Table 3 Enzyme kinetic parameters of ACT3.

From: Critical enzymes for biosynthesis of cucurbitacin derivatives in watermelon and their biological significance

Substrates

Km (µM)

kcat (S−1)

Kcat/Km (M−1 S−1)

Vmax (nmol/min/mg)

CuB

11.75 ± 1.74

1.24 × 10−2

10.56 × 102

10.34 ± 1.12

CuD

10.39 ± 1.19

1.83 × 10−2

17.63 × 102

15.27 ± 1.17

CuE

7.63 ± 4.83

0.55 × 10−2

7.21 × 102

4.58 ± 1.86

CuE-Glu

11.63 ± 1.62

2.47 × 10−2

21.21 × 102

20.56 ± 2.06

CuI

8.62 ± 0.95

1.29 × 10−2

14.97 × 102

10.75 ± 0.71

  1. ACT3 enzyme activity was determined using variable concentrations of substrate at a fixed enzyme concentration at 30 °C. Vmax and Km values were obtained by fitting values to Michaelis–Menten kinetics. Values are means ± SD, n = 3.
Back to article page