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Polymerase: KF D424A

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Polymerase Reference Property Result Context
KF D424A The 3'-5' exonuclease of DNA polymerase I of Escherichia coli: contribution of each amino acid at the active site to the reaction. Specific Activity 9000 units/mg Technique: Polymerase assay (poly[d(AT)]
KF D424A The 3'-5' exonuclease of DNA polymerase I of Escherichia coli: contribution of each amino acid at the active site to the reaction. kcat 1.3E-08 /second Reaction: 3-5' Exonuclease; Technique: Steady State (dsDNA, assuming WT has rate 0.001/s); Experimental conditions: pH (pH 7.5), Temp (37°C)
KF D424A The fidelity of DNA synthesis catalyzed by derivatives of Escherichia coli DNA polymerase I. 3-5' Exonuclease (proofreading) No
KF D424A The fidelity of DNA synthesis catalyzed by derivatives of Escherichia coli DNA polymerase I. Frameshift Error Rate 5E-06 errors/bp Technique: M13mp2 forward mutation assay (1mM dNTP; combined with D355A,E357A results)
KF D424A The fidelity of DNA synthesis catalyzed by derivatives of Escherichia coli DNA polymerase I. Nucleotide Substitution Rate 2.5E-05 errors/bp Technique: M13mp2 forward mutation assay (1mM dNTP; combined with D355A,E357A results)
KF D424A Genetic and crystallographic studies of the 3',5'-exonucleolytic site of DNA polymerase I. Other Important Residues Metal B not bound
KF D424A Genetic and crystallographic studies of the 3',5'-exonucleolytic site of DNA polymerase I. Specific Activity 9300 units/mg Technique: Polymerase assay (poly[d(AT)]
KF D424A Genetic and crystallographic studies of the 3',5'-exonucleolytic site of DNA polymerase I. Specific Activity 1.3E-05 units/mg Technique: Exo activity (arbitrary units) (relative to WT = 1)
KF D424A The fidelity of DNA synthesis catalyzed by derivatives of Escherichia coli DNA polymerase I. 3-5' Exonuclease (proofreading) No
KF D424A The fidelity of DNA synthesis catalyzed by derivatives of Escherichia coli DNA polymerase I. Frameshift Error Rate 0.0043 errors/bp Technique: Forward mutational (1 uM dNTP)
KF D424A The fidelity of DNA synthesis catalyzed by derivatives of Escherichia coli DNA polymerase I. Nucleotide Substitution Rate 0.00012 errors/bp Technique: Reversion (1 uM dNTP)

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.