4.1.99.5	A118F	site-directed mutagenesis, the mutant shows increased activity with n-butanal compared to the wild-type enzyme. A118F does not show any obvious activity against C14,16,18 aldehydes, and only exhibits slight activity towards n-dodecanal and n-decanal for long-chain substrates	747351	
4.1.99.5	A121F	site-directed mutagenesis, the mutant shows increased activity with C4,6,7 aldehydes compared to the wild-type enzyme	747351	
4.1.99.5	A134F	site-directed mutagenesis, the mutant has the same global architecture as wild-type enzyme, the mutant shows highly reduced activity with the majority of long-chain aldehyde substrates tested. the A134F variant displays an approximate fourfold increase in the rate of butanal consumption and approximately sixfold increase in pentanal consumption compared to wild-type enzyme, the mutant generates enhanced levels of propane production in whole-cell biotransformations compared to wild-type cADO	-, 727312	
4.1.99.5	A134F	site-directed mutagenesis, the mutant shows slightly increased activity compared to wild-type	-, 748564	
4.1.99.5	C107A	site-directed mutagenesis, the mutation does not affect the hydrocarbon producing activity of the enzyme	-, 749051	
4.1.99.5	C107A/C117A	site-directed mutagenesis, the mutation does not affect the hydrocarbon producing activity of the enzyme	-, 749051	
4.1.99.5	C117A	site-directed mutagenesis, the mutation does not affect the hydrocarbon producing activity of the enzyme	-, 749051	
4.1.99.5	C70F	site-directed mutagenesis, the mutant shows increased activity with n-hexanal compared to the wild-type enzyme	747351	
4.1.99.5	C71A	site-directed mutagenesis, the mutant shows reduced hydrocarbon producing activity and facilitated formation of a dimer compared to wild-type enzyme	-, 749051	
4.1.99.5	C71A/C107A	site-directed mutagenesis, the mutant has reduced activity compared to wild-type, and an activity comparable to or even lower than the activity of the C71A variant	749051