RELATION BETWEEN EVOLUTIONARY DISTANCE AND ENZYMATIC-PROPERTIES AMONGTHE MEMBERS OF THE CYP52A SUBFAMILY OF CANDIDA-MALTOSA

The CYP52A subfamily of the alkane-assimilating yeast Candida maltosa consists of six structurally related isoforms. Four of them (CYP52A3, 4, 5, and 9) are strongly induced by alkanes and play an important rol e for the conversion of various alkanes and fatty acids. Taking advant age of a homologous overexpression system, we found in the present stu dy that both of the two other CYP52A forms, CYP52A10 and CYP52A11, rep resent specialists for the hydroxylation of lauric acid suggesting the ir preference for short-chain fatty acids. At the same time, they hydr oxylated palmitic acid only moderately and failed to convert hexadecan e. Based on the now completed knowledge about the principal substrate specificities of all members of the CYP52A subfamily of C. maltosa, it became apparent that evolutionarily more distantly related P450 forms developed either to alkane or to fatty acid hydroxylases, whereas P45 0 forms which retained the ability to convert both types of substrates were also found to be evolutionarily related to both alkane and fatty acid hydroxylases. (C) 1998 Academic Press.