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Table 2 Kinetic parameters of SFVmac PR-RTs for polymerization and DNA binding

From: AZT resistance alters enzymatic properties and creates an ATP-binding site in SFVmac reverse transcriptase

Enzyme 1 K M (μM) 1 V max (mM/min) V max /K M (1/min) 2 K D P/T (nM)
WT 57 (±7) 2.1 (±0.08) 36.8 (±4.7) 9.6 (±0.7)
K211I 160 (±28) 0.3 (±0.02) 1.9 (±0.4) 19.6 (±2.3)
I224T 94 (±9) 2.2 (±0.08) 23.4 (±2.4) 8.9 (±1.4)
S345T 34 (±6) 1.1 (±0.05) 32.4 (±5.9) 8.7 (±0.9)
E350K 32 (±8) 1.8 (±0.10) 56.3 (±14.4) 9.7 (±1.7)
mt2a 252 (±39) 0.5 (±0.04) 2.0 (±0.3) 7.8 (±1.2)
mt2b 159 (±41) 0.6 (±0.02) 3.8 (±1.0) 15.8 (±2.5)
mt2c 9 (±3) 2.5 (±0.10) 277.8 (±92.6) 17.2 (±2.1)
mt3 67 (±14) 2.0 (±0.10) 29.9 (±6.2) 15.8 (±2.1)
mt4 110 (±11) 1.3 (±0.05) 11.8 (±1.3) 9.5 (±1.6)
  1. 1KM- and vmax-values were obtained by using the Michaelis-Menten equation to fit a curve to the data. 2KD-values were obtained as described previously [14] by using an equation for a two state model to fit a curve to the titration data. Standard errors are given in parenthesis.