Table 2 Kinetic parameters of enzymatic hydrolysis of PAR

From: Structural and biochemical evidence supporting poly ADP-ribosylation in the bacterium Deinococcus radiodurans

Protein

Km(µM)

Vmax (µmol/min/mg protein)

kcat (1/s)

kcat/Km (1/s/µM)

WT

2.96 ± 0.90

515.60 ± 62.90

266.40 ± 32.50

90.00 ± 29.47

T267R

9.34 ± 1.92

384.30 ± 46.81

198.60 ± 24.19

21.26 ± 4.92

T267K

11.14 ± 2.75

351.00 ± 53.73

181.40 ± 27.76

16.28 ± 4.73

E112A

ND

ND

ND

ND

  1. Values are mean plus or minus SEM (n = 3 independent experiments). Fitted Michaelis–Menten plots are shown in Fig. 5a
  2. PAR poly-ADP-ribose, WT wild type, ND no enzymatic activity detected
Back to article page