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 Web of Science 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 Web of Science (65) Citing Articles via Google Scholar Google Scholar Articles by Gardner, H. W. Articles by Plattner, R. D. Search for Related Content PubMed PubMed Citation Articles by Gardner, H. W. Articles by Plattner, R. D. Agricola Articles by Gardner, H. W. Articles by Plattner, R. D.

Metabolism and Enzymology

Hydroperoxide Lyase and Other Hydroperoxide-Metabolizing Activity in Tissues of Soybean, Glycine max

Seed Biosynthesis Research, National Center For Agricultural Utilization Research, Peoria, Illinois 61604, United States Department of Agriculture, Agricultural Research Service, Peoria, Illinois 61604

Hydroperoxide lyase (HPLS) activity in soybean (Glycine max) seed/seedlings, leaves, and chloroplasts of leaves required detergent solubilization for maximum in vitro activity. On a per milligram of protein basis, more HPLS activity was found in leaves, especially chloroplasts, than in seeds or seedlings. The total yield of hexanal from 13(S)-hydroperoxy-cis-9,trans-11-octadecadienoic acid (13S-HPOD) from leaf or chloroplast preparations was 58 and 66 to 85%, respectively. Because of significant competing hydroperoxide-metabolizing activities from other enzymes in seed/seedling preparations, the hexanal yields from this source were lower (36-56%). Some of the products identified from the seed or seedling preparations indicated that the competing activity was mainly due to both a hydroperoxide peroxygenase and reactions catalyzed by lipoxygenase. Different HPLS isozyme compositions in the seed/seedling versus the leaf/chloroplast preparations were indicated by differences in the activity as a function of pH, the K_m values, relative V_max with 13S-HPOD and 13(S)-hydroperoxy-cis-9,trans-11,cis-15-octadecatrienoic acid (13S-HPOT), and the specificity with different substrates. With regard to the latter, both seed/seedling and chloroplast HPLS utilized the 13S-HPOD and 13S-HPOT substrates, but only seeds/seedlings were capable of metabolizing 9(S)-hydroperoxy-trans-10,cis-12-octadecadienoic acid into 9-oxononanoic acid, isomeric nonenals, and 4-hydroxynonenal. From 13S-HPOD and 13S-HPOT, the products were identified as 12-oxo-cis-9-dodecenoic acid, as well as hexanal from 13S-HPOD and cis-3-hexenal from 13S-HPOT. In seed preparations, there was partial isomerization of the cis-3 or cis-9 into trans-2 or trans-10 double bonds, respectively.

This article has been cited by other articles:

				E.W. Chehab, G. Raman, J.W. Walley, J.V. Perea, G. Banu, S. Theg, and K. Dehesh Rice HYDROPEROXIDE LYASES with Unique Expression Patterns Generate Distinct Aldehyde Signatures in Arabidopsis Plant Physiology, May 1, 2006; 141(1): 121 - 134. [Abstract] [Full Text] [PDF]

				F. Schaller Enzymes of the biosynthesis of octadecanoid-derived signalling molecules J. Exp. Bot., January 1, 2001; 52(354): 11 - 23. [Abstract] [Full Text] [PDF]

				J. E. Froehlich, A. Itoh, and G. A. Howe Tomato Allene Oxide Synthase and Fatty Acid Hydroperoxide Lyase, Two Cytochrome P450s Involved in Oxylipin Metabolism, Are Targeted to Different Membranes of Chloroplast Envelope Plant Physiology, January 1, 2001; 125(1): 306 - 317. [Abstract] [Full Text]

				G. A. Howe, G. I. Lee, A. Itoh, L. Li, and A. E. DeRocher Cytochrome P450-Dependent Metabolism of Oxylipins in Tomato. Cloning and Expression of Allene Oxide Synthase and Fatty Acid Hydroperoxide Lyase Plant Physiology, June 1, 2000; 123(2): 711 - 724. [Abstract] [Full Text]

				N. J. Bate, S. Sivasankar, C. Moxon, J. M.C. Riley, J. E. Thompson, and S. J. Rothstein Molecular Characterization of an Arabidopsis Gene Encoding Hydroperoxide Lyase, a Cytochrome P-450 That Is Wound Inducible Plant Physiology, August 1, 1998; 117(4): 1393 - 1400. [Abstract] [Full Text]

				Z. Pan, B. Camara, H. W. Gardner, and R. A. Backhaus Aspirin Inhibition and Acetylation of the Plant Cytochrome P450, Allene Oxide Synthase, Resembles that of Animal Prostaglandin Endoperoxide H Synthase J. Biol. Chem., July 17, 1998; 273(29): 18139 - 18145. [Abstract] [Full Text] [PDF]

				H. W. Gardner and M. J. Grove Soybean Lipoxygenase-1 Oxidizes 3Z-Nonenal . A Route to 4S-Hydroperoxy-2E-Nonenal and Related Products Plant Physiology, April 1, 1998; 116(4): 1359 - 1366. [Abstract] [Full Text]