Table 1 Kinetic parameters of PhoA at 24 °C, in 100 mM Tris buffered solution (pH 8.2) with 100 µM magnesium chloride.

From: Enzyme promiscuity in natural environments: alkaline phosphatase in the ocean

Substrate

kcat (s−1)

KM (µmol l−1)

kcat/KM (µmol l−1 s−1)

P-monoesterase

0.5 ± 0.03

94 ± 35

(4.8 ± 0.8) × 10−3

P-diesterase

(1.7 ± 0.1) × 10−2

0.3 ± 0.1

(5.5 ± 0.8) × 10−2

P-triesterase

(2.5 ± 0.1) × 10−2

(1.5 ± 0.4) × 10−2

1.7 ± 0.3

  1. Data are reported as the mean ± standard deviation of curve fitting.
  2. kcat turnover rate (Vmax divided by enzyme concentration), KM Michaelis–Menten constant, kcat/KM catalytic efficiency.
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