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Table 2 Apparent k cat values of some cADO mutants and WT against the preferred substrates in the presence of the competition substrates

From: Structure-oriented substrate specificity engineering of aldehyde-deformylating oxygenase towards aldehydes carbon chain length

Mutants Preferred/competition aldehydes k cat app (min−1)
WT C7 0.80 ± 0.086
C7/C4 0.80 ± 0.079
C7/C18 0.77 ± 0.14
A121F C7 1.41 ± 0.036
C7/C4 0.75 ± 0.093
C7/C18 0.69 ± 0.01
I24Y C7 1.05 ± 0.076
C7/C4 0.82 ± 0.024
C7/C18 0.39 ± 0.026
WT C8 0.33 ± 0.064
C8/C4 0.35 ± 0.057
C8/C18 0.24 ± 0.017
M193Y C8 1.05 ± 0.20
C8/C4 1.05 ± 0.18
C8/C18 0.52 ± 0.032
WT C9 0.24 ± 0.021
C9/C4 0.23 ± 0.025
C9/C18 0.18 ± 0.023
L198F C9 0.50 ± 0.024
C9/C4 0.25 ± 0.076
C9/C18 0.25 ± 0.015
  1. The apparent k cat values of some cADO mutants and WT against the preferred substrates (2 mM C7,8,9 aldehydes) in the presence of the competition substrates (2 mM n-butanal or 150 μM n-octadecanal) were determined, respectively