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Table 2 Additional kinetic parameters for ACMO

From: Kinetic characterization of acetone monooxygenase from Gordonia sp. strain TY-5

Enzyme Parameters Measured values
ACMO K I (NADP+) 166 ± 13 µM
H325K K I (NADP+) 27 ± 6 µM
ACMO kunc (s−1) 0.26 ± 0.02 s−1
ACMO kred (s−1) 59 ± 3 s−1
ACMO K d (NADPH) 120 ± 14 μM
  1. The inhibition constant for NADP+, Ki (NADP+) was determined in the presence of 200 μM butanone. The turnover rates for uncoupled NADPH oxidation (kunc) were measured with 100 μM NADPH. The limiting rate constant for NADPH-dependent flavin reduction (kred) and the dissociation constant for NADPH (Kd (NADPH)) were determined by fitting Eq. 6 to the data shown in Fig. 4a. All reactions were performed at 25 °C in 50 mM HEPES–NaOH, pH 7.5