Molecular and functional characterization of a fads2 orthologue in the Amazonian teleost, Arapaima gigas

• Tipo: Artigo em Revista Científica Internacional
• Data: 2017

Autores

Lopes Marques, M (Autor) Outra; Ozorio, R (Autor) Outra; Amaral, R (Autor) Outra; Tocher, DR (Autor) Outra; Monroig, O (Autor) Outra; Filipe F C Castro (Autor) FCUP

Revista

Título: COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY

Vol. 203

Páginas: 84-91

ISSN: 0305-0491

Editora: Elsevier

Indexação

ISI Web of Knowledge - 27 Citações

Scopus - 26 Citações

Outras Informações

ID Authenticus: P-00M-4EW

DOI: 10.1016/j.cbpb.2016.09.007

Abstract (EN): The Brazilian teleost Arapaima gigas is an iconic species of the Amazon. In recent years a significant effort has been put into the farming of arapaima to mitigate overfishing threats. However, little is known regarding the nutritional requirements of A. gigas in particular those for essential fatty acids including the long-chain polyunsaturated fatty acids (LC-PUFA) eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA). The ability to biosynthesize LC-PUFA is dependent upon the gene repertoire of fatty acyl desaturases (Fads) and elongases (Elov1), as well as their fatty acid specificities. In the present study we characterized both molecularly and functionally an orthologue of the desaturase fatty acid desaturase 2 (fads2) from A. gigas. The isolated sequence displayed the typical desaturase features, a cytochrome b(5)-domain with the heme-binding motif, two transmembrane domains and three histidine-rich regions. Functional characterization of A. gigas fads2 showed that, similar to other teleosts, the A. gigas fads2 exhibited a predominant Delta 6 activity complemented with some capacity for Delta 8 denaturation. Given that A. gigas belongs to one of the oldest teleostei lineages, the Osteoglossomorpha, these findings offer a significant insight into the evolution LC-PUFA biosynthesis in teleosts.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 8