /second Reaction: 3-5' Exonuclease; Substrate: DNA template
T4 Functional consequences and exonuclease kinetic parameters of point mutations in bacteriophage T4 DNA polymerase. KM 6.9uM Reaction: 3-5' Exonuclease; Substrate: DNA template
T4 Functional consequences and exonuclease kinetic parameters of point mutations in bacteriophage T4 DNA polymerase. KM 0.4uM Reaction: 3-5' Exonuclease; Substrate: DNA template
T4 Functional consequences and exonuclease kinetic parameters of point mutations in bacteriophage T4 DNA polymerase. kcat 65.1 /second Reaction: 3-5' Exonuclease; Substrate: DNA template
T4 Functional consequences and exonuclease kinetic parameters of point mutations in bacteriophage T4 DNA polymerase. kcat 0.16 /second Reaction: 3-5' Exonuclease; Substrate: DNA template
T4 Enzymatic synthesis of deoxyribonucleic acid. 36. A proofreading function for the 3' leads to 5' exonuclease activity in deoxyribonucleic acid polymerases. Vmax 1100 /minute Reaction: 3-5' Exonuclease; Substrate: DNA template; Experimental conditions: pH (pH 7), Temp (37°C)
T4 Enzymatic synthesis of deoxyribonucleic acid. 36. A proofreading function for the 3' leads to 5' exonuclease activity in deoxyribonucleic acid polymerases. Vmax 350 /minute Reaction: 3-5' Exonuclease; Substrate: DNA template; Experimental conditions: pH (pH 7), Temp (37°C)
T4 Enzymatic synthesis of deoxyribonucleic acid. 36. A proofreading function for the 3' leads to 5' exonuclease activity in deoxyribonucleic acid polymerases. Vmax 850 /minute Reaction: 3-5' Exonuclease; Substrate: DNA template; Experimental conditions: pH (pH 7), Temp (30°C)
T4 Enzymatic synthesis of deoxyribonucleic acid. 36. A proofreading function for the 3' leads to 5' exonuclease activity in deoxyribonucleic acid polymerases. Vmax 27 /minute Reaction: 3-5' Exonuclease; Substrate: DNA template; Experimental conditions: pH (pH 7), Temp (30°C)
T4 An antimutator deoxyribonucleic acid polymerase. I. Purification and properties of the enzyme. KM 17uM Reaction: Nucleotide incorporation; Substrate: dTTP; Experimental conditions: Temp (30°C)
T4 An antimutator deoxyribonucleic acid polymerase. I. Purification and properties of the enzyme. KM 17uM Reaction: Nucleotide incorporation; Substrate: dTTP; Experimental conditions: Temp (43°C)
T4 An antimutator deoxyribonucleic acid polymerase. I. Purification and properties of the enzyme. KM 47uM Reaction: 3-5' Exonuclease; Substrate: DNA template; Experimental conditions: Temp (30°C)
T4 An antimutator deoxyribonucleic acid polymerase. I. Purification and properties of the enzyme. Vmax 0.33 /minute Reaction: Nucleotide incorporation; Substrate: dTTP; Experimental conditions: Temp (30°C)
T4 An antimutator deoxyribonucleic acid polymerase. I. Purification and properties of the enzyme. Vmax 0.66 /minute Reaction: Nucleotide incorporation; Substrate: dTTP; Experimental conditions: Temp (43°C)
T4 An antimutator deoxyribonucleic acid polymerase. I. Purification and properties of the enzyme. Vmax 0.15 /minute Reaction: 3-5' Exonuclease; Substrate: DNA template
T4 T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template. KM 1600uM Reaction: Nucleotide incorporation; Substrate: dCTP; Experimental conditions: pH (pH 8.8), Temp (30°C)
T4 T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template. KM 1.9uM Reaction: Nucleotide incorporation; Substrate: dCTP; Experimental conditions: pH (pH 8.8), Temp (30°C)
T4 T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template. KM 17uM Reaction: Nucleotide incorporation; Substrate: dATP; Experimental conditions: pH (pH 8.8), Temp (30°C)
T4 T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template. KM 1.3uM Reaction: Nucleotide incorporation; Substrate: dATP; Experimental conditions: pH (pH 8.8), Temp (30°C)
T4 T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template. KM 6uM Reaction: Nucleotide incorporation; Substrate: dTTP; Experimental conditions: pH (pH 8.8), Temp (30°C)
T4 T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template. KM 1.8uM Reaction: Nucleotide incorporation; Substrate: dTTP; Experimental conditions: pH (pH 8.8), Temp (30°C)
T4 T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template. KM 190uM Reaction: Nucleotide incorporation; Substrate: dGTP; Experimental conditions: pH (pH 8.8), Temp (30°C)
T4 T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template. KM 1.3uM Reaction: Nucleotide incorporation; Substrate: dGTP; Experimental conditions: pH (pH 8.8), Temp (30°C)
T4 T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template. Vmax 60 /minute Reaction: Nucleotide incorporation; Substrate: dGTP; Experimental conditions: pH (pH 8.8), Temp (30°C)
T4 T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template. Vmax 60 /minute Reaction: Nucleotide incorporation; Substrate: dCTP; Experimental conditions: pH (pH 8.8), Temp (30°C)
T4 T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template. Vmax 800 /minute Reaction: Nucleotide incorporation; Substrate: dATP; Experimental conditions: pH (pH 8.8), Temp (30°C)
T4 T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template. Vmax 1120 /minute Reaction: Nucleotide incorporation; Substrate: dTTP; Experimental conditions: pH (pH 8.8), Temp (30°C)
T4 T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template. Vmax 80 /minute Reaction: Nucleotide incorporation; Substrate: dGTP; Experimental conditions: pH (pH 8.8), Temp (30°C)
T4 T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template. Vmax 160 /minute Reaction: Nucleotide incorporation; Substrate: dCTP; Experimental conditions: pH (pH 8.8), Temp (30°C)
T4 T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template. Vmax 50 /minute Reaction: Nucleotide incorporation; Substrate: dATP; Experimental conditions: pH (pH 8.8), Temp (30°C)
T4 T4 DNA polymerase has a lower apparent Km for deoxynucleoside triphosphates complementary rather than noncomplementary to the template. Vmax 54 /minute Reaction: Nucleotide incorporation; Substrate: dTTP; Experimental conditions: pH (pH 8.8), Temp (30°C)
T4 Molecular basis for substitution mutations. Effect of primer terminal and template residues on nucleotide selection by phage T4 DNA polymerase in vitro. KM 12.3uM Reaction: Nucleotide incorporation; Substrate: dCTP; Technique: Steady State (Template: poly (dG)-(dC))
T4 Molecular basis for substitution mutations. Effect of primer terminal and template residues on nucleotide selection by phage T4 DNA polymerase in vitro. KM 38uM Reaction: Nucleotide incorporation; Substrate: dATP; Technique: Steady State (Template: poly(dA)-(dT))
T4 Molecular basis for substitution mutations. Effect of primer terminal and template residues on nucleotide selection by phage T4 DNA polymerase in vitro. KM 605uM Reaction: Misincorporation; Substrate: dGTP; Technique: Steady State (Template: poly(dA)-(dT))
T4 Molecular basis for substitution mutations. Effect of primer terminal and template residues on nucleotide selection by phage T4 DNA polymerase in vitro. KM 5950uM Reaction: Misincorporation; Substrate: dCTP; Technique: Steady State (Template: poly(dA)-(dT))
T4 Molecular basis for substitution mutations. Effect of primer terminal and template residues on nucleotide selection by phage T4 DNA polymerase in vitro. KM 1850uM Reaction: Misincorporation; Substrate: dATP; Technique: Steady State (Template: poly(dG)-(dC))
T4 Molecular basis for substitution mutations. Effect of primer terminal and template residues on nucleotide selection by phage T4 DNA polymerase in vitro. KM 4940uM Reaction: Misincorporation; Substrate: dTTP; Technique: Steady State (Template: poly(dG)-(dC))
T4 Molecular basis for substitution mutations. Effect of primer terminal and template residues on nucleotide selection by phage T4 DNA polymerase in vitro. KM 6.4uM Reaction: Nucleotide incorporation; Substrate: dGTP; Technique: Steady State (Template: poly(dG)-(dC))
T4 Incorporation of reporter-labeled nucleotides by DNA polymerases. 3-5' Exonuclease (proofreading) Yes
T4 Incorporation of reporter-labeled nucleotides by DNA polymerases. Incorporation of non-standard nucleotides Unspecified
T4 Incorporation of reporter-labeled nucleotides by DNA polymerases. Cloned or native Unspecified
T4 Incorporation of reporter-labeled nucleotides by DNA polymerases. 5-3' Exonuclease Unspecified
T4 Incorporation of reporter-labeled nucleotides by DNA polymerases. Tagged Unspecified
T4 Incorporation of reporter-labeled nucleotides by DNA polymerases. Full length or truncated Unspecified
T4 Incorporation of reporter-labeled nucleotides by DNA polymerases. Application name PCR
T4 On the role of deoxyribonucleic acid polymerase in determining mutation rates. Characterization of the defect in the T4 deoxyribonucleic acid polymerase caused by the ts L88 mutation. 3-5' Exonuclease (proofreading) Yes
T4 On the role of deoxyribonucleic acid polymerase in determining mutation rates. Characterization of the defect in the T4 deoxyribonucleic acid polymerase caused by the ts L88 mutation. Cloned or native Native organism
T4 On the role of deoxyribonucleic acid polymerase in determining mutation rates. Characterization of the defect in the T4 deoxyribonucleic acid polymerase caused by the ts L88 mutation. Tagged No
T4 On the role of deoxyribonucleic acid polymerase in determining mutation rates. Characterization of the defect in the T4 deoxyribonucleic acid polymerase caused by the ts L88 mutation. Full length or truncated Full length
T4 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 130 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover (Substrate: 3'-tailed duplex all-oxygen substrate)
T4 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 91 /second Reaction: 3-5' Exonuclease; Substrate: DNA template
T4 Characterization of the stimulatory effect of T4 gene 45 protein and the gene 44/62 protein complex on DNA synthesis by T4 DNA polymerase. Processivity 3000bp
T4 Characterization of the stimulatory effect of T4 gene 45 protein and the gene 44/62 protein complex on DNA synthesis by T4 DNA polymerase. Nucleotide incorporation accessory protein(s) 44/62 and 45 proteins
T4 A single mutation in bacteriophage T4 DNA polymerase (A737V, tsL141) decreases its processivity as a polymerase and increases its processivity as a 3'-->5' exonuclease. 3-5' Exonuclease (proofreading) Yes
T4 A single mutation in bacteriophage T4 DNA polymerase (A737V, tsL141) decreases its processivity as a polymerase and increases its processivity as a 3'-->5' exonuclease. Cloned or native Cloned in E. coli
T4 A single mutation in bacteriophage T4 DNA polymerase (A737V, tsL141) decreases its processivity as a polymerase and increases its processivity as a 3'-->5' exonuclease. Full length or truncated Full length
T4 A single mutation in bacteriophage T4 DNA polymerase (A737V, tsL141) decreases its processivity as a polymerase and increases its processivity as a 3'-->5' exonuclease. Specific Activity 3039 units/mg
T4 Processivity of the gene 41 DNA helicase at the bacteriophage T4 DNA replication fork. Full length or truncated Full length
T4 Processivity of the gene 41 DNA helicase at the bacteriophage T4 DNA replication fork. Processivity 380bp
T4 Processivity of the gene 41 DNA helicase at the bacteriophage T4 DNA replication fork. Vmax 400 /second Reaction: Nucleotide incorporation; Substrate: dNTPs
T4 Dissociation of bacteriophage T4 DNA polymerase and its processivity clamp after completion of Okazaki fragment synthesis. Cloned or native Cloned in E. coli
T4 Dissociation of bacteriophage T4 DNA polymerase and its processivity clamp after completion of Okazaki fragment synthesis. Full length or truncated Full length
T4 Dissociation of bacteriophage T4 DNA polymerase and its processivity clamp after completion of Okazaki fragment synthesis. Processivity 1500bp
T4 The dynamic processivity of the T4 DNA polymerase during replication. Full length or truncated Full length
T4 The dynamic processivity of the T4 DNA polymerase during replication. Vmax 150 /second Reaction: Nucleotide incorporation; Substrate: dNTPs
T4 The dynamic processivity of the T4 DNA polymerase during replication. Kd 145nM Reaction: Nucleotide incorporation; Substrate: dNTPs
T4 The slow dissociation of the T4 DNA polymerase holoenzyme when stalled by nucleotide omission. An indication of a highly processive enzyme. 3-5' Exonuclease (proofreading) Unspecified
T4 The slow dissociation of the T4 DNA polymerase holoenzyme when stalled by nucleotide omission. An indication of a highly processive enzyme. Cloned or native Cloned in E. coli
T4 The slow dissociation of the T4 DNA polymerase holoenzyme when stalled by nucleotide omission. An indication of a highly processive enzyme. 5-3' Exonuclease Unspecified
T4 The slow dissociation of the T4 DNA polymerase holoenzyme when stalled by nucleotide omission. An indication of a highly processive enzyme. Full length or truncated Full length
T4 The slow dissociation of the T4 DNA polymerase holoenzyme when stalled by nucleotide omission. An indication of a highly processive enzyme. Processivity 46bp
T4 RNA priming of DNA replication by bacteriophage T4 proteins. Extension from RNA primer Yes
T4 Pentaribonucleotides of mixed sequence are synthesized and efficiently prime de novo DNA chain starts in the T4 bacteriophage DNA replication system. Extension from RNA primer Yes
T4 Studies of the DNA helicase-RNA primase unit from bacteriophage T4. A trinucleotide sequence on the DNA template starts RNA primer synthesis. Extension from RNA primer Yes
T4 Bacteriophage T4 DNA primase-helicase. Characterization of the DNA synthesis primed by T4 61 protein in the absence of T4 41 protein. Extension from RNA primer Yes
T4 DNA synthesis on a double-stranded DNA template by the T4 bacteriophage DNA polymerase and the T4 gene 32 DNA unwinding protein. Nick Extension Yes, unspecified mechanism
T4 Bacteriophage T4 RNase H removes both RNA primers and adjacent DNA from the 5' end of lagging strand fragments. RNase H Yes
T4 The proofreading 3'-->5' exonuclease activity of DNA polymerases: a kinetic barrier to translesion DNA synthesis. 3-5' Exonuclease (proofreading) Yes
T4 The proofreading 3'-->5' exonuclease activity of DNA polymerases: a kinetic barrier to translesion DNA synthesis. 5-3' Exonuclease No
T4 The proofreading 3'-->5' exonuclease activity of DNA polymerases: a kinetic barrier to translesion DNA synthesis. Extension from RNA primer Yes
T4 Architecture of the bacteriophage T4 replication complex revealed with nanoscale biopointers. 3-5' Exonuclease (proofreading) Yes
T4 Architecture of the bacteriophage T4 replication complex revealed with nanoscale biopointers. 5-3' Exonuclease No
T4 Architecture of the bacteriophage T4 replication complex revealed with nanoscale biopointers. Extension from RNA primer Yes
T4 Spectrum of spontaneous frameshift mutations. Sequences of bacteriophage T4 rII gene frameshifts. Frameshift Error Rate 3E-07 errors/bp
T4 Enzymatic synthesis of deoxyribonucleic acid. XXV. Purification and properties of deoxyribonucleic acid polymerase induced by infection with phage T4. Molecular Weight 1.12E+05 Dalton
T4 Enzymatic synthesis of deoxyribonucleic acid. XXV. Purification and properties of deoxyribonucleic acid polymerase induced by infection with phage T4. 3-5' Exonuclease (proofreading) Yes
T4 Enzymatic synthesis of deoxyribonucleic acid. XXV. Purification and properties of deoxyribonucleic acid polymerase induced by infection with phage T4. 5-3' Exonuclease No
T4 Enzymatic synthesis of deoxyribonucleic acid. XXV. Purification and properties of deoxyribonucleic acid polymerase induced by infection with phage T4. Full length or truncated Full length
T4 Enzymatic synthesis of deoxyribonucleic acid. XXV. Purification and properties of deoxyribonucleic acid polymerase induced by infection with phage T4. Optimal pH pH 8.5
T4 Enzymatic synthesis of deoxyribonucleic acid. XXV. Purification and properties of deoxyribonucleic acid polymerase induced by infection with phage T4. Specific Activity 3.3E+04 units/mg Technique: Polymerase Assay (calf thymus DNA)
T4 Enzymatic synthesis of deoxyribonucleic acid. XXV. Purification and properties of deoxyribonucleic acid polymerase induced by infection with phage T4. Strand Displacement No
T4 Enzymatic synthesis of deoxyribonucleic acid. XXV. Purification and properties of deoxyribonucleic acid polymerase induced by infection with phage T4. Percent/Fold Effect 0 % decrease Reaction: 3-5' Exonuclease; Substrate: DNA template; Experimental conditions: Mg++ (6mM)
T4 Enzymatic synthesis of deoxyribonucleic acid. XXV. Purification and properties of deoxyribonucleic acid polymerase induced by infection with phage T4. Percent/Fold Effect 75 % decrease Reaction: 3-5' Exonuclease; Substrate: DNA template; Experimental conditions: Mg++ (.1mM)
T4 Enzymatic synthesis of deoxyribonucleic acid. XXV. Purification and properties of deoxyribonucleic acid polymerase induced by infection with phage T4. Percent/Fold Effect 0 % decrease Reaction: 3-5' Exonuclease; Substrate: DNA template; Experimental conditions: NTPs (0mM)
T4 Enzymatic synthesis of deoxyribonucleic acid. XXV. Purification and properties of deoxyribonucleic acid polymerase induced by infection with phage T4. Percent/Fold Effect 49 % decrease Reaction: 3-5' Exonuclease; Substrate: DNA template; Experimental conditions: GTP (0.2mM), ATP (0mM), CTP (0mM), TTP (0mM)
T4 Enzymatic synthesis of deoxyribonucleic acid. XXV. Purification and properties of deoxyribonucleic acid polymerase induced by infection with phage T4. Percent/Fold Effect 81 % decrease Reaction: 3-5' Exonuclease; Substrate: DNA template; Experimental conditions: GTP (0.2mM), ATP (0.2mM), CTP (0mM)
T4 Enzymatic synthesis of deoxyribonucleic acid. XXV. Purification and properties of deoxyribonucleic acid polymerase induced by infection with phage T4. Percent/Fold Effect 96 % decrease Reaction: 3-5' Exonuclease; Substrate: DNA template; Experimental conditions: GTP (0.2mM), ATP (0.2mM), CTP (0.2mM), TTP (0mM)
T4 Enzymatic synthesis of deoxyribonucleic acid. XXV. Purification and properties of deoxyribonucleic acid polymerase induced by infection with phage T4. Gap Filling Yes
T4 Effect of accessory proteins on T4 DNA polymerase replication fidelity. 3-5' Exonuclease (proofreading) Yes
T4 Effect of accessory proteins on T4 DNA polymerase replication fidelity. 5-3' Exonuclease Unspecified
T4 Effect of accessory proteins on T4 DNA polymerase replication fidelity. Frameshift Error Rate 1.2E-06 errors/bp Technique: M13mp2 forward mutation assay
T4 Effect of accessory proteins on T4 DNA polymerase replication fidelity. Nucleotide Substitution Rate 9.4E-07 errors/bp Technique: M13mp2 forward mutation assay
T4 Effect of accessory proteins on T4 DNA polymerase replication fidelity. Nucleotide Substitution Rate 3.3E-06 errors/bp Technique: M13mp2 opal codon reversion assay
T4 Enzymatic synthesis of deoxyribonucleic acid. XXXII. Replication of duplex deoxyribonucleic acid by polymerase at a single strand break. 5-3' Exonuclease No
T4 A constant rate of spontaneous mutation in DNA-based microbes. Overall Error Rate 2E-08 errors/bp Technique: rII+ reversion

Version:20240415

Using Polbase tables:

Sorting:

Tables may be sorted by clicking on any of the column titles. A second click reverses the sort order. <Ctrl> + click on the column titles to sort by more than one column (e.g. family then name).

Filtering:

It is also possible to filter the table by typing into the search box above the table. This will instantly hide lines from the table that do not contain your search text.