RB69
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Different behaviors in vivo of mutations in the beta hairpin loop of the DNA polymerases of the closely related phages T4 and RB69.
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Kd
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54nM
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Reaction: Polymerase-DNA interaction; Substrate: DNA template
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RB69
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Structural and biochemical investigation of the role in proofreading of a beta hairpin loop found in the exonuclease domain of a replicative DNA polymerase of the B family.
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3-5' Exonuclease (proofreading)
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Yes
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RB69
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The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
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Kd
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909uM
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Reaction: Misincorporation; Substrate: dATP
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RB69
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The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
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Kd
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761uM
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Reaction: Misincorporation; Substrate: dGTP
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RB69
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The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
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Kd
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4500uM
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Reaction: Misincorporation; Substrate: dCTP
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RB69
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The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
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Kd
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725uM
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Reaction: Misincorporation; Substrate: dGTP
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RB69
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The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
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Kd
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3363uM
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Reaction: Misincorporation; Substrate: dCTP
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RB69
|
The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
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Kd
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1715uM
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Reaction: Misincorporation; Substrate: dTTP
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RB69
|
The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
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Kd
|
2085uM
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Reaction: Misincorporation; Substrate: dCTP
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RB69
|
The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
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Kd
|
1986uM
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Reaction: Misincorporation; Substrate: dTTP
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RB69
|
The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
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Kd
|
1391uM
|
Reaction: Misincorporation; Substrate: dTTP
|
RB69
|
The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
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Kd
|
50uM
|
Reaction: Nucleotide incorporation; Substrate: dATP
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RB69
|
The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
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Kd
|
69uM
|
Reaction: Nucleotide incorporation; Substrate: dCTP
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RB69
|
The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
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Kd
|
26uM
|
Reaction: Nucleotide incorporation; Substrate: dGTP
|
RB69
|
The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
|
Kd
|
42uM
|
Reaction: Nucleotide incorporation; Substrate: dTTP
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RB69
|
The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
|
Kd
|
811uM
|
Reaction: Misincorporation; Substrate: dATP
|
RB69
|
The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
|
Kd
|
784uM
|
Reaction: Misincorporation; Substrate: dGTP
|
RB69
|
The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
|
Kd
|
1800uM
|
Reaction: Misincorporation; Substrate: dATP
|
RB69
|
The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
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kcat
|
0.004 /second
|
Reaction: Misincorporation; Substrate: dATP
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RB69
|
The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
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kcat
|
0.011 /second
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Reaction: Misincorporation; Substrate: dGTP
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RB69
|
The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
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kcat
|
0.77 /second
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Reaction: Misincorporation; Substrate: dCTP
|
RB69
|
The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
|
kcat
|
0.041 /second
|
Reaction: Misincorporation; Substrate: dGTP
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RB69
|
The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
|
kcat
|
0.001 /second
|
Reaction: Misincorporation; Substrate: dCTP
|
RB69
|
The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
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kcat
|
0.09 /second
|
Reaction: Misincorporation; Substrate: dTTP
|
RB69
|
The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
|
kcat
|
0.013 /second
|
Reaction: Misincorporation; Substrate: dCTP
|
RB69
|
The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
|
kcat
|
0.14 /second
|
Reaction: Misincorporation; Substrate: dTTP
|
RB69
|
The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
|
kcat
|
0.015 /second
|
Reaction: Misincorporation; Substrate: dTTP
|
RB69
|
The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
|
kcat
|
220 /second
|
Reaction: Nucleotide incorporation; Substrate: dATP
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RB69
|
The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
|
kcat
|
200 /second
|
Reaction: Nucleotide incorporation; Substrate: dCTP
|
RB69
|
The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
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kcat
|
167 /second
|
Reaction: Nucleotide incorporation; Substrate: dGTP
|
RB69
|
The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
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kcat
|
240 /second
|
Reaction: Nucleotide incorporation; Substrate: dTTP
|
RB69
|
The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
|
kcat
|
0.013 /second
|
Reaction: Misincorporation; Substrate: dATP
|
RB69
|
The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
|
kcat
|
0.003 /second
|
Reaction: Misincorporation; Substrate: dGTP
|
RB69
|
The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination.
|
kcat
|
0.08 /second
|
Reaction: Misincorporation; Substrate: dATP
|
RB69
|
Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity.
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kcat
|
17 /second
|
Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover (Substrat: 3'-tailed duplex phosphorothioate)
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RB69
|
Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity.
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kcat
|
3 /second
|
Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 6.5)
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RB69
|
Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity.
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kcat
|
5 /second
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Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 7)
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RB69
|
Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity.
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kcat
|
6.6 /second
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Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 7.5)
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RB69
|
Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity.
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kcat
|
7.7 /second
|
Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 8)
|
RB69
|
Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity.
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kcat
|
8.1 /second
|
Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 8.5)
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RB69
|
Pre-steady-state kinetics of RB69 DNA polymerase and its exo domain mutants: effect of pH and thiophosphoryl linkages on 3'-5' exonuclease activity.
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kcat
|
24 /second
|
Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover (Substrate: 3'-tailed duplex all-oxygen substrate)
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RB69
|
Structure and enzymatic properties of a chimeric bacteriophage RB69 DNA polymerase and single-stranded DNA binding protein with increased processivity.
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Cloned or native
|
Cloned in E. coli
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RB69
|
Structure and enzymatic properties of a chimeric bacteriophage RB69 DNA polymerase and single-stranded DNA binding protein with increased processivity.
|
Full length or truncated
|
Full length
|
|
RB69
|
Structure and enzymatic properties of a chimeric bacteriophage RB69 DNA polymerase and single-stranded DNA binding protein with increased processivity.
|
Processivity
|
45.5bp
|
|
RB69
|
Structure and enzymatic properties of a chimeric bacteriophage RB69 DNA polymerase and single-stranded DNA binding protein with increased processivity.
|
Kd
|
2.17nM
|
|