Steady-state and pre-steady-state kinetic constants were determined for reverse transcriptase catalyzed incorporation of nucleotides and nucleotide analogues into defined-sequence DNA primed-RNA templates. 3'-Azido-3'-deoxythymidine 5'-triphosphate (AZTTP) was almost as efficient a substrate (kcat/Km) as dTTP for the enzyme. In contrast, the
Catalytic Cooperativity among Subunits of Escherichia coli Transcription Termination Factor Rho KINETICS AND SUBSTRATE STRUCTURAL REQUIREMENTS
Browne R J, et al.
The Journal of Biological Chemistry, 280(14), 13292-13299 (2005)
We used a series of dATP and dGTP analogues to determine how DNA polymerase I from Bacillus stearothermophilus (BF), a prototypical A family polymerase, uses N-1, N(2), N-3, and N(6) of purine dNTPs to differentiate between right and wrong nucleotide
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