WillowV1, Main, Corpus, bibRecord, 001E18

Gaining insight into the role of serine 282 in B. napus FAE1 condensing enzyme.

Identifieur interne : 001E18 ( Main/Corpus ); précédent : 001E17; suivant : 001E19

Gaining insight into the role of serine 282 in B. napus FAE1 condensing enzyme.

Auteurs : Vesna Katavic ; Dennis L. Barton ; E Michael Giblin ; Darwin W. Reed ; Arvind Kumar ; David C. Taylor

Source :

FEBS letters [ 0014-5793 ] ; 2004.

RBID : pubmed:15044011

English descriptors

KwdEn :
- Acetyltransferases (genetics), Acetyltransferases (metabolism), Amino Acids (chemistry), Amino Acids (metabolism), Brassica napus (enzymology), Brassica napus (genetics), Fatty Acid Elongases (MeSH), Molecular Structure (MeSH), Mutagenesis, Site-Directed (MeSH), Plant Proteins (genetics), Plant Proteins (metabolism), Serine (metabolism).
MESH :
- chemical , chemistry : Amino Acids.
- chemical , genetics : Acetyltransferases, Plant Proteins.
- chemical , metabolism : Acetyltransferases, Amino Acids, Plant Proteins, Serine.
- enzymology : Brassica napus.
- genetics : Brassica napus.
- chemical : Fatty Acid Elongases, Molecular Structure, Mutagenesis, Site-Directed.

Abstract

To gain some insight whether there is an absolute requirement for the serine 282 to yield a functional fatty acid elongase 1 condensing enzyme we have introduced point mutations in the FAE1 coding sequence which led to the substitution of serine 282 with several aliphatic or aromatic amino acids. The mutated FAE1 polypeptides were expressed in yeast. Gas chromatography analyses of the fatty acid methyl esters from yeast lysates and fatty acid elongase activity assays demonstrated that there is not an absolute requirement for serine at position 282 to yield a functional FAE1 condensing enzyme.

DOI: 10.1016/S0014-5793(04)00198-X
PubMed: 15044011

Links to Exploration step

pubmed:15044011

Le document en format XML

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<author><name sortKey="Katavic, Vesna" sort="Katavic, Vesna" uniqKey="Katavic V" first="Vesna" last="Katavic">Vesna Katavic</name>
<affiliation><nlm:affiliation>CanAmera Foods/Bunge at Plant Biotechnology Institute, P.O. Box 479, 125 Willow Court, Osler, SK, Canada S0K 3A0. vesna.katavic@nrc.ca</nlm:affiliation>
</affiliation>
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<author><name sortKey="Barton, Dennis L" sort="Barton, Dennis L" uniqKey="Barton D" first="Dennis L" last="Barton">Dennis L. Barton</name>
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<author><name sortKey="Giblin, E Michael" sort="Giblin, E Michael" uniqKey="Giblin E" first="E Michael" last="Giblin">E Michael Giblin</name>
</author>
<author><name sortKey="Reed, Darwin W" sort="Reed, Darwin W" uniqKey="Reed D" first="Darwin W" last="Reed">Darwin W. Reed</name>
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<author><name sortKey="Kumar, Arvind" sort="Kumar, Arvind" uniqKey="Kumar A" first="Arvind" last="Kumar">Arvind Kumar</name>
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<author><name sortKey="Taylor, David C" sort="Taylor, David C" uniqKey="Taylor D" first="David C" last="Taylor">David C. Taylor</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Gaining insight into the role of serine 282 in B. napus FAE1 condensing enzyme.</title>
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<affiliation><nlm:affiliation>CanAmera Foods/Bunge at Plant Biotechnology Institute, P.O. Box 479, 125 Willow Court, Osler, SK, Canada S0K 3A0. vesna.katavic@nrc.ca</nlm:affiliation>
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<author><name sortKey="Barton, Dennis L" sort="Barton, Dennis L" uniqKey="Barton D" first="Dennis L" last="Barton">Dennis L. Barton</name>
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<author><name sortKey="Giblin, E Michael" sort="Giblin, E Michael" uniqKey="Giblin E" first="E Michael" last="Giblin">E Michael Giblin</name>
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<author><name sortKey="Reed, Darwin W" sort="Reed, Darwin W" uniqKey="Reed D" first="Darwin W" last="Reed">Darwin W. Reed</name>
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<author><name sortKey="Kumar, Arvind" sort="Kumar, Arvind" uniqKey="Kumar A" first="Arvind" last="Kumar">Arvind Kumar</name>
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<author><name sortKey="Taylor, David C" sort="Taylor, David C" uniqKey="Taylor D" first="David C" last="Taylor">David C. Taylor</name>
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<series><title level="j">FEBS letters</title>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Acetyltransferases (genetics)</term>
<term>Acetyltransferases (metabolism)</term>
<term>Amino Acids (chemistry)</term>
<term>Amino Acids (metabolism)</term>
<term>Brassica napus (enzymology)</term>
<term>Brassica napus (genetics)</term>
<term>Fatty Acid Elongases (MeSH)</term>
<term>Molecular Structure (MeSH)</term>
<term>Mutagenesis, Site-Directed (MeSH)</term>
<term>Plant Proteins (genetics)</term>
<term>Plant Proteins (metabolism)</term>
<term>Serine (metabolism)</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Amino Acids</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Acetyltransferases</term>
<term>Plant Proteins</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Acetyltransferases</term>
<term>Amino Acids</term>
<term>Plant Proteins</term>
<term>Serine</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Brassica napus</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Brassica napus</term>
</keywords>
<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Fatty Acid Elongases</term>
<term>Molecular Structure</term>
<term>Mutagenesis, Site-Directed</term>
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<front><div type="abstract" xml:lang="en">To gain some insight whether there is an absolute requirement for the serine 282 to yield a functional fatty acid elongase 1 condensing enzyme we have introduced point mutations in the FAE1 coding sequence which led to the substitution of serine 282 with several aliphatic or aromatic amino acids. The mutated FAE1 polypeptides were expressed in yeast. Gas chromatography analyses of the fatty acid methyl esters from yeast lysates and fatty acid elongase activity assays demonstrated that there is not an absolute requirement for serine at position 282 to yield a functional FAE1 condensing enzyme.</div>
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<DateRevised><Year>2019</Year>
<Month>12</Month>
<Day>10</Day>
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<Month>Mar</Month>
<Day>26</Day>
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<Title>FEBS letters</Title>
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<ArticleTitle>Gaining insight into the role of serine 282 in B. napus FAE1 condensing enzyme.</ArticleTitle>
<Pagination><MedlinePgn>118-24</MedlinePgn>
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<Abstract><AbstractText>To gain some insight whether there is an absolute requirement for the serine 282 to yield a functional fatty acid elongase 1 condensing enzyme we have introduced point mutations in the FAE1 coding sequence which led to the substitution of serine 282 with several aliphatic or aromatic amino acids. The mutated FAE1 polypeptides were expressed in yeast. Gas chromatography analyses of the fatty acid methyl esters from yeast lysates and fatty acid elongase activity assays demonstrated that there is not an absolute requirement for serine at position 282 to yield a functional FAE1 condensing enzyme.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Katavic</LastName>
<ForeName>Vesna</ForeName>
<Initials>V</Initials>
<AffiliationInfo><Affiliation>CanAmera Foods/Bunge at Plant Biotechnology Institute, P.O. Box 479, 125 Willow Court, Osler, SK, Canada S0K 3A0. vesna.katavic@nrc.ca</Affiliation>
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<Author ValidYN="Y"><LastName>Giblin</LastName>
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<Author ValidYN="Y"><LastName>Reed</LastName>
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<Author ValidYN="Y"><LastName>Kumar</LastName>
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<Author ValidYN="Y"><LastName>Taylor</LastName>
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<MeshHeading><DescriptorName UI="D029688" MajorTopicYN="N">Brassica napus</DescriptorName>
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<MeshHeading><DescriptorName UI="D015394" MajorTopicYN="N">Molecular Structure</DescriptorName>
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<MeshHeading><DescriptorName UI="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName>
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<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
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<MeshHeading><DescriptorName UI="D012694" MajorTopicYN="N">Serine</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
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Gaining insight into the role of serine 282 in B. napus FAE1 condensing enzyme.

Gaining insight into the role of serine 282 in B. napus FAE1 condensing enzyme.

Source :

English descriptors

Abstract

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki