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

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

Mutants	Preferred/competition aldehydes	k ^app_cat (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

The apparent k _cat values of some cADO mutants and WT against the preferred substrates (2 mM C_7,8,9 aldehydes) in the presence of the competition substrates (2 mM n-butanal or 150 μM n-octadecanal) were determined, respectively

ISSN: 2731-3654