Enzymatic preparations and specialized analytical tools have shown that chloroplast-derived glycolipids are the main substrates for the biosynthetic pathway that produces antiproliferative polyunsaturated aldehydes in broken cells of the marine diatom Thalassiosira rotula. This process, which is associated with the formation of free fatty acids and lyso compounds from polar lipids but not triglycerides, is largely dependent on glycolipid hydrolytic activity, rather than phospholipase A2 as previously suggested. Preliminary characterization of lipolytic enzymes has revealed protein bands of 40-45 kDa. Under native conditions these proteins seem to be associated with soluble aggregates that have an apparent molecular weight of approximately 200 kDa. The biochemical process, which is similar to that described in the algal-bloom forming diatom Skeletonema costatum, suggests a mechanism based on decompartmentalization and mixing of preexisting enzymes and substrates.

Chloroplastic Glycolipids Fuel the Aldehyde Biosynthesis in the Marine Diatom Thalassiosira rotula

Cutignano A;d'Ippolito G;Cimino G;Febbraio F;Nucci R;Fontana A
2006

Abstract

Enzymatic preparations and specialized analytical tools have shown that chloroplast-derived glycolipids are the main substrates for the biosynthetic pathway that produces antiproliferative polyunsaturated aldehydes in broken cells of the marine diatom Thalassiosira rotula. This process, which is associated with the formation of free fatty acids and lyso compounds from polar lipids but not triglycerides, is largely dependent on glycolipid hydrolytic activity, rather than phospholipase A2 as previously suggested. Preliminary characterization of lipolytic enzymes has revealed protein bands of 40-45 kDa. Under native conditions these proteins seem to be associated with soluble aggregates that have an apparent molecular weight of approximately 200 kDa. The biochemical process, which is similar to that described in the algal-bloom forming diatom Skeletonema costatum, suggests a mechanism based on decompartmentalization and mixing of preexisting enzymes and substrates.
2006
Istituto di Biochimica delle Proteine - IBP - Sede Napoli
Istituto di Chimica Biomolecolare - ICB - Sede Pozzuoli
aldehydes
biosynthesis
chemical ecology
glycolipids
lipases
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/168896
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