The CYP52 multigene family of Candida maltosa encodes functionally diverse n-alkane-inducible cytochromes P450.

The n-alkane-assimilating yeast Candida maltosa contains several structurally related cytochromes P450 (P450) encoded by the CYP52 multigene family, which are inducible by various long-chain hydrocarbons and fatty acids and which are responsible for the initial hydroxylation steps in the metabolism of these substrates. In the present work, the four major n-alkane-inducible C. maltosa P450 forms; CYP52A3, CYP52A4, CYP52A5, and CYP52A9, were enzymatically characterized, taking advantage of heterologous P450/reductase coexpression in Saccharomyces cerevisiae. Testing various alkanes and fatty acids, distinct preferences of the individual P450 forms concerning substrate class and chain length were detected, thus providing new insight into the functional diversity of the C. maltosa CYP52 family. Moreover, the results obtained emphasize these structurally related enzymes as a powerful tool for future studies on P450 structure-function relationships.