http://www.cnr.it/ontology/cnr/individuo/prodotto/ID15351
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
- 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
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
- 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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