PoplarV1, Main, Exploration, bibRecord, 004963

4-Coumarate:coenzyme A ligase in hybrid poplar. Properties of native enzymes, cDNA cloning, and analysis of recombinant enzymes.

Identifieur interne : 004963 ( Main/Exploration ); précédent : 004962; suivant : 004964

4-Coumarate:coenzyme A ligase in hybrid poplar. Properties of native enzymes, cDNA cloning, and analysis of recombinant enzymes.

Auteurs : S M Allina [Canada] ; A. Pri-Hadash ; D A Theilmann ; B E Ellis ; C J Douglas

Source :

Plant physiology [ 0032-0889 ] ; 1998.

RBID : pubmed:9489021

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Chromatography, Liquid (MeSH), Cloning, Molecular (MeSH), Coenzyme A Ligases (genetics), Coenzyme A Ligases (isolation & purification), Coenzyme A Ligases (metabolism), Coumaric Acids (metabolism), DNA, Complementary (MeSH), Gene Expression Regulation, Developmental (MeSH), Gene Expression Regulation, Plant (MeSH), Isoenzymes (genetics), Isoenzymes (isolation & purification), Isoenzymes (metabolism), Molecular Sequence Data (MeSH), Recombinant Proteins (genetics), Recombinant Proteins (isolation & purification), Recombinant Proteins (metabolism), Sequence Homology, Amino Acid (MeSH), Trees (enzymology).
MESH :
- chemical , genetics : Coenzyme A Ligases, Isoenzymes, Recombinant Proteins.
- chemical , isolation & purification : Coenzyme A Ligases, Isoenzymes, Recombinant Proteins.
- chemical , metabolism : Coenzyme A Ligases, Coumaric Acids, Isoenzymes, Recombinant Proteins.
- enzymology : Trees.
- Amino Acid Sequence, Chromatography, Liquid, Cloning, Molecular, DNA, Complementary, Gene Expression Regulation, Developmental, Gene Expression Regulation, Plant, Molecular Sequence Data, Sequence Homology, Amino Acid.

Abstract

The enzyme 4-coumarate:coenzyme A ligase (4CL) is important in providing activated thioester substrates for phenylpropanoid natural product biosynthesis. We tested different hybrid poplar (Populus trichocarpa x Populus deltoides) tissues for the presence of 4CL isoforms by fast-protein liquid chromatography and detected a minimum of three 4CL isoforms. These isoforms shared similar hydroxycinnamic acid substrate-utilization profiles and were all inactive against sinapic acid, but instability of the native forms precluded extensive further analysis. 4CL cDNA clones were isolated and grouped into two major classes, the predicted amino acid sequences of which were 86% identical. Genomic Southern blots showed that the cDNA classes represent two poplar 4CL genes, and northern blots provided evidence for their differential expression. Recombinant enzymes corresponding to the two genes were expressed using a baculovirus system. The two recombinant proteins had substrate utilization profiles similar to each other and to the native poplar 4CL isoforms (4-coumaric acid > ferulic acid > caffeic acid; there was no conversion of sinapic acid), except that both had relatively high activity toward cinnamic acid. These results are discussed with respect to the role of 4CL in the partitioning of carbon in phenylpropanoid metabolism.

DOI: 10.1104/pp.116.2.743
PubMed: 9489021
PubMed Central: PMC35134

Affiliations:

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Le document en format XML

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<term>Coenzyme A Ligases (isolation & purification)</term>
<term>Coenzyme A Ligases (metabolism)</term>
<term>Coumaric Acids (metabolism)</term>
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<term>Gene Expression Regulation, Plant (MeSH)</term>
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<term>Isoenzymes (isolation & purification)</term>
<term>Isoenzymes (metabolism)</term>
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<term>Recombinant Proteins (isolation & purification)</term>
<term>Recombinant Proteins (metabolism)</term>
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<term>Trees (enzymology)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>ADN complémentaire (MeSH)</term>
<term>Acides coumariques (métabolisme)</term>
<term>Arbres (enzymologie)</term>
<term>Chromatographie en phase liquide (MeSH)</term>
<term>Clonage moléculaire (MeSH)</term>
<term>Coenzyme A ligases (génétique)</term>
<term>Coenzyme A ligases (isolement et purification)</term>
<term>Coenzyme A ligases (métabolisme)</term>
<term>Données de séquences moléculaires (MeSH)</term>
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<term>Isoenzymes (isolement et purification)</term>
<term>Isoenzymes (métabolisme)</term>
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<term>Protéines recombinantes (isolement et purification)</term>
<term>Protéines recombinantes (métabolisme)</term>
<term>Régulation de l'expression des gènes au cours du développement (MeSH)</term>
<term>Régulation de l'expression des gènes végétaux (MeSH)</term>
<term>Similitude de séquences d'acides aminés (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
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<term>Isoenzymes</term>
<term>Recombinant Proteins</term>
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<term>Recombinant Proteins</term>
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<term>Isoenzymes</term>
<term>Protéines recombinantes</term>
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<term>Données de séquences moléculaires</term>
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<term>Régulation de l'expression des gènes végétaux</term>
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<front><div type="abstract" xml:lang="en">The enzyme 4-coumarate:coenzyme A ligase (4CL) is important in providing activated thioester substrates for phenylpropanoid natural product biosynthesis. We tested different hybrid poplar (Populus trichocarpa x Populus deltoides) tissues for the presence of 4CL isoforms by fast-protein liquid chromatography and detected a minimum of three 4CL isoforms. These isoforms shared similar hydroxycinnamic acid substrate-utilization profiles and were all inactive against sinapic acid, but instability of the native forms precluded extensive further analysis. 4CL cDNA clones were isolated and grouped into two major classes, the predicted amino acid sequences of which were 86% identical. Genomic Southern blots showed that the cDNA classes represent two poplar 4CL genes, and northern blots provided evidence for their differential expression. Recombinant enzymes corresponding to the two genes were expressed using a baculovirus system. The two recombinant proteins had substrate utilization profiles similar to each other and to the native poplar 4CL isoforms (4-coumaric acid > ferulic acid > caffeic acid; there was no conversion of sinapic acid), except that both had relatively high activity toward cinnamic acid. These results are discussed with respect to the role of 4CL in the partitioning of carbon in phenylpropanoid metabolism.</div>
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<Abstract><AbstractText>The enzyme 4-coumarate:coenzyme A ligase (4CL) is important in providing activated thioester substrates for phenylpropanoid natural product biosynthesis. We tested different hybrid poplar (Populus trichocarpa x Populus deltoides) tissues for the presence of 4CL isoforms by fast-protein liquid chromatography and detected a minimum of three 4CL isoforms. These isoforms shared similar hydroxycinnamic acid substrate-utilization profiles and were all inactive against sinapic acid, but instability of the native forms precluded extensive further analysis. 4CL cDNA clones were isolated and grouped into two major classes, the predicted amino acid sequences of which were 86% identical. Genomic Southern blots showed that the cDNA classes represent two poplar 4CL genes, and northern blots provided evidence for their differential expression. Recombinant enzymes corresponding to the two genes were expressed using a baculovirus system. The two recombinant proteins had substrate utilization profiles similar to each other and to the native poplar 4CL isoforms (4-coumaric acid > ferulic acid > caffeic acid; there was no conversion of sinapic acid), except that both had relatively high activity toward cinnamic acid. These results are discussed with respect to the role of 4CL in the partitioning of carbon in phenylpropanoid metabolism.</AbstractText>
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<affiliations><list><country><li>Canada</li>
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<region><li>Colombie-Britannique</li>
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<settlement><li>Vancouver</li>
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<orgName><li>Université de la Colombie-Britannique</li>
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<name sortKey="Pri Hadash, A" sort="Pri Hadash, A" uniqKey="Pri Hadash A" first="A" last="Pri-Hadash">A. Pri-Hadash</name>
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4-Coumarate:coenzyme A ligase in hybrid poplar. Properties of native enzymes, cDNA cloning, and analysis of recombinant enzymes.

4-Coumarate:coenzyme A ligase in hybrid poplar. Properties of native enzymes, cDNA cloning, and analysis of recombinant enzymes.

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