Open AccessInduction and Specificity of a (Cytochrome P‐450)‐Dependent Laurate In‐chain‐Hydroxylase from Higher Plant Microsomes
Author(s) -
SALAÜN JeanPierre,
BENVENISTE Irène,
REICHHART Danièle,
DURST Francis
Publication year - 1981
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1981.tb05657.x
Subject(s) - cytochrome , lauric acid , enzyme , biochemistry , chemistry , monooxygenase , microsome , cytochrome p450 , fatty acid
The sustrate 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 C 12 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 laureates were detected. The activity of the enzyme, 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.