PhytophthoraV1, Main, Exploration, bibRecord, 000A33

Determination of Substrate Preferences for Desaturases and Elongases for Production of Docosahexaenoic Acid from Oleic Acid in Engineered Canola.

Identifieur interne : 000A33 ( Main/Exploration ); précédent : 000A32; suivant : 000A34

Determination of Substrate Preferences for Desaturases and Elongases for Production of Docosahexaenoic Acid from Oleic Acid in Engineered Canola.

Auteurs : Jenny Lindberg Yilmaz [Suède] ; Ze Long Lim [Canada] ; Mirela Beganovic [Suède] ; Steven Breazeale [États-Unis] ; Carl Andre [États-Unis] ; Sten Stymne [Suède] ; Patricia Vrinten [Canada] ; Toralf Senger [États-Unis]

Source :

Lipids [ 1558-9307 ] ; 2017.

RBID : pubmed:28197856

Descripteurs français

KwdFr :
- Acetyltransferases (génétique), Acetyltransferases (métabolisme), Acide docosahexaénoïque (métabolisme), Acide eicosapentanoïque (métabolisme), Acide oléique (métabolisme), Acyl coenzyme A (métabolisme), Brassica napus (composition chimique), Brassica napus (enzymologie), Brassica napus (génétique), Fatty acid desaturases (génétique), Fatty acid desaturases (métabolisme), Génie génétique (MeSH), Humains (MeSH), Malonyl coenzyme A (métabolisme), Protéines végétales (génétique), Protéines végétales (métabolisme), Saccharomyces cerevisiae (génétique), Spécificité du substrat (MeSH).
MESH :
- composition chimique : Brassica napus.
- enzymologie : Brassica napus.
- génétique : Acetyltransferases, Brassica napus, Fatty acid desaturases, Protéines végétales, Saccharomyces cerevisiae.
- métabolisme : Acetyltransferases, Acide docosahexaénoïque, Acide eicosapentanoïque, Acide oléique, Acyl coenzyme A, Fatty acid desaturases, Malonyl coenzyme A, Protéines végétales.
- Génie génétique, Humains, Spécificité du substrat.

English descriptors

KwdEn :
- Acetyltransferases (genetics), Acetyltransferases (metabolism), Acyl Coenzyme A (metabolism), Brassica napus (chemistry), Brassica napus (enzymology), Brassica napus (genetics), Docosahexaenoic Acids (metabolism), Eicosapentaenoic Acid (metabolism), Fatty Acid Desaturases (genetics), Fatty Acid Desaturases (metabolism), Genetic Engineering (MeSH), Humans (MeSH), Malonyl Coenzyme A (metabolism), Oleic Acid (metabolism), Plant Proteins (genetics), Plant Proteins (metabolism), Saccharomyces cerevisiae (genetics), Substrate Specificity (MeSH).
MESH :
- chemical , genetics : Acetyltransferases, Fatty Acid Desaturases, Plant Proteins.
- chemical , metabolism : Acetyltransferases, Acyl Coenzyme A, Docosahexaenoic Acids, Eicosapentaenoic Acid, Fatty Acid Desaturases, Malonyl Coenzyme A, Oleic Acid, Plant Proteins.
- chemistry : Brassica napus.
- enzymology : Brassica napus.
- genetics : Brassica napus, Saccharomyces cerevisiae.
- Genetic Engineering, Humans, Substrate Specificity.

Abstract

Production of eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA) in plant seed oils has been pursued to improve availability of these omega-3 fatty acids that provide important human health benefits. Canola (Brassica napus), through the introduction of 10 enzymes, can convert oleic acid (OLA) into EPA and ultimately DHA through a pathway consisting of two elongation and five desaturation steps. Herein we present an assessment of the substrate specificity of the seven desaturases and three elongases that were introduced into canola by expressing individual proteins in yeast. In vivo feeding experiments were conducted with 14 potential fatty acid intermediates in an OLA to DHA pathway to determine the fatty acid substrate profiles for each enzyme. Membrane fractions were prepared from yeast expression strains and shown to contain active enzymes. The elongases, as expected, extended acyl-CoA substrates in the presence of malonyl-CoA. To distinguish between enzymes that desaturate CoA- and phosphatidylcholine-linked fatty acid substrates, we developed a novel in vitro method. We show that a delta-12 desaturase from Phytophthora sojae, an omega-3 desaturase from Phytophthora infestans and a delta-4 desaturase from Thraustochytrium sp., all prefer phosphatidylcholine-linked acyl substrates with comparatively low use of acyl-CoA substrates. To further validate our method, a delta-9 desaturase from Saccharomyces cerevisiae was confirmed to use acyl-CoA as substrate, but could not use phosphatidylcholine-linked substrates. The results and the assay methods presented herein will be useful in efforts to improve modeling of fatty acid metabolism and production of EPA and DHA in plants.

DOI: 10.1007/s11745-017-4235-4
PubMed: 28197856
PubMed Central: PMC5325871

Affiliations:

Canada, Suède, États-Unis

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000A40
to stream Main, to step Curation: 000A40

Le document en format XML

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<series><title level="j">Lipids</title>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Acetyltransferases (genetics)</term>
<term>Acetyltransferases (metabolism)</term>
<term>Acyl Coenzyme A (metabolism)</term>
<term>Brassica napus (chemistry)</term>
<term>Brassica napus (enzymology)</term>
<term>Brassica napus (genetics)</term>
<term>Docosahexaenoic Acids (metabolism)</term>
<term>Eicosapentaenoic Acid (metabolism)</term>
<term>Fatty Acid Desaturases (genetics)</term>
<term>Fatty Acid Desaturases (metabolism)</term>
<term>Genetic Engineering (MeSH)</term>
<term>Humans (MeSH)</term>
<term>Malonyl Coenzyme A (metabolism)</term>
<term>Oleic Acid (metabolism)</term>
<term>Plant Proteins (genetics)</term>
<term>Plant Proteins (metabolism)</term>
<term>Saccharomyces cerevisiae (genetics)</term>
<term>Substrate Specificity (MeSH)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Acetyltransferases (génétique)</term>
<term>Acetyltransferases (métabolisme)</term>
<term>Acide docosahexaénoïque (métabolisme)</term>
<term>Acide eicosapentanoïque (métabolisme)</term>
<term>Acide oléique (métabolisme)</term>
<term>Acyl coenzyme A (métabolisme)</term>
<term>Brassica napus (composition chimique)</term>
<term>Brassica napus (enzymologie)</term>
<term>Brassica napus (génétique)</term>
<term>Fatty acid desaturases (génétique)</term>
<term>Fatty acid desaturases (métabolisme)</term>
<term>Génie génétique (MeSH)</term>
<term>Humains (MeSH)</term>
<term>Malonyl coenzyme A (métabolisme)</term>
<term>Protéines végétales (génétique)</term>
<term>Protéines végétales (métabolisme)</term>
<term>Saccharomyces cerevisiae (génétique)</term>
<term>Spécificité du substrat (MeSH)</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Acetyltransferases</term>
<term>Fatty Acid Desaturases</term>
<term>Plant Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Acetyltransferases</term>
<term>Acyl Coenzyme A</term>
<term>Docosahexaenoic Acids</term>
<term>Eicosapentaenoic Acid</term>
<term>Fatty Acid Desaturases</term>
<term>Malonyl Coenzyme A</term>
<term>Oleic Acid</term>
<term>Plant Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Brassica napus</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Brassica napus</term>
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</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Brassica napus</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Acetyltransferases</term>
<term>Brassica napus</term>
<term>Fatty acid desaturases</term>
<term>Protéines végétales</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acetyltransferases</term>
<term>Acide docosahexaénoïque</term>
<term>Acide eicosapentanoïque</term>
<term>Acide oléique</term>
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<term>Fatty acid desaturases</term>
<term>Malonyl coenzyme A</term>
<term>Protéines végétales</term>
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<term>Humans</term>
<term>Substrate Specificity</term>
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<front><div type="abstract" xml:lang="en">Production of eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA) in plant seed oils has been pursued to improve availability of these omega-3 fatty acids that provide important human health benefits. Canola (Brassica napus), through the introduction of 10 enzymes, can convert oleic acid (OLA) into EPA and ultimately DHA through a pathway consisting of two elongation and five desaturation steps. Herein we present an assessment of the substrate specificity of the seven desaturases and three elongases that were introduced into canola by expressing individual proteins in yeast. In vivo feeding experiments were conducted with 14 potential fatty acid intermediates in an OLA to DHA pathway to determine the fatty acid substrate profiles for each enzyme. Membrane fractions were prepared from yeast expression strains and shown to contain active enzymes. The elongases, as expected, extended acyl-CoA substrates in the presence of malonyl-CoA. To distinguish between enzymes that desaturate CoA- and phosphatidylcholine-linked fatty acid substrates, we developed a novel in vitro method. We show that a delta-12 desaturase from Phytophthora sojae, an omega-3 desaturase from Phytophthora infestans and a delta-4 desaturase from Thraustochytrium sp., all prefer phosphatidylcholine-linked acyl substrates with comparatively low use of acyl-CoA substrates. To further validate our method, a delta-9 desaturase from Saccharomyces cerevisiae was confirmed to use acyl-CoA as substrate, but could not use phosphatidylcholine-linked substrates. The results and the assay methods presented herein will be useful in efforts to improve modeling of fatty acid metabolism and production of EPA and DHA in plants.</div>
</front>
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<Abstract><AbstractText>Production of eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA) in plant seed oils has been pursued to improve availability of these omega-3 fatty acids that provide important human health benefits. Canola (Brassica napus), through the introduction of 10 enzymes, can convert oleic acid (OLA) into EPA and ultimately DHA through a pathway consisting of two elongation and five desaturation steps. Herein we present an assessment of the substrate specificity of the seven desaturases and three elongases that were introduced into canola by expressing individual proteins in yeast. In vivo feeding experiments were conducted with 14 potential fatty acid intermediates in an OLA to DHA pathway to determine the fatty acid substrate profiles for each enzyme. Membrane fractions were prepared from yeast expression strains and shown to contain active enzymes. The elongases, as expected, extended acyl-CoA substrates in the presence of malonyl-CoA. To distinguish between enzymes that desaturate CoA- and phosphatidylcholine-linked fatty acid substrates, we developed a novel in vitro method. We show that a delta-12 desaturase from Phytophthora sojae, an omega-3 desaturase from Phytophthora infestans and a delta-4 desaturase from Thraustochytrium sp., all prefer phosphatidylcholine-linked acyl substrates with comparatively low use of acyl-CoA substrates. To further validate our method, a delta-9 desaturase from Saccharomyces cerevisiae was confirmed to use acyl-CoA as substrate, but could not use phosphatidylcholine-linked substrates. The results and the assay methods presented herein will be useful in efforts to improve modeling of fatty acid metabolism and production of EPA and DHA in plants.</AbstractText>
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<Author ValidYN="Y"><LastName>Lim</LastName>
<ForeName>Ze Long</ForeName>
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<AffiliationInfo><Affiliation>Bioriginal Food and Science Corporation, Saskatoon, SK, S7N 0W9, Canada.</Affiliation>
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<Author ValidYN="Y"><LastName>Beganovic</LastName>
<ForeName>Mirela</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Scandinavian Biotechnology Research (ScanBiRes) AB, 230 53, Alnarp, Sweden.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Andre</LastName>
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</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Stymne</LastName>
<ForeName>Sten</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Department of Plant Breeding, Swedish University of Agricultural Sciences, 230 53, Alnarp, Sweden.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Vrinten</LastName>
<ForeName>Patricia</ForeName>
<Initials>P</Initials>
<AffiliationInfo><Affiliation>Bioriginal Food and Science Corporation, Saskatoon, SK, S7N 0W9, Canada.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Senger</LastName>
<ForeName>Toralf</ForeName>
<Initials>T</Initials>
<AffiliationInfo><Affiliation>BASF Plant Science LP, Research Triangle Park, NC, 27709, USA.</Affiliation>
</AffiliationInfo>
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<Language>eng</Language>
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<Month>02</Month>
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Determination of Substrate Preferences for Desaturases and Elongases for Production of Docosahexaenoic Acid from Oleic Acid in Engineered Canola.

Determination of Substrate Preferences for Desaturases and Elongases for Production of Docosahexaenoic Acid from Oleic Acid in Engineered Canola.

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