The CYPome of Sorangium cellulosum So ce56 and Identification of CYP109D1 as a New Fatty Acid Hydroxylase

SummaryThe first systematic study of the complete cytochrome P450 complement (CYPome) of Sorangium cellulosum So ce56, which is a producer of important secondary metabolites and has the largest bacterial genome sequenced to date, is presented. We describe the bioinformatic analysis of the So ce56 cytochrome P450 complement consisting of 21 putative P450 genes. Because fatty acids play a pivotal role during the complex life cycle of myxobacteria, we focused our studies on the characterization of fatty acid hydroxylases. Three novel potential fatty acid hydroxylases (CYP109D1, CYP264A1, and CYP266A1) were used for detailed characterization. One of them, CYP109D1 was able to perform subterminal hydroxylation of saturated fatty acids with the support of two autologous and one heterologous electron transfer system(s). The kinetic parameters for the product hydroxylation were derived.

► Study of complete CYPome of Sorangium cellulosum So ce56
► Identification of two autologous and one heterologous redox partner for CYP109D1
► Kinetic studies of fatty acid hydroxylation by CYP109D1