This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Benveniste, I. Articles by Durst, F. Search for Related Content PubMed PubMed Citation Articles by Benveniste, I. Articles by Durst, F. Agricola Articles by Benveniste, I. Articles by Durst, F.

Articles

Cytochrome P-450-Dependent -Hydroxylation of Lauric Acid by Microsomes from Pea Seedlings ¹

Laboratoire de Physiologie Vegetale, Universite Louis Pasteur, Equipe de Recherhe Associee au Centre National de la Recherche Scientifique 104, 67083 Strasbourg Cedex, France

Microsomes from apical buds of pea (Pisum sativum L. var. Téléphone à rames) seedlings hydroxylate lauric acid at the -position. This oxidation is catalyzed by a cytochrome P-450 enzyme which differs from laurate hydroxylases previously described in microorganisms and mammals by its strict substrate specificity and the ability of low NADH concentrations to support unusually high oxidation rates. The apparent K_m for lauric acid was 20 micromolar. NADPH- and NADH-dependent laurate hydroxylation followed non-Michaelian kinetics with apparent K_m values ranging from 0.2 to 28 micromolar for NADPH, and 0.2 to 318 micromolar for NADH. When induced by the photomorphogenic photoreceptor phytochrome, the time course for the enhancement of laurate -hydroxylase was totally different from that of the cinnamic acid 4-hydroxylase, providing evidence for the existence of multiple cytochrome P-450 species in pea microsomes.

This article has been cited by other articles:

				R. Hofer, I. Briesen, M. Beck, F. Pinot, L. Schreiber, and R. Franke The Arabidopsis cytochrome P450 CYP86A1 encodes a fatty acid {omega}-hydroxylase involved in suberin monomer biosynthesis J. Exp. Bot., June 1, 2008; 59(9): 2347 - 2360. [Abstract] [Full Text] [PDF]

				S. Kandel, M. Morant, I. Benveniste, E. Blee, D. Werck-Reichhart, and F. Pinot Cloning, Functional Expression, and Characterization of CYP709C1, the First Sub-terminal Hydroxylase of Long Chain Fatty Acid in Plants: INDUCTION BY CHEMICALS AND METHYL JASMONATE J. Biol. Chem., October 28, 2005; 280(43): 35881 - 35889. [Abstract] [Full Text] [PDF]

				M. Fukuchi-Mizutani, M. Mizutani, Y. Tanaka, T. Kusumi, and D. Ohta Microsomal Electron Transfer in Higher Plants: Cloning and Heterologous Expression of NADH-Cytochrome b5 Reductase from Arabidopsis Plant Physiology, January 1, 1999; 119(1): 353 - 362. [Abstract] [Full Text]

				F. Pinot, I. Benveniste, J.-P. Salaün, and F. Durst Methyl Jasmonate Induces Lauric Acid omega -Hydroxylase Activity and Accumulation of CYP94A1 Transcripts but Does Not Affect Epoxide Hydrolase Activities in Vicia sativa Seedlings Plant Physiology, December 1, 1998; 118(4): 1481 - 1486. [Abstract] [Full Text]

				F. Adas, F. Berthou, D. Picart, P. Lozac'h, F. Beaugé, and Y. Amet Involvement of cytochrome P450 2E1 in the ({omega}–1)-hydroxylation of oleic acid in human and rat liver microsomes J. Lipid Res., June 1, 1998; 39(6): 1210 - 1219. [Abstract] [Full Text]

				S. Pflugmacher and H. Sandermann Jr. Cytochrome P450 Monooxygenases for Fatty Acids and Xenobiotics in Marine Macroalgae Plant Physiology, May 1, 1998; 117(1): 123 - 128. [Abstract] [Full Text]

				F. Cabello-Hurtado, Y. Batard, J.-P. Salaun, F. Durst, F. Pinot, and D. Werck-Reichhart Cloning, Expression in Yeast, and Functional Characterization of CYP81B1, a Plant Cytochrome P450 That Catalyzes In-chain Hydroxylation of Fatty Acids J. Biol. Chem., March 27, 1998; 273(13): 7260 - 7267. [Abstract] [Full Text] [PDF]