2018
DOI: 10.12691/jfnr-6-2-4
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Molecular Cloning and Functional Characterisation of a Polyunsaturated Fatty Acid Elongase in a Marine Bivalve <i>Crassostrea</i><i> </i><i>angulata</i>

Abstract: The elongases of fatty acids (ELO) are essential for long chain polyunsaturated fatty acid (LC-PUFA) biosynthesis, and their activities depend on the substrates. The full length cDNA of Crassostrea angulata ELO (CaELO) was cloned by RACE PCR and its function was confirmed. The CaELO encodes a polypeptide of 309 amino acid residues, which containes a histidine box HXXHH motif conserved in all elongases and shares high similarity to the elongases of Chlamys nobilis and Octopus vulgaris. Phylogenetic analysis sho… Show more

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Cited by 17 publications
(11 citation statements)
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References 29 publications
(55 reference statements)
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“…This protein was termed "Elovl5/2" or "Elovl2/5" (Monroig et al 2013b(Monroig et al , 2016bLiu et al 2013) based on its phylogenetic relationship with the vertebrate Elovl2 and Elovl5 elongases. Similar proteins were subsequently characterised from S. officinalis (Monroig et al 2016a), C. nobilis (Liu et al 2013) and Crassostrea angulata (Zhang et al 2018). Regarding its function, the mollusc Elovl2/5 can efficiently elongate C 18-20 PUFA substrates, but has no activity towards C 22 substrates.…”
Section: Molluscsmentioning
confidence: 88%
“…This protein was termed "Elovl5/2" or "Elovl2/5" (Monroig et al 2013b(Monroig et al , 2016bLiu et al 2013) based on its phylogenetic relationship with the vertebrate Elovl2 and Elovl5 elongases. Similar proteins were subsequently characterised from S. officinalis (Monroig et al 2016a), C. nobilis (Liu et al 2013) and Crassostrea angulata (Zhang et al 2018). Regarding its function, the mollusc Elovl2/5 can efficiently elongate C 18-20 PUFA substrates, but has no activity towards C 22 substrates.…”
Section: Molluscsmentioning
confidence: 88%
“…However, in conditions of a PUFA deficiency in animals living in extreme environmental conditions, for example, in deep-sea ecosystems, there is no compensation for this deficiency by endogenous synthesis of PUFAs. As a result, a low content of PUFAs in mollusks or their absence is observed with the simultaneous compensatory increase in the number of NMI FAs [116,[135][136][137][138][139]. There is ample evidence of the increase in NMI FAs with a shortage of PUFA [71,76,119,140].…”
Section: Dietary Source Of Pufas Versus Own Biosynthetic Capability Omentioning
confidence: 99%
“…Two different types of Elovl with roles in LC-PUFA biosynthesis have been characterized from marine molluscs. More specifically, an enzyme called "Elovl2/5", regarded as an ancestral protein of the vertebrate Elovl2 and Elovl5 [16], has been characterized from the cephalopods Octopus vulgaris and Sepia officinalis [17,18], and the bivalves Chlamys nobilis and Crassostrea angulate [19,20]. Furthermore, Elovl4 orthologs have been characterized from C. nobilis and O.…”
Section: Introductionmentioning
confidence: 99%