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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