On the mechanism of light induction of plant microsomal cinnamic acid 4-hydroxylase. 1975

D Scheel, and H Sandermann
Institut für Biologie II, Lehrstuhl Biochemie der Pflanzen, Universität Freiburg, Schänzlestr. 9-11, D-78, Freiburg, i.Br., Federal Republic of Germany.

The specific activities of the enzymes cinnamic acid 4-hydroxylase and cytidine-5'-diphospho-choline: 1,2-diacylglycerol cholinephosphotransferase (E.C. 2.7.8.2) were determined in microsomal fractions from a) dark-grown and b) irradiated parsley (Petroselinum hortense Hoffm.) cell suspension cultures. Cinnamic acid 4-hydroxylase activity was increased 4-fold after light treatment, while cholinephosphotransferase activity was decreased by about one third of its original activity. It can be concluded that increased microsomal lecithin biosynthesis is not required for the light-induced increase of cinnamic acid 4-hydroxylase activity, although the latter enzyme has previously been found to require a lipid cofactor for activity.

UI MeSH Term Description Entries

Related Publications

D Scheel, and H Sandermann
September 1973, Archives of biochemistry and biophysics,
D Scheel, and H Sandermann
August 1968, Die Naturwissenschaften,
D Scheel, and H Sandermann
June 1991, Indian journal of biochemistry & biophysics,
D Scheel, and H Sandermann
July 1991, Archives of biochemistry and biophysics,
D Scheel, and H Sandermann
January 1996, Methods in enzymology,
D Scheel, and H Sandermann
October 1967, Archives of biochemistry and biophysics,
D Scheel, and H Sandermann
October 1992, Indian journal of biochemistry & biophysics,
D Scheel, and H Sandermann
October 1975, Analytical biochemistry,
Copied contents to your clipboard!