THE CYP52 MULTIGENE FAMILY OF CANDIDA-MALTOSA ENCODES FUNCTIONALLY DIVERSE N-ALKANE-INDUCIBLE CYTOCHROMES P450

The n-alkane-assimilating yeast Candida maltosa contains several struc turally related cytochromes P450 (P450) encoded by the CYP52 multigene family, which are inducible by various long-chain hydrocarbons and fa tty acids and which are responsible for the initial hydroxylation step s in the metabolism of these substrates. In the present work, the four major n-alkane-inducible C. maltosa P450 forms, CYP52A3, CYP52A4, CYP 52A5, and CYP52A9, were enzymatically characterized, taking advantage of heterologous P450/reductase coexpression in Saccharomyces cerevisia e. Testing various alkanes and fatty acids, distinct preferences of th e individual P450 forms concerning substrate class and chain length we re detected, thus providing new insight into the functional diversity of the C. maltosa CYP52 family. Moreover, the results obtained emphasi ze these structurally related enzymes as a powerful tool for future st udies on P450 structure-function relationships. (C) 1996 Academic Pres s, Inc.