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Table 1 Steady-state kinetic parameters of ACMO and GSTACMO

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

Enzyme Variable substrate kcat (s−1) Km (µM) kcat/Km (M−1 s−1) × 103
ACMO NADPH 2.0 ± 0.1 6.7 ± 0.8 300 ± 36
ACMO Acetone 1.4 ± 0.2 170 ± 11 8.5 ± 0.59
ACMO Butanone 2.1 ± 0.1 0.34 ± 0.03 6000 ± 550
ACMO 2-Pentanone 1.9 ± 0.1 0.37 ± 0.06 4800 ± 760
ACMO 2-Heptanone 3.9 ± 0.1 1.5 ± 0.1 2600 ± 130
ACMO 3-Methylbutanone 2.2 ± 0.1 4.4 ± 0.5 510 ± 55
ACMO 2,4-Dimethyl-3-pentanone 1.5 ± 0.1 1500 ± 220 1.0 ± 0.15
ACMO Cyclobutanone 2.0 ± 0.1 1.5 ± 0.2 1400 ± 190
ACMO Cyclopentanone 4.3 ± 0.1 120 ± 11 35 ± 3.2
ACMO Cyclohexanone 3.6 ± 0.2 2400 ± 400 1.5 ± 0.3
ACMO Bicyclo[3.2.0]hept-2-en-6-one 1.5 ± 0.1 6.7 ± 1.3 220 ± 45
ACMO Phenylacetone 1.0 ± 0.1 8.9 ± 1.5 112 ± 20
GSTACMO Cyclohexanone 2.8 ± 0.1 2300 ± 380 1.2 ± 0.2
H325K NADPH 1.6 ± 0.1 0.48 ± 0.05 3250 ± 320
H325K Butanone 1.6 ± 0.1 0.48 ± 0.05 3250 ± 320
  1. The experiments were performed in 50 mM HEPES–NaOH pH 7.5 at 25 °C as described in “Materials and methods”. Butanone was present at a fixed saturating concentration of 200 μM in steady-state experiments where NADPH served as the variable substrate. For experiments where the ketone served as the variable substrate, NADPH was present at 100 µM