Chloroplastic Glycolipids Fuel the Aldehyde Biosynthesis in the Marine Diatom Thalassiosira rotula (Articolo in rivista)

Type
Label
  • Chloroplastic Glycolipids Fuel the Aldehyde Biosynthesis in the Marine Diatom Thalassiosira rotula (Articolo in rivista) (literal)
Anno
  • 2006-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1002/cbic.200500343 (literal)
Alternative label
  • Cutignano A.; d'Ippolito G.; Romano G.; Lamari, N.; Cimino G.; Febbraio F.; Nucci R.; Fontana A. (2006)
    Chloroplastic Glycolipids Fuel the Aldehyde Biosynthesis in the Marine Diatom Thalassiosira rotula
    in ChemBioChem (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Cutignano A.; d'Ippolito G.; Romano G.; Lamari, N.; Cimino G.; Febbraio F.; Nucci R.; Fontana A. (literal)
Pagina inizio
  • 450 (literal)
Pagina fine
  • 456 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 7 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 3 (literal)
Note
  • Scopu (literal)
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • CNR, Istituto di Chimica Biomolecolare, Via Campi Flegrei 34, 80078 Pozzuoli, Napoli (Italy); Stazione Zoologica \"A. Dohrn\", Villa Comunale 1, 80121 Napoli (Italy); CNR, Istituto di Chimica delle Proteine (IBP), Via Pietro Castellino 111, 80131 Napoli (Italy) (literal)
Titolo
  • Chloroplastic Glycolipids Fuel the Aldehyde Biosynthesis in the Marine Diatom Thalassiosira rotula (literal)
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. (literal)
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