Biosynthesis of Castor Oil: Effect of Polyamines on the Acylation of Lysophosphatidic Acid at the sn-2 Position with Ricinoleic Acid

Mitsuhiro TOMOSUGI; Akane OHSHIRO; Shin’ichiro HARA; Ken’ichi ICHIHARA

doi:10.1271/bbb.70044

This article has now been updated. Please use the final version.

Biosynthesis of Castor Oil: Effect of Polyamines on the Acylation of Lysophosphatidic Acid at the sn-2 Position with Ricinoleic Acid

Mitsuhiro TOMOSUGI, Akane OHSHIRO, Shin’ichiro HARA, Ken’ichi ICHIHARA

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Keywords: polyamine, lysophosphatidic acid acyltransferase, 2-ricinoleoyl phosphatidic acid

JOURNAL FREE ACCESS Advance online publication

Article ID: 70044

DOI https://doi.org/10.1271/bbb.70044

The final version of this article is now available: Vol. 71 (2007) , No. 8 p.2052

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Abstract

Polyamines with diamine structures of chain length longer than 3C were essential for the synthesis of phosphatidic acid (PA) from ricinoleoyl-CoA and lysophosphatidic acid (LPA) by the castor LPA acyltransferase reaction, suggesting that polyamines modulate enzyme affinity for the acyl-CoA substrate in vivo.

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