Dissociation constant of polymerase beta

Value 23 µM Range: ±4 µM
Organism Bacteriophage T7
Reference Ahn J, Kraynov VS, Zhong X, Werneburg BG, Tsai MD. DNA polymerase beta: effects of gapped DNA substrates on dNTP specificity, fidelity, processivity and conformational changes. Biochem J. 1998 Apr 1331 ( Pt 1):79-87 Table - link PubMed ID9512464
Method Pre-steady-state kinetic analysis was used to compare the catalytic properties of DNA polymerase beta (Pol beta) for single-base gap-filling and regular duplex DNA synthesis. The rate of polymerization (kpol) and the apparent equilibrium dissociation constant of dNTP (Kd) were determined with single-nucleotide gapped DNA substrates for all four possible correct base pairs and twelve possible incorrect base pairs, and the results were compared with those obtained previously with non-gapped primer/template duplex DNA substrates.
Entered by Uri M
ID 104146