A lipoxygenase with linoleate diol synthase activity from Nostoc sp. PCC 7120.

A lipoxygenase with linoleate diol synthase activity from Nostoc sp. PCC 7120. Research Abstract Details 

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A lipoxygenase with linoleate diol synthase activity from Nostoc sp. PCC 7120. Abstract Text:

Imke Lang,Cornelia Göbel,Andrea Porzel,Ingo Heilmann,Ivo Feussner,Imke Lang,Cornelia Göbel,Andrea Porzel,Ingo Heilmann,Ivo Feussner,

The dioxygenation of PUFAs (polyunsaturated fatty acids) in plants is mainly catalysed by members of the LOX (lipoxygenase) enzyme family. LOX products may be further metabolized, and are known as signalling substances in plant development and in responses to wounding and pathogen attack. In contrast with the situation in eukaryotes, information on the relevance of lipid peroxide metabolism in prokaryotic organisms is scarce. Therefore, we aimed to analyse LOXs and oxylipin patterns of cyanobacterial origin. A search of the genomic sequence of the cyanobacterium Nostoc sp. PCC 7120 suggested an open reading frame encoding a putative LOX named NspLOX that harboured an N-terminal extension. Individual analysis of recombinant C-terminal domain revealed enzymatic activity as a linoleate (9R)-LOX. Analysis of the full-length NspLOX protein, however, revealed linoleate diol synthase activity, generating (10E,12E)-9,14-dihydroxy-10,12-octadecadienoic acid as the main product from LA (linoleic acid) and (10E,12E,14E)-9,16-dihydroxy-10,12,14-octadecatrienoic acid as the main product from ALA (alpha-LA) substrates respectively, with ALA as preferred substrate. The enzyme exhibited a broad pH optimum between pH 7 and pH 10. Soluble extracts of Nostoc sp. contain more 9-LOX-derived hydroperoxides in sonified than in non-sonified cells, but products of full-length NspLOX were not detectable under the conditions used. As no other LOX-like sequence was identified in the genome of Nostoc sp. PCC 7120, the results presented suggest that (9R)-LOX-derived oxylipins may represent the endogenous products of NspLOX. Based on the biochemical results of NspLOX, we suggest that this bifunctional enzyme may represent a more ancient way to control the intracellular amount of oxylipins in this cyanobacterium.

A lipoxygenase with linoleate diol synthase activity from Nostoc sp. PCC 7120. Publishing Authors By Initials

I Lang,C Göbel,A Porzel,I Heilmann,I Feussner,I Lang,C Göbel,A Porzel,I Heilmann,I Feussner,

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A lipoxygenase with linoleate diol synthase activity from Nostoc sp. PCC 7120. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: The Biochemical journal

VOLUME: 410

Page Numbers: 347-57

Journal Abbreviation: Biochem. J.

ISSN: 1470-8728

DAY: 1

MONTH: Mar

YEAR: 2008

A lipoxygenase with linoleate diol synthase activity from Nostoc sp. PCC 7120. Information

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LANGUAGE: eng

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Grant and Affiliation Information for A lipoxygenase with linoleate diol synthase activity from Nostoc sp. PCC 7120.

AFFILIATION: Department of Plant Biochemistry, Albrecht-von-Haller-Institute for Plant Sciences, Georg-August-University, 37077 Goettingen, Germany.

Country: England

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MEDLINETA: Biochem J

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