Abstract

The European perch (Perca fluviatilis) is a carnivorous freshwater fish able to metabolise polyunsaturated fatty acids (PUFA) into highly unsaturated fatty acids (HUFA). This makes it a potential candidate for sustainable aquaculture development. In this study, special attention is given to the fatty-acid elongase (ELOVL) family, one of the two enzymatic systems implied in the HUFA biosynthesis. Structural information on European perch enzyme converting PUFA into HUFA is obtained by both molecular cloning and in silico characterization of an ELOVL5-like elongase from P. fluviatilis (pfELOVL). The full-length cDNA sequence consists of a 885-base pair Open Reading Frame coding for a 294-amino acid protein. Phylogenetic analysis and sequence alignment with fish elongases predict the pfELOVL clusters within the ELOVL5 sub-group. The amino-acid sequence displays the typical ELOVL features: several transmembrane α helices (TMH), an endoplasmic reticulum (ER) retention signal, and four “conserved boxes” involved in the catalytic site. In addition, the topology analysis predicts a 7-TMH structure addressed in the ER membrane. A 3D model of the protein embedded in an ER-like membrane environment is also provided using de novo modelling and molecular dynamics. From docking studies, two putative enzyme–substrate-binding modes, including H bonds and CH–π interactions, emphasize the role of specific residues in the “conserved boxes”.

Original languageEnglish
Article number242
Pages (from-to)242
Number of pages14
Journal3 Biotech
Volume9
Issue number6
DOIs
Publication statusPublished - 1 Jun 2019

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Perca fluviatilis
highly unsaturated fatty acids
molecular cloning
endoplasmic reticulum
fatty acids
polyunsaturated fatty acids
molecular dynamics
sequence alignment
active sites
freshwater fish
topology
open reading frames
aquaculture
amino acid sequences
proteins
biosynthesis
amino acids
phylogeny
enzymes
fish

Cite this

@article{c090ddeedef544b0a9db42b357f06857,
title = "Molecular cloning and 3D model of a fatty-acid elongase in a carnivorous freshwater teleost, the European perch (Perca fluviatilis)",
abstract = "The European perch (Perca fluviatilis) is a carnivorous freshwater fish able to metabolise polyunsaturated fatty acids (PUFA) into highly unsaturated fatty acids (HUFA). This makes it a potential candidate for sustainable aquaculture development. In this study, special attention is given to the fatty-acid elongase (ELOVL) family, one of the two enzymatic systems implied in the HUFA biosynthesis. Structural information on European perch enzyme converting PUFA into HUFA is obtained by both molecular cloning and in silico characterization of an ELOVL5-like elongase from P. fluviatilis (pfELOVL). The full-length cDNA sequence consists of a 885-base pair Open Reading Frame coding for a 294-amino acid protein. Phylogenetic analysis and sequence alignment with fish elongases predict the pfELOVL clusters within the ELOVL5 sub-group. The amino-acid sequence displays the typical ELOVL features: several transmembrane α helices (TMH), an endoplasmic reticulum (ER) retention signal, and four “conserved boxes” involved in the catalytic site. In addition, the topology analysis predicts a 7-TMH structure addressed in the ER membrane. A 3D model of the protein embedded in an ER-like membrane environment is also provided using de novo modelling and molecular dynamics. From docking studies, two putative enzyme–substrate-binding modes, including H bonds and CH–π interactions, emphasize the role of specific residues in the “conserved boxes”.",
author = "Emmanuel Tinti and Florian Geay and {Lopes Rodrigues}, Maximilien and Patrick Kestemont and Eric Perp{\`e}te and Catherine Michaux",
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T1 - Molecular cloning and 3D model of a fatty-acid elongase in a carnivorous freshwater teleost, the European perch (Perca fluviatilis)

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AU - Geay, Florian

AU - Lopes Rodrigues, Maximilien

AU - Kestemont, Patrick

AU - Perpète, Eric

AU - Michaux, Catherine

PY - 2019/6/1

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