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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).