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Table 2 Kinetic parameters of Sty(A2)B reductases

From: Catalytic and hydrodynamic properties of styrene monooxygenases from Rhodococcus opacus 1CP are modulated by cofactor binding

Reductase-strain

Substrate changed*

Maximum activity (U mg−1)

k cat (s−1)

K M (µM)

Catalytic efficiency (s−1 µM−1)

StyB-1CP

NADH

75.1 ± 1.8

26.9 ± 0.6

59.3 ± 4.2

0.454

FAD

91.9 ± 6.6

32.9 ± 2.3

108.3 ± 18.3

0.304

StyB-ST

NADH

28.8

8.8 ± 0.1

18.9 ± 1.0

0.466

FAD

28.7

8.7 ± 0.3

2.6 ± 0.4

3.346

StyA2B-1CP**

NADH

3.7

3.9 ± 0.3

58 ± 9

0.068

FAD

4.9

5.2 ± 0.2

26 ± 2

0.203

  1. * One of the substrates was applied in excess and the concentration of the other one was varied.
  2. ** Data as previously reported (Tischler et al. 2010).