Table 1 Kinetic parameters of the NADH and NADPH peroxidases from intestinal sulfate-reducing bacteria*

From: NADH and NADPH peroxidases as antioxidant defense mechanisms in intestinal sulfate-reducing bacteria

Kinetic parameters

D. piger Vib-7

D. orale Rod-9

NADH

NADPH

NADH

NADPH

Exponential growth phase

 V0 (µmol × min-1 × mg−1 protein)

141 ± 13

289 ± 27

127 ± 11

144 ± 13

 Pmax (µmol × mg−1 protein)

51 ± 4

43 ± 3

38 ± 3

27 ± 2

 τ (min)

0.36 ± 0.03

0.15 ± 0.012

0.30 ± 0.017

0.19 ± 0.017

 Vmax (µmol × min−1 × mg−1 protein)

66 ± 5

61 ± 5

58 ± 6

70 ± 6

 Km (mM)

0.97 ± 0.08

1.21 ± 0.11

1.58 ± 0.13

4.76 ± 0.44

Stationary growth phase

 V0 (µmol × min−1 × mg−1 protein)

828 ± 7

343 ± 24

368 ± 34

103 ± 9

 Pmax (µmol × mg−1 protein)

84 ± 7

43 ± 4

51 ± 4

32 ± 2

 τ (min)

0.10 ± 0.09

0.13 ± 0.01

0.14 ± 0.01

0.31 ± 0.02

 Vmax (µmol × min−1 × mg−1 protein)

132 ± 12

69 ± 5

78 ± 6

70 ± 6

 Km (mM)

1.42 ± 0.11

1.49 ± 0.13

1.02 ± 0.10

3.24 ± 0.31

  1. *V0 is initial (instantaneous) reaction rate; Pmax is maximum amount (plateau) of the reaction product; τ is the reaction time (half saturation period), Vmax is maximum rate of the enzyme reaction; Km is Michaelis constant which was determined by substrate (hydrogen peroxide). Statistical significance of the values mean ± SD, n = 5; ***P < 0.001, compared to the D. piger Vib-7 strain.