HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

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 Google Scholar Google Scholar Articles by Brash, A. R. Articles by Meijer, L. Search for Related Content PubMed PubMed Citation Articles by Brash, A. R. Articles by Meijer, L. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 266, Issue 34, 22926-22931, 12, 1991

Allene oxide and aldehyde biosynthesis in starfish oocytes

AR Brash, MA Hughes, DJ Hawkins, WE Boeglin, WC Song and L Meijer
Department of Pharmacology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-6602.

Allene oxides are a very unusual type of epoxide that, in biological systems, are formed by the enzymic dehydration of fatty acid hydroperoxides (lipoxygenase products). This reaction occurs widely in plants, in which allene oxide synthesis is a key step in the conversion of linolenic acid to jasmonic acid, the plant growth regulator. We report biosynthesis of the allene oxide (8R)-8,9-epoxyeicosa- (5Z,9,11Z,14Z)-tetraenoic acid via the (8R)-lipoxygenase metabolism of arachidonic acid in starfish oocytes. Formation of the allene oxide was deduced from high pressure liquid chromatography, UV, gas chromatography-mass spectrometry and 1H-NMR analyses of the precise structure and mechanism of biosynthesis of its major hydrolysis product, the alpha-ketol 8-hydroxy-9-ketoeicosa-(5Z,11Z,14Z)-trienoic acid. A second enzymic activity detected in the oocytes (hydroperoxide lyase) cleaves specifically the (8R)-hydroperoxy substrate into C7 and C13 fragments, identified as the hydroxyacid, (5Z)-7-hydroxyheptenoic acid, and two aldehydes, (2E,4Z,7Z)-tridecenal and its 4E isomer. Discovery of the allene oxide synthase and hydroperoxide lyase marks the first definitive localization of these enzymic activities to an animal cell. It was established previously that the (8R)-lipoxygenase metabolite (8R)-HETE will activate the maturation (re-initiation of meiosis) of starfish oocytes. The individual 8-lipoxygenase products may be involved at distinct stages of cell development.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				J. Liu, S. A. Seibold, C. J. Rieke, I. Song, R. I. Cukier, and W. L. Smith Prostaglandin Endoperoxide H Synthases: PEROXIDASE HYDROPEROXIDE SPECIFICITY AND CYCLOOXYGENASE ACTIVATION J. Biol. Chem., June 22, 2007; 282(25): 18233 - 18244. [Abstract] [Full Text] [PDF]

				M. L. Oldham, A. R. Brash, and M. E. Newcomer The structure of coral allene oxide synthase reveals a catalase adapted for metabolism of a fatty acid hydroperoxide PNAS, January 11, 2005; 102(2): 297 - 302. [Abstract] [Full Text] [PDF]

				O. Boutaud and A. R. Brash Purification and Catalytic Activities of the Two Domains of the Allene Oxide Synthase-Lipoxygenase Fusion Protein of the Coral Plexaura homomalla J. Biol. Chem., November 19, 1999; 274(47): 33764 - 33770. [Abstract] [Full Text] [PDF]

				R. Koljak, O. Boutaud, B. Shieh, N. Samel, and A. R. Brash Identification of a Naturally Occurring Peroxidase-Lipoxygenase Fusion Protein Science, September 26, 1997; 277(5334): 1994 - 1996. [Abstract] [Full Text]