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Polymerase: RB69

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Polymerase Reference Property Result Context
RB69 Different behaviors in vivo of mutations in the beta hairpin loop of the DNA polymerases of the closely related phages T4 and RB69. Kd 54nM Reaction: Polymerase-DNA interaction; Substrate: DNA template
RB69 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. 3-5' Exonuclease (proofreading) Yes
RB69 The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. Kd 909uM Reaction: Misincorporation; Substrate: dATP
RB69 The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. Kd 761uM Reaction: Misincorporation; Substrate: dGTP
RB69 The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. Kd 4500uM Reaction: Misincorporation; Substrate: dCTP
RB69 The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. Kd 725uM Reaction: Misincorporation; Substrate: dGTP
RB69 The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. Kd 3363uM Reaction: Misincorporation; Substrate: dCTP
RB69 The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. Kd 1715uM Reaction: Misincorporation; Substrate: dTTP
RB69 The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. Kd 2085uM Reaction: Misincorporation; Substrate: dCTP
RB69 The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. Kd 1986uM Reaction: Misincorporation; Substrate: dTTP
RB69 The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. Kd 1391uM Reaction: Misincorporation; Substrate: dTTP
RB69 The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. Kd 50uM Reaction: Nucleotide incorporation; Substrate: dATP
RB69 The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. Kd 69uM Reaction: Nucleotide incorporation; Substrate: dCTP
RB69 The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. 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
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. kcat 0.004 /second Reaction: Misincorporation; Substrate: dATP
RB69 The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. kcat 0.011 /second Reaction: Misincorporation; Substrate: dGTP
RB69 The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. kcat 0.77 /second Reaction: Misincorporation; Substrate: dCTP
RB69 The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. kcat 0.041 /second Reaction: Misincorporation; Substrate: dGTP
RB69 The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. kcat 0.001 /second Reaction: Misincorporation; Substrate: dCTP
RB69 The L561A substitution in the nascent base-pair binding pocket of RB69 DNA polymerase reduces base discrimination. kcat 0.09 /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
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. 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. 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. kcat 17 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover (Substrat: 3'-tailed duplex phosphorothioate)
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. kcat 3 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 6.5)
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. kcat 5 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 7)
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. kcat 6.6 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 7.5)
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. 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. kcat 8.1 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover ; Experimental conditions: pH (pH 8.5)
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. kcat 24 /second Reaction: 3-5' Exonuclease; Substrate: DNA template; Technique: Single Turnover (Substrate: 3'-tailed duplex all-oxygen substrate)
RB69 Structure and enzymatic properties of a chimeric bacteriophage RB69 DNA polymerase and single-stranded DNA binding protein with increased processivity. Cloned or native Cloned in E. coli
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

Version:20241218

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.