Fidelity of nucleotide incorporation by human mitochondrial DNA polymerase
AA Johnson, KA Johnson - Journal of Biological Chemistry, 2001 - ASBMB
We have examined the fidelity of polymerization catalyzed by the human mitochondrial DNA
polymerase using wild-type and exonuclease-deficient (E200A mutation) forms of
recombinant, reconstituted holoenzyme. Each of the four nucleotides bind and incorporate
with similar kinetics; the average dissociation constant for ground state binding is 0.8 μm,
and the average rate of polymerization is 37 s− 1, defining a specificity constant k cat/K m=
4.6× 10 7 m− 1 s− 1. Mismatched nucleotides show weaker ground-state nucleotide binding …
polymerase using wild-type and exonuclease-deficient (E200A mutation) forms of
recombinant, reconstituted holoenzyme. Each of the four nucleotides bind and incorporate
with similar kinetics; the average dissociation constant for ground state binding is 0.8 μm,
and the average rate of polymerization is 37 s− 1, defining a specificity constant k cat/K m=
4.6× 10 7 m− 1 s− 1. Mismatched nucleotides show weaker ground-state nucleotide binding …
