Induction and specificity of a (cytochrome P-450)-dependent laurate in-chain-hydroxylase from higher plant microsomes.

The substrate and product specifities of the (cytochrome P-450)-dependent laurate monooxygenase from tuber tissues of Jerusalem artichoke (Helianthus tuberosus L.) were investigated. The plant enzyme appeared strictly specific for the C12 free fatty acid and produced a mixture of C-8, C-9 and C-10 hydroxylated lauric acids, the C-9 derivative being predominant. No C-12 or C-11 hydroxylated laurates were detected. The activity of the enzyme, which was not detectable in the intact tuber, was induced by slicing and aging the tissues on water, and strongly superinduced by the addition of manganese and phenobarbital to the aging medium. Regulation of laurate hydroxylase was clearly independent from that of cinnamic acid 4-hydroxylase, another plant cytochrome P-450 enzyme.