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Table 2 Kinetic parameters of FFA conversion catalyzed by CYP-Aa162 and CYP-Sm46Δ29

From: In vitro oxidative decarboxylation of free fatty acids to terminal alkenes by two new P450 peroxygenases

Enzymes

C a12

C b14

k cat (min−1)

K H (uM)

K cat /K H (uM−1 min−1)

Hill coefficient (n)

k cat (min−1)

K m (uM)

K cat /K m (uM−1 min−1)

CYP-Aa162c

46.1 ± 17.1

93.1 ± 37.7

0.5

2.1 ± 0.8

nd

nd

nd

CYP-Sm46Δ29d

24.5 ± 6.3

58.4 ± 19.0

0.4

2.2 ± 1.0

62.5 ± 4.5

41.3 ± 5.1

1.5

  1. nd not determined
  2. aData were fitted to Hill equation (\(v = {\raise0.7ex\hbox{${V_{ \hbox{max} } \left[ {\text{S}} \right]^{n} }$} \!\mathord{\left/ {\vphantom {{V_{ \hbox{max} } \left[ {\text{S}} \right]^{n} } {\left( {K_{H}^{n} + \left[ {\text{S}} \right]^{n} } \right)}}}\right.\kern-0pt} \!\lower0.7ex\hbox{${\left( {K_{H}^{n} + \left[ {\text{S}} \right]^{n} } \right)}$}},\) n Hill coefficient)
  3. bSubstantial substrate inhibition was observed with this substrate. Data shown here were derived from Michaelis–Menten equation after omitting the inhibited rates at high substrate concentrations
  4. cInitial rates were measured by the amount of substrate consumption per μM enzyme per min
  5. dInitial rates were measured by the amount of 1-alkene formation per μM enzyme per min. Data (shown as mean ± SE) were calculated using OriginPro 8.0 program
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Biotechnology for Biofuels and Bioproducts

ISSN: 2731-3654

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