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  • Title: Steady-state kinetics of mouse DNA polymerase beta.
    Author: Tanabe K, Bohn EW, Wilson SH.
    Journal: Biochemistry; 1979 Jul 24; 18(15):3401-6. PubMed ID: 465481.
    Abstract:
    DNA polymerase beta from mouse myeloma has been purified to near homogeneity, and its properties have been examined. The enzyme did not catalyze a detectable level of dNTP turnover, pyrophosphate exchange, pyrophosphorolysis, 3'-exonuclease degradation, or 5'-exonuclease degradation. Steady-state kinetic studies point to an ordered bibi mechanism for the polymerization reaction. Metal activation, which is required for polymerization, did not alter the Km for either the dNTP or the template--primer.
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