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Fatty Acyl-CoA Reductase and Wax Synthase from Euglena gracilis in the Biosynthesis of Medium-Chain Wax Esters
Fatty Acyl-CoA Reductase and Wax Synthase from Euglena gracilis in the Biosynthesis of Medium-Chain Wax Esters
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Fatty Acyl-CoA Reductase and Wax Synthase from Euglena gracilis in the Biosynthesis of Medium-Chain Wax Esters
Fatty Acyl-CoA Reductase and Wax Synthase from Euglena gracilis in the Biosynthesis of Medium-Chain Wax Esters

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Fatty Acyl-CoA Reductase and Wax Synthase from Euglena gracilis in the Biosynthesis of Medium-Chain Wax Esters
Fatty Acyl-CoA Reductase and Wax Synthase from Euglena gracilis in the Biosynthesis of Medium-Chain Wax Esters
Journal Article

Fatty Acyl-CoA Reductase and Wax Synthase from Euglena gracilis in the Biosynthesis of Medium-Chain Wax Esters

2010
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Overview
Euglena gracilis, a unicellular phytoflagellate, can accumulate a large amount of medium-chain wax esters under anaerobic growth conditions. Here we report the identification and characterization of two genes involved in the biosynthesis of wax esters in E. gracilis. The first gene encodes a fatty acyl-CoA reductase (EgFAR) involved in the conversion of fatty acyl-CoAs to fatty alcohols and the second gene codes for a wax synthase (EgWS) catalyzing esterification of fatty acyl-CoAs and fatty alcohols, yielding wax esters. When expressed in yeast (Saccharomyces cerevisiae), EgFAR converted myristic acid (14:0) and palmitic acid (16:0) to their corresponding alcohols (14:0Alc and 16:0Alc) with myristic acid as the preferred substrate. EgWS utilized a broad range of fatty acyl-CoAs and fatty alcohols as substrates with the preference towards myristic acid and palmitoleyl alcohol. The wax biosynthetic pathway was reconstituted by co-expressing EgFAR and EgWS in yeast. When myristic acid was fed to the yeast, myristyl myristate (14:0-14:0), myristyl palmitoleate (14:0-16:1), myristyl palmitate (14:0-16:0) and palmityl myristate (16:0-14:0) were produced. These results indicate EgFAR and EgWS are likely the two enzymes involved in the biosynthesis of medium-chain wax esters in E. gracilis.
Publisher
Berlin/Heidelberg : Springer-Verlag,Springer-Verlag,Springer‐Verlag,Springer Nature B.V
Subject

acyltransferases

/ Acyltransferases - classification

/ Acyltransferases - genetics

/ Acyltransferases - metabolism

/ Alcohols

/ aldehyde oxidoreductases

/ Aldehyde Oxidoreductases - classification

/ Aldehyde Oxidoreductases - genetics

/ Aldehyde Oxidoreductases - metabolism

/ Amino Acid Sequence

/ Animals

/ biochemical pathways

/ Biomedical and Life Sciences

/ Biosynthesis

/ chemistry

/ classification

/ complementary DNA

/ enzyme activity

/ enzyme substrates

/ Enzymes

/ enzymology

/ Esterification

/ Esters

/ Esters - chemistry

/ Esters - metabolism

/ Euglena

/ Euglena gracilis

/ Euglena gracilis - chemistry

/ Euglena gracilis - enzymology

/ Euglena gracilis - metabolism

/ fatty acid esters

/ Fatty Acids

/ Fatty Acids - chemistry

/ Fatty Acids - metabolism

/ Fatty acyl‐CoA reductase

/ Fatty alcohol

/ fatty alcohols

/ gene expression

/ genetic transformation

/ genetics

/ Growth conditions

/ Life Sciences

/ Lipidology

/ Lipids

/ Long-chain-alcohol O-fatty-acyl-transferase

/ Medical Biochemistry

/ Medicinal Chemistry

/ medium chain fatty acids

/ metabolism

/ Microbial Genetics and Genomics

/ molecular cloning

/ Molecular Sequence Data

/ Neurochemistry

/ Nutrition

/ Original Article

/ Palmitic acid

/ Phylogeny

/ Protozoan Proteins

/ Protozoan Proteins - genetics

/ Protozoan Proteins - metabolism

/ recombinant fusion proteins

/ reductase

/ Saccharomyces cerevisiae

/ Sequence Alignment

/ sequence analysis

/ Substrate Specificity

/ Wax ester

/ Wax synthase

/ wax-ester synthase

/ Waxes

/ Waxes - chemistry

/ Waxes - metabolism

/ Yeasts