Skip to main content

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.