Activity, stability, and structural properties of the wild type and mutant aldehyde deformylating oxygenases (ADs).

1Hydrocarbon producing activity relative to that of the wild type.2Expression level of AD protein, including the soluble and insoluble forms, in Escherichia coli is shown relative to that of the wild type.3Solubility of AD when only AD was overexpressed in E. coli for in vitro characterization of the structure and stability. +: > 60% soluble; +/–: 20–60% soluble;–: 4Fraction of dimers (%), as estimated by size exclusion chromatography.5Melting temperature, as measured by thermal denaturation. Errors are ±1°C. The Tm for the second transition is also shown for the double mutants in parenthesis.6The means and standard deviations of duplicate or quadruplicate measurements are shown.7not determined.Activity, stability, and structural properties of the wild type and mutant aldehyde deformylating oxygenases (ADs).