AustralieFrV1, PascalFrancis, Corpus, bibRecord, 006234

Biochemical characterization of the Chlamydomonas reinhardtii α-1,4 glucanotransferase supports a direct function in amylopectin biosynthesis

Identifieur interne : 006234 ( PascalFrancis/Corpus ); précédent : 006233; suivant : 006235

Biochemical characterization of the Chlamydomonas reinhardtii α-1,4 glucanotransferase supports a direct function in amylopectin biosynthesis

Auteurs : C. Colleoni ; D. Dauvillee ; G. Mouille ; M. Morell ; M. Samuel ; M.-C. Slomiany ; L. Lienard ; F. Wattebled ; C. D'Hulst ; S. Ball

Source :

Plant physiology : (Bethesda) [ 0032-0889 ] ; 1999.

RBID : Pascal:99-0458902

Descripteurs français

Pascal (Inist)
- Caractérisation, Biosynthèse, Transferases, Variant génétique, Déficit fonctionnel, Chlamydomonas reinhardtii, Amylopectine, Amidon, α-1,4 glucanotransferase.

English descriptors

KwdEn :
- Amylopectin, Biosynthesis, Characterization, Chlamydomonas reinhardtii, Functional deficit, Genetic variant, Starch, Transferases.

Abstract

Plant α-1,4 glucanotransferases (disproportionating enzymes, or D-enzymes) transfer glucan chains among oligosaccharides with the concomitant release of glucose (Glc). Analysis of Chlamydomonas reinhardtii sta11-1 mutants revealed a correlation between a D-enzyme deficiency and specific alterations in amylopectin structure and starch biosynthesis, thereby suggesting previously unknown biosynthetic functions. This study characterized the biochemical activities of the α-1,4 glucanotransferase that is deficient in sta11-1 mutants. The enzyme exhibited the glucan transfer and Glc production activities that define D-enzymes. D-enzyme also transferred glucans among the outer chains of amylopectin (using the polysaccharide chains as both donor and acceptor) and from malto-oligosaccharides into the outer chains of either amylopectin or glycogen. In contrast to transfer among oligosaccharides, which occurs readily with maltotriose, transfer into polysaccharide required longer donor molecules. All three enzymatic activities, evolution of Glc from oligosaccharides, glucan transfer from oligosaccharides into polysaccharides, and transfer among polysaccharide outer chains, were evident in a single 62-kD band. Absence of all three activities co-segregated with the sta11-1 mutation, which is known to cause abnormal accumulation of oligosaccharides at the expense of starch. To explain these data we propose that D-enzymes function directly in building the amylopectin structure.

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

A01	`01`	`1`		`@0 0032-0889`
A02	`01`			`@0 PPHYA5`
A03		`1`		`@0 Plant physiol. : (Bethesda)`
A05				`@2 120`
A06				`@2 4`
A08	`01`	`1`	`ENG`	`@1 Biochemical characterization of the Chlamydomonas reinhardtii α-1,4 glucanotransferase supports a direct function in amylopectin biosynthesis`
A11	`01`	`1`		`@1 COLLEONI (C.)`
A11	`02`	`1`		`@1 DAUVILLEE (D.)`
A11	`03`	`1`		`@1 MOUILLE (G.)`
A11	`04`	`1`		`@1 MORELL (M.)`
A11	`05`	`1`		`@1 SAMUEL (M.)`
A11	`06`	`1`		`@1 SLOMIANY (M.-C.)`
A11	`07`	`1`		`@1 LIENARD (L.)`
A11	`08`	`1`		`@1 WATTEBLED (F.)`
A11	`09`	`1`		`@1 D'HULST (C.)`
A11	`10`	`1`		`@1 BALL (S.)`
A14	`01`			`@1 Laboratoire de Chimie Biologique, Unité Mixte de Recherche du Centre National de la Recherche Scientifique no. 8576, Université des Sciences et Technologies de Lille @2 59655 Villeneuve d'Ascq @3 FRA @Z 1 aut. @Z 2 aut. @Z 3 aut. @Z 6 aut. @Z 7 aut. @Z 8 aut. @Z 9 aut. @Z 10 aut.`
A14	`02`			`@1 Commonwealth Scientific and Industrial Research Organization, Division of Plant Industry, G.P.O. Box 1600 @2 Canberra, Australian Capital Territory 2601 @3 AUS @Z 4 aut. @Z 5 aut.`
A20				`@1 1005-1013`
A21				`@1 1999`
A23	`01`			`@0 ENG`
A43	`01`			`@1 INIST @2 3000 @5 354000089453480080`
A44				`@0 0000 @1 © 1999 INIST-CNRS. All rights reserved.`
A45				`@0 24 ref.`
A47	`01`	`1`		`@0 99-0458902`
A60				`@1 P`
A61				`@0 A`
A64	`01`	`1`		`@0 Plant physiology : (Bethesda)`
A66	`01`			`@0 USA`
C01	`01`		`ENG`	@0 Plant α-1,4 glucanotransferases (disproportionating enzymes, or D-enzymes) transfer glucan chains among oligosaccharides with the concomitant release of glucose (Glc). Analysis of Chlamydomonas reinhardtii sta11-1 mutants revealed a correlation between a D-enzyme deficiency and specific alterations in amylopectin structure and starch biosynthesis, thereby suggesting previously unknown biosynthetic functions. This study characterized the biochemical activities of the α-1,4 glucanotransferase that is deficient in sta11-1 mutants. The enzyme exhibited the glucan transfer and Glc production activities that define D-enzymes. D-enzyme also transferred glucans among the outer chains of amylopectin (using the polysaccharide chains as both donor and acceptor) and from malto-oligosaccharides into the outer chains of either amylopectin or glycogen. In contrast to transfer among oligosaccharides, which occurs readily with maltotriose, transfer into polysaccharide required longer donor molecules. All three enzymatic activities, evolution of Glc from oligosaccharides, glucan transfer from oligosaccharides into polysaccharides, and transfer among polysaccharide outer chains, were evident in a single 62-kD band. Absence of all three activities co-segregated with the sta11-1 mutation, which is known to cause abnormal accumulation of oligosaccharides at the expense of starch. To explain these data we propose that D-enzymes function directly in building the amylopectin structure.
C02	`01`	`X`		`@0 002A10E02`
C03	`01`	`X`	`FRE`	`@0 Caractérisation @5 01`
C03	`01`	`X`	`ENG`	`@0 Characterization @5 01`
C03	`01`	`X`	`SPA`	`@0 Caracterización @5 01`
C03	`02`	`X`	`FRE`	`@0 Biosynthèse @5 02`
C03	`02`	`X`	`ENG`	`@0 Biosynthesis @5 02`
C03	`02`	`X`	`SPA`	`@0 Biosíntesis @5 02`
C03	`03`	`X`	`FRE`	`@0 Transferases @2 FE @5 03`
C03	`03`	`X`	`ENG`	`@0 Transferases @2 FE @5 03`
C03	`03`	`X`	`SPA`	`@0 Transferases @2 FE @5 03`
C03	`04`	`X`	`FRE`	`@0 Variant génétique @5 04`
C03	`04`	`X`	`ENG`	`@0 Genetic variant @5 04`
C03	`04`	`X`	`SPA`	`@0 Variante genética @5 04`
C03	`05`	`X`	`FRE`	`@0 Déficit fonctionnel @5 05`
C03	`05`	`X`	`ENG`	`@0 Functional deficit @5 05`
C03	`05`	`X`	`SPA`	`@0 Deficiencia funcional @5 05`
C03	`06`	`X`	`FRE`	`@0 Chlamydomonas reinhardtii @2 NS @5 10`
C03	`06`	`X`	`ENG`	`@0 Chlamydomonas reinhardtii @2 NS @5 10`
C03	`06`	`X`	`SPA`	`@0 Chlamydomonas reinhardtii @2 NS @5 10`
C03	`07`	`X`	`FRE`	`@0 Amylopectine @5 15`
C03	`07`	`X`	`ENG`	`@0 Amylopectin @5 15`
C03	`07`	`X`	`SPA`	`@0 Amilopectina @5 15`
C03	`08`	`X`	`FRE`	`@0 Amidon @5 16`
C03	`08`	`X`	`ENG`	`@0 Starch @5 16`
C03	`08`	`X`	`SPA`	`@0 Almidón @5 16`
C03	`09`	`X`	`FRE`	`@0 α-1,4 glucanotransferase @2 FE @4 INC @5 68`
C07	`01`	`X`	`FRE`	`@0 Enzyme`
C07	`01`	`X`	`ENG`	`@0 Enzyme`
C07	`01`	`X`	`SPA`	`@0 Enzima`
C07	`02`	`X`	`FRE`	`@0 Chlorophyceae @2 NS`
C07	`02`	`X`	`ENG`	`@0 Chlorophyceae @2 NS`
C07	`02`	`X`	`SPA`	`@0 Chlorophyceae @2 NS`
C07	`03`	`X`	`FRE`	`@0 Chlorophyta @2 NS`
C07	`03`	`X`	`ENG`	`@0 Chlorophyta @2 NS`
C07	`03`	`X`	`SPA`	`@0 Chlorophyta @2 NS`
C07	`04`	`X`	`FRE`	`@0 Algae @2 NS`
C07	`04`	`X`	`ENG`	`@0 Algae @2 NS`
C07	`04`	`X`	`SPA`	`@0 Algae @2 NS`
C07	`05`	`X`	`FRE`	`@0 Thallophyta @2 NS`
C07	`05`	`X`	`ENG`	`@0 Thallophyta @2 NS`
C07	`05`	`X`	`SPA`	`@0 Thallophyta @2 NS`
N21				`@1 291`

Format Inist (serveur)

NO :	PASCAL 99-0458902 INIST
ET :	Biochemical characterization of the Chlamydomonas reinhardtii α-1,4 glucanotransferase supports a direct function in amylopectin biosynthesis
AU :	COLLEONI (C.); DAUVILLEE (D.); MOUILLE (G.); MORELL (M.); SAMUEL (M.); SLOMIANY (M.-C.); LIENARD (L.); WATTEBLED (F.); D'HULST (C.); BALL (S.)
AF :	Laboratoire de Chimie Biologique, Unité Mixte de Recherche du Centre National de la Recherche Scientifique no. 8576, Université des Sciences et Technologies de Lille/59655 Villeneuve d'Ascq/France (1 aut., 2 aut., 3 aut., 6 aut., 7 aut., 8 aut., 9 aut., 10 aut.); Commonwealth Scientific and Industrial Research Organization, Division of Plant Industry, G.P.O. Box 1600/Canberra, Australian Capital Territory 2601/Australie (4 aut., 5 aut.)
DT :	Publication en série; Niveau analytique
SO :	Plant physiology : (Bethesda); ISSN 0032-0889; Coden PPHYA5; Etats-Unis; Da. 1999; Vol. 120; No. 4; Pp. 1005-1013; Bibl. 24 ref.
LA :	Anglais
EA :	Plant α-1,4 glucanotransferases (disproportionating enzymes, or D-enzymes) transfer glucan chains among oligosaccharides with the concomitant release of glucose (Glc). Analysis of Chlamydomonas reinhardtii sta11-1 mutants revealed a correlation between a D-enzyme deficiency and specific alterations in amylopectin structure and starch biosynthesis, thereby suggesting previously unknown biosynthetic functions. This study characterized the biochemical activities of the α-1,4 glucanotransferase that is deficient in sta11-1 mutants. The enzyme exhibited the glucan transfer and Glc production activities that define D-enzymes. D-enzyme also transferred glucans among the outer chains of amylopectin (using the polysaccharide chains as both donor and acceptor) and from malto-oligosaccharides into the outer chains of either amylopectin or glycogen. In contrast to transfer among oligosaccharides, which occurs readily with maltotriose, transfer into polysaccharide required longer donor molecules. All three enzymatic activities, evolution of Glc from oligosaccharides, glucan transfer from oligosaccharides into polysaccharides, and transfer among polysaccharide outer chains, were evident in a single 62-kD band. Absence of all three activities co-segregated with the sta11-1 mutation, which is known to cause abnormal accumulation of oligosaccharides at the expense of starch. To explain these data we propose that D-enzymes function directly in building the amylopectin structure.
CC :	002A10E02
FD :	Caractérisation; Biosynthèse; Transferases; Variant génétique; Déficit fonctionnel; Chlamydomonas reinhardtii; Amylopectine; Amidon; α-1,4 glucanotransferase
FG :	Enzyme; Chlorophyceae; Chlorophyta; Algae; Thallophyta
ED :	Characterization; Biosynthesis; Transferases; Genetic variant; Functional deficit; Chlamydomonas reinhardtii; Amylopectin; Starch
EG :	Enzyme; Chlorophyceae; Chlorophyta; Algae; Thallophyta
SD :	Caracterización; Biosíntesis; Transferases; Variante genética; Deficiencia funcional; Chlamydomonas reinhardtii; Amilopectina; Almidón
LO :	INIST-3000.354000089453480080
ID :	99-0458902

Links to Exploration step

Pascal:99-0458902

Le document en format XML

<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en" level="a">Biochemical characterization of the Chlamydomonas reinhardtii α-1,4 glucanotransferase supports a direct function in amylopectin biosynthesis</title>
<author><name sortKey="Colleoni, C" sort="Colleoni, C" uniqKey="Colleoni C" first="C." last="Colleoni">C. Colleoni</name>
<affiliation><inist:fA14 i1="01"><s1>Laboratoire de Chimie Biologique, Unité Mixte de Recherche du Centre National de la Recherche Scientifique no. 8576, Université des Sciences et Technologies de Lille</s1>
<s2>59655 Villeneuve d'Ascq</s2>
<s3>FRA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>6 aut.</sZ>
<sZ>7 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
<sZ>10 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="Dauvillee, D" sort="Dauvillee, D" uniqKey="Dauvillee D" first="D." last="Dauvillee">D. Dauvillee</name>
<affiliation><inist:fA14 i1="01"><s1>Laboratoire de Chimie Biologique, Unité Mixte de Recherche du Centre National de la Recherche Scientifique no. 8576, Université des Sciences et Technologies de Lille</s1>
<s2>59655 Villeneuve d'Ascq</s2>
<s3>FRA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>6 aut.</sZ>
<sZ>7 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
<sZ>10 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="Mouille, G" sort="Mouille, G" uniqKey="Mouille G" first="G." last="Mouille">G. Mouille</name>
<affiliation><inist:fA14 i1="01"><s1>Laboratoire de Chimie Biologique, Unité Mixte de Recherche du Centre National de la Recherche Scientifique no. 8576, Université des Sciences et Technologies de Lille</s1>
<s2>59655 Villeneuve d'Ascq</s2>
<s3>FRA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>6 aut.</sZ>
<sZ>7 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
<sZ>10 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="Morell, M" sort="Morell, M" uniqKey="Morell M" first="M." last="Morell">M. Morell</name>
<affiliation><inist:fA14 i1="02"><s1>Commonwealth Scientific and Industrial Research Organization, Division of Plant Industry, G.P.O. Box 1600</s1>
<s2>Canberra, Australian Capital Territory 2601</s2>
<s3>AUS</s3>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="Samuel, M" sort="Samuel, M" uniqKey="Samuel M" first="M." last="Samuel">M. Samuel</name>
<affiliation><inist:fA14 i1="02"><s1>Commonwealth Scientific and Industrial Research Organization, Division of Plant Industry, G.P.O. Box 1600</s1>
<s2>Canberra, Australian Capital Territory 2601</s2>
<s3>AUS</s3>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="Slomiany, M C" sort="Slomiany, M C" uniqKey="Slomiany M" first="M.-C." last="Slomiany">M.-C. Slomiany</name>
<affiliation><inist:fA14 i1="01"><s1>Laboratoire de Chimie Biologique, Unité Mixte de Recherche du Centre National de la Recherche Scientifique no. 8576, Université des Sciences et Technologies de Lille</s1>
<s2>59655 Villeneuve d'Ascq</s2>
<s3>FRA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>6 aut.</sZ>
<sZ>7 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
<sZ>10 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="Lienard, L" sort="Lienard, L" uniqKey="Lienard L" first="L." last="Lienard">L. Lienard</name>
<affiliation><inist:fA14 i1="01"><s1>Laboratoire de Chimie Biologique, Unité Mixte de Recherche du Centre National de la Recherche Scientifique no. 8576, Université des Sciences et Technologies de Lille</s1>
<s2>59655 Villeneuve d'Ascq</s2>
<s3>FRA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>6 aut.</sZ>
<sZ>7 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
<sZ>10 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="Wattebled, F" sort="Wattebled, F" uniqKey="Wattebled F" first="F." last="Wattebled">F. Wattebled</name>
<affiliation><inist:fA14 i1="01"><s1>Laboratoire de Chimie Biologique, Unité Mixte de Recherche du Centre National de la Recherche Scientifique no. 8576, Université des Sciences et Technologies de Lille</s1>
<s2>59655 Villeneuve d'Ascq</s2>
<s3>FRA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>6 aut.</sZ>
<sZ>7 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
<sZ>10 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="D Hulst, C" sort="D Hulst, C" uniqKey="D Hulst C" first="C." last="D'Hulst">C. D'Hulst</name>
<affiliation><inist:fA14 i1="01"><s1>Laboratoire de Chimie Biologique, Unité Mixte de Recherche du Centre National de la Recherche Scientifique no. 8576, Université des Sciences et Technologies de Lille</s1>
<s2>59655 Villeneuve d'Ascq</s2>
<s3>FRA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>6 aut.</sZ>
<sZ>7 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
<sZ>10 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="Ball, S" sort="Ball, S" uniqKey="Ball S" first="S." last="Ball">S. Ball</name>
<affiliation><inist:fA14 i1="01"><s1>Laboratoire de Chimie Biologique, Unité Mixte de Recherche du Centre National de la Recherche Scientifique no. 8576, Université des Sciences et Technologies de Lille</s1>
<s2>59655 Villeneuve d'Ascq</s2>
<s3>FRA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>6 aut.</sZ>
<sZ>7 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
<sZ>10 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">INIST</idno>
<idno type="inist">99-0458902</idno>
<date when="1999">1999</date>
<idno type="stanalyst">PASCAL 99-0458902 INIST</idno>
<idno type="RBID">Pascal:99-0458902</idno>
<idno type="wicri:Area/PascalFrancis/Corpus">006234</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a">Biochemical characterization of the Chlamydomonas reinhardtii α-1,4 glucanotransferase supports a direct function in amylopectin biosynthesis</title>
<author><name sortKey="Colleoni, C" sort="Colleoni, C" uniqKey="Colleoni C" first="C." last="Colleoni">C. Colleoni</name>
<affiliation><inist:fA14 i1="01"><s1>Laboratoire de Chimie Biologique, Unité Mixte de Recherche du Centre National de la Recherche Scientifique no. 8576, Université des Sciences et Technologies de Lille</s1>
<s2>59655 Villeneuve d'Ascq</s2>
<s3>FRA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>6 aut.</sZ>
<sZ>7 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
<sZ>10 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="Dauvillee, D" sort="Dauvillee, D" uniqKey="Dauvillee D" first="D." last="Dauvillee">D. Dauvillee</name>
<affiliation><inist:fA14 i1="01"><s1>Laboratoire de Chimie Biologique, Unité Mixte de Recherche du Centre National de la Recherche Scientifique no. 8576, Université des Sciences et Technologies de Lille</s1>
<s2>59655 Villeneuve d'Ascq</s2>
<s3>FRA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>6 aut.</sZ>
<sZ>7 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
<sZ>10 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="Mouille, G" sort="Mouille, G" uniqKey="Mouille G" first="G." last="Mouille">G. Mouille</name>
<affiliation><inist:fA14 i1="01"><s1>Laboratoire de Chimie Biologique, Unité Mixte de Recherche du Centre National de la Recherche Scientifique no. 8576, Université des Sciences et Technologies de Lille</s1>
<s2>59655 Villeneuve d'Ascq</s2>
<s3>FRA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>6 aut.</sZ>
<sZ>7 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
<sZ>10 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="Morell, M" sort="Morell, M" uniqKey="Morell M" first="M." last="Morell">M. Morell</name>
<affiliation><inist:fA14 i1="02"><s1>Commonwealth Scientific and Industrial Research Organization, Division of Plant Industry, G.P.O. Box 1600</s1>
<s2>Canberra, Australian Capital Territory 2601</s2>
<s3>AUS</s3>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="Samuel, M" sort="Samuel, M" uniqKey="Samuel M" first="M." last="Samuel">M. Samuel</name>
<affiliation><inist:fA14 i1="02"><s1>Commonwealth Scientific and Industrial Research Organization, Division of Plant Industry, G.P.O. Box 1600</s1>
<s2>Canberra, Australian Capital Territory 2601</s2>
<s3>AUS</s3>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="Slomiany, M C" sort="Slomiany, M C" uniqKey="Slomiany M" first="M.-C." last="Slomiany">M.-C. Slomiany</name>
<affiliation><inist:fA14 i1="01"><s1>Laboratoire de Chimie Biologique, Unité Mixte de Recherche du Centre National de la Recherche Scientifique no. 8576, Université des Sciences et Technologies de Lille</s1>
<s2>59655 Villeneuve d'Ascq</s2>
<s3>FRA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>6 aut.</sZ>
<sZ>7 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
<sZ>10 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="Lienard, L" sort="Lienard, L" uniqKey="Lienard L" first="L." last="Lienard">L. Lienard</name>
<affiliation><inist:fA14 i1="01"><s1>Laboratoire de Chimie Biologique, Unité Mixte de Recherche du Centre National de la Recherche Scientifique no. 8576, Université des Sciences et Technologies de Lille</s1>
<s2>59655 Villeneuve d'Ascq</s2>
<s3>FRA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>6 aut.</sZ>
<sZ>7 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
<sZ>10 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="Wattebled, F" sort="Wattebled, F" uniqKey="Wattebled F" first="F." last="Wattebled">F. Wattebled</name>
<affiliation><inist:fA14 i1="01"><s1>Laboratoire de Chimie Biologique, Unité Mixte de Recherche du Centre National de la Recherche Scientifique no. 8576, Université des Sciences et Technologies de Lille</s1>
<s2>59655 Villeneuve d'Ascq</s2>
<s3>FRA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>6 aut.</sZ>
<sZ>7 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
<sZ>10 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="D Hulst, C" sort="D Hulst, C" uniqKey="D Hulst C" first="C." last="D'Hulst">C. D'Hulst</name>
<affiliation><inist:fA14 i1="01"><s1>Laboratoire de Chimie Biologique, Unité Mixte de Recherche du Centre National de la Recherche Scientifique no. 8576, Université des Sciences et Technologies de Lille</s1>
<s2>59655 Villeneuve d'Ascq</s2>
<s3>FRA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>6 aut.</sZ>
<sZ>7 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
<sZ>10 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
<author><name sortKey="Ball, S" sort="Ball, S" uniqKey="Ball S" first="S." last="Ball">S. Ball</name>
<affiliation><inist:fA14 i1="01"><s1>Laboratoire de Chimie Biologique, Unité Mixte de Recherche du Centre National de la Recherche Scientifique no. 8576, Université des Sciences et Technologies de Lille</s1>
<s2>59655 Villeneuve d'Ascq</s2>
<s3>FRA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>6 aut.</sZ>
<sZ>7 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
<sZ>10 aut.</sZ>
</inist:fA14>
</affiliation>
</author>
</analytic>
<series><title level="j" type="main">Plant physiology : (Bethesda)</title>
<title level="j" type="abbreviated">Plant physiol. : (Bethesda)</title>
<idno type="ISSN">0032-0889</idno>
<imprint><date when="1999">1999</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
<seriesStmt><title level="j" type="main">Plant physiology : (Bethesda)</title>
<title level="j" type="abbreviated">Plant physiol. : (Bethesda)</title>
<idno type="ISSN">0032-0889</idno>
</seriesStmt>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amylopectin</term>
<term>Biosynthesis</term>
<term>Characterization</term>
<term>Chlamydomonas reinhardtii</term>
<term>Functional deficit</term>
<term>Genetic variant</term>
<term>Starch</term>
<term>Transferases</term>
</keywords>
<keywords scheme="Pascal" xml:lang="fr"><term>Caractérisation</term>
<term>Biosynthèse</term>
<term>Transferases</term>
<term>Variant génétique</term>
<term>Déficit fonctionnel</term>
<term>Chlamydomonas reinhardtii</term>
<term>Amylopectine</term>
<term>Amidon</term>
<term>α-1,4 glucanotransferase</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Plant α-1,4 glucanotransferases (disproportionating enzymes, or D-enzymes) transfer glucan chains among oligosaccharides with the concomitant release of glucose (Glc). Analysis of Chlamydomonas reinhardtii sta11-1 mutants revealed a correlation between a D-enzyme deficiency and specific alterations in amylopectin structure and starch biosynthesis, thereby suggesting previously unknown biosynthetic functions. This study characterized the biochemical activities of the α-1,4 glucanotransferase that is deficient in sta11-1 mutants. The enzyme exhibited the glucan transfer and Glc production activities that define D-enzymes. D-enzyme also transferred glucans among the outer chains of amylopectin (using the polysaccharide chains as both donor and acceptor) and from malto-oligosaccharides into the outer chains of either amylopectin or glycogen. In contrast to transfer among oligosaccharides, which occurs readily with maltotriose, transfer into polysaccharide required longer donor molecules. All three enzymatic activities, evolution of Glc from oligosaccharides, glucan transfer from oligosaccharides into polysaccharides, and transfer among polysaccharide outer chains, were evident in a single 62-kD band. Absence of all three activities co-segregated with the sta11-1 mutation, which is known to cause abnormal accumulation of oligosaccharides at the expense of starch. To explain these data we propose that D-enzymes function directly in building the amylopectin structure.</div>
</front>
</TEI>
<inist><standard h6="B"><pA><fA01 i1="01" i2="1"><s0>0032-0889</s0>
</fA01>
<fA02 i1="01"><s0>PPHYA5</s0>
</fA02>
<fA03 i2="1"><s0>Plant physiol. : (Bethesda)</s0>
</fA03>
<fA05><s2>120</s2>
</fA05>
<fA06><s2>4</s2>
</fA06>
<fA08 i1="01" i2="1" l="ENG"><s1>Biochemical characterization of the Chlamydomonas reinhardtii α-1,4 glucanotransferase supports a direct function in amylopectin biosynthesis</s1>
</fA08>
<fA11 i1="01" i2="1"><s1>COLLEONI (C.)</s1>
</fA11>
<fA11 i1="02" i2="1"><s1>DAUVILLEE (D.)</s1>
</fA11>
<fA11 i1="03" i2="1"><s1>MOUILLE (G.)</s1>
</fA11>
<fA11 i1="04" i2="1"><s1>MORELL (M.)</s1>
</fA11>
<fA11 i1="05" i2="1"><s1>SAMUEL (M.)</s1>
</fA11>
<fA11 i1="06" i2="1"><s1>SLOMIANY (M.-C.)</s1>
</fA11>
<fA11 i1="07" i2="1"><s1>LIENARD (L.)</s1>
</fA11>
<fA11 i1="08" i2="1"><s1>WATTEBLED (F.)</s1>
</fA11>
<fA11 i1="09" i2="1"><s1>D'HULST (C.)</s1>
</fA11>
<fA11 i1="10" i2="1"><s1>BALL (S.)</s1>
</fA11>
<fA14 i1="01"><s1>Laboratoire de Chimie Biologique, Unité Mixte de Recherche du Centre National de la Recherche Scientifique no. 8576, Université des Sciences et Technologies de Lille</s1>
<s2>59655 Villeneuve d'Ascq</s2>
<s3>FRA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>6 aut.</sZ>
<sZ>7 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
<sZ>10 aut.</sZ>
</fA14>
<fA14 i1="02"><s1>Commonwealth Scientific and Industrial Research Organization, Division of Plant Industry, G.P.O. Box 1600</s1>
<s2>Canberra, Australian Capital Territory 2601</s2>
<s3>AUS</s3>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
</fA14>
<fA20><s1>1005-1013</s1>
</fA20>
<fA21><s1>1999</s1>
</fA21>
<fA23 i1="01"><s0>ENG</s0>
</fA23>
<fA43 i1="01"><s1>INIST</s1>
<s2>3000</s2>
<s5>354000089453480080</s5>
</fA43>
<fA44><s0>0000</s0>
<s1>© 1999 INIST-CNRS. All rights reserved.</s1>
</fA44>
<fA45><s0>24 ref.</s0>
</fA45>
<fA47 i1="01" i2="1"><s0>99-0458902</s0>
</fA47>
<fA60><s1>P</s1>
</fA60>
<fA61><s0>A</s0>
</fA61>
<fA64 i1="01" i2="1"><s0>Plant physiology : (Bethesda)</s0>
</fA64>
<fA66 i1="01"><s0>USA</s0>
</fA66>
<fC01 i1="01" l="ENG"><s0>Plant α-1,4 glucanotransferases (disproportionating enzymes, or D-enzymes) transfer glucan chains among oligosaccharides with the concomitant release of glucose (Glc). Analysis of Chlamydomonas reinhardtii sta11-1 mutants revealed a correlation between a D-enzyme deficiency and specific alterations in amylopectin structure and starch biosynthesis, thereby suggesting previously unknown biosynthetic functions. This study characterized the biochemical activities of the α-1,4 glucanotransferase that is deficient in sta11-1 mutants. The enzyme exhibited the glucan transfer and Glc production activities that define D-enzymes. D-enzyme also transferred glucans among the outer chains of amylopectin (using the polysaccharide chains as both donor and acceptor) and from malto-oligosaccharides into the outer chains of either amylopectin or glycogen. In contrast to transfer among oligosaccharides, which occurs readily with maltotriose, transfer into polysaccharide required longer donor molecules. All three enzymatic activities, evolution of Glc from oligosaccharides, glucan transfer from oligosaccharides into polysaccharides, and transfer among polysaccharide outer chains, were evident in a single 62-kD band. Absence of all three activities co-segregated with the sta11-1 mutation, which is known to cause abnormal accumulation of oligosaccharides at the expense of starch. To explain these data we propose that D-enzymes function directly in building the amylopectin structure.</s0>
</fC01>
<fC02 i1="01" i2="X"><s0>002A10E02</s0>
</fC02>
<fC03 i1="01" i2="X" l="FRE"><s0>Caractérisation</s0>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="ENG"><s0>Characterization</s0>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="SPA"><s0>Caracterización</s0>
<s5>01</s5>
</fC03>
<fC03 i1="02" i2="X" l="FRE"><s0>Biosynthèse</s0>
<s5>02</s5>
</fC03>
<fC03 i1="02" i2="X" l="ENG"><s0>Biosynthesis</s0>
<s5>02</s5>
</fC03>
<fC03 i1="02" i2="X" l="SPA"><s0>Biosíntesis</s0>
<s5>02</s5>
</fC03>
<fC03 i1="03" i2="X" l="FRE"><s0>Transferases</s0>
<s2>FE</s2>
<s5>03</s5>
</fC03>
<fC03 i1="03" i2="X" l="ENG"><s0>Transferases</s0>
<s2>FE</s2>
<s5>03</s5>
</fC03>
<fC03 i1="03" i2="X" l="SPA"><s0>Transferases</s0>
<s2>FE</s2>
<s5>03</s5>
</fC03>
<fC03 i1="04" i2="X" l="FRE"><s0>Variant génétique</s0>
<s5>04</s5>
</fC03>
<fC03 i1="04" i2="X" l="ENG"><s0>Genetic variant</s0>
<s5>04</s5>
</fC03>
<fC03 i1="04" i2="X" l="SPA"><s0>Variante genética</s0>
<s5>04</s5>
</fC03>
<fC03 i1="05" i2="X" l="FRE"><s0>Déficit fonctionnel</s0>
<s5>05</s5>
</fC03>
<fC03 i1="05" i2="X" l="ENG"><s0>Functional deficit</s0>
<s5>05</s5>
</fC03>
<fC03 i1="05" i2="X" l="SPA"><s0>Deficiencia funcional</s0>
<s5>05</s5>
</fC03>
<fC03 i1="06" i2="X" l="FRE"><s0>Chlamydomonas reinhardtii</s0>
<s2>NS</s2>
<s5>10</s5>
</fC03>
<fC03 i1="06" i2="X" l="ENG"><s0>Chlamydomonas reinhardtii</s0>
<s2>NS</s2>
<s5>10</s5>
</fC03>
<fC03 i1="06" i2="X" l="SPA"><s0>Chlamydomonas reinhardtii</s0>
<s2>NS</s2>
<s5>10</s5>
</fC03>
<fC03 i1="07" i2="X" l="FRE"><s0>Amylopectine</s0>
<s5>15</s5>
</fC03>
<fC03 i1="07" i2="X" l="ENG"><s0>Amylopectin</s0>
<s5>15</s5>
</fC03>
<fC03 i1="07" i2="X" l="SPA"><s0>Amilopectina</s0>
<s5>15</s5>
</fC03>
<fC03 i1="08" i2="X" l="FRE"><s0>Amidon</s0>
<s5>16</s5>
</fC03>
<fC03 i1="08" i2="X" l="ENG"><s0>Starch</s0>
<s5>16</s5>
</fC03>
<fC03 i1="08" i2="X" l="SPA"><s0>Almidón</s0>
<s5>16</s5>
</fC03>
<fC03 i1="09" i2="X" l="FRE"><s0>α-1,4 glucanotransferase</s0>
<s2>FE</s2>
<s4>INC</s4>
<s5>68</s5>
</fC03>
<fC07 i1="01" i2="X" l="FRE"><s0>Enzyme</s0>
</fC07>
<fC07 i1="01" i2="X" l="ENG"><s0>Enzyme</s0>
</fC07>
<fC07 i1="01" i2="X" l="SPA"><s0>Enzima</s0>
</fC07>
<fC07 i1="02" i2="X" l="FRE"><s0>Chlorophyceae</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="02" i2="X" l="ENG"><s0>Chlorophyceae</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="02" i2="X" l="SPA"><s0>Chlorophyceae</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="03" i2="X" l="FRE"><s0>Chlorophyta</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="03" i2="X" l="ENG"><s0>Chlorophyta</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="03" i2="X" l="SPA"><s0>Chlorophyta</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="04" i2="X" l="FRE"><s0>Algae</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="04" i2="X" l="ENG"><s0>Algae</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="04" i2="X" l="SPA"><s0>Algae</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="05" i2="X" l="FRE"><s0>Thallophyta</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="05" i2="X" l="ENG"><s0>Thallophyta</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="05" i2="X" l="SPA"><s0>Thallophyta</s0>
<s2>NS</s2>
</fC07>
<fN21><s1>291</s1>
</fN21>
</pA>
</standard>
<server><NO>PASCAL 99-0458902 INIST</NO>
<ET>Biochemical characterization of the Chlamydomonas reinhardtii α-1,4 glucanotransferase supports a direct function in amylopectin biosynthesis</ET>
<AU>COLLEONI (C.); DAUVILLEE (D.); MOUILLE (G.); MORELL (M.); SAMUEL (M.); SLOMIANY (M.-C.); LIENARD (L.); WATTEBLED (F.); D'HULST (C.); BALL (S.)</AU>
<AF>Laboratoire de Chimie Biologique, Unité Mixte de Recherche du Centre National de la Recherche Scientifique no. 8576, Université des Sciences et Technologies de Lille/59655 Villeneuve d'Ascq/France (1 aut., 2 aut., 3 aut., 6 aut., 7 aut., 8 aut., 9 aut., 10 aut.); Commonwealth Scientific and Industrial Research Organization, Division of Plant Industry, G.P.O. Box 1600/Canberra, Australian Capital Territory 2601/Australie (4 aut., 5 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>Plant physiology : (Bethesda); ISSN 0032-0889; Coden PPHYA5; Etats-Unis; Da. 1999; Vol. 120; No. 4; Pp. 1005-1013; Bibl. 24 ref.</SO>
<LA>Anglais</LA>
<EA>Plant α-1,4 glucanotransferases (disproportionating enzymes, or D-enzymes) transfer glucan chains among oligosaccharides with the concomitant release of glucose (Glc). Analysis of Chlamydomonas reinhardtii sta11-1 mutants revealed a correlation between a D-enzyme deficiency and specific alterations in amylopectin structure and starch biosynthesis, thereby suggesting previously unknown biosynthetic functions. This study characterized the biochemical activities of the α-1,4 glucanotransferase that is deficient in sta11-1 mutants. The enzyme exhibited the glucan transfer and Glc production activities that define D-enzymes. D-enzyme also transferred glucans among the outer chains of amylopectin (using the polysaccharide chains as both donor and acceptor) and from malto-oligosaccharides into the outer chains of either amylopectin or glycogen. In contrast to transfer among oligosaccharides, which occurs readily with maltotriose, transfer into polysaccharide required longer donor molecules. All three enzymatic activities, evolution of Glc from oligosaccharides, glucan transfer from oligosaccharides into polysaccharides, and transfer among polysaccharide outer chains, were evident in a single 62-kD band. Absence of all three activities co-segregated with the sta11-1 mutation, which is known to cause abnormal accumulation of oligosaccharides at the expense of starch. To explain these data we propose that D-enzymes function directly in building the amylopectin structure.</EA>
<CC>002A10E02</CC>
<FD>Caractérisation; Biosynthèse; Transferases; Variant génétique; Déficit fonctionnel; Chlamydomonas reinhardtii; Amylopectine; Amidon; α-1,4 glucanotransferase</FD>
<FG>Enzyme; Chlorophyceae; Chlorophyta; Algae; Thallophyta</FG>
<ED>Characterization; Biosynthesis; Transferases; Genetic variant; Functional deficit; Chlamydomonas reinhardtii; Amylopectin; Starch</ED>
<EG>Enzyme; Chlorophyceae; Chlorophyta; Algae; Thallophyta</EG>
<SD>Caracterización; Biosíntesis; Transferases; Variante genética; Deficiencia funcional; Chlamydomonas reinhardtii; Amilopectina; Almidón</SD>
<LO>INIST-3000.354000089453480080</LO>
<ID>99-0458902</ID>
</server>
</inist>
</record>

Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Wicri/Asie/explor/AustralieFrV1/Data/PascalFrancis/Corpus

HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 006234 | SxmlIndent | more

HfdSelect -h $EXPLOR_AREA/Data/PascalFrancis/Corpus/biblio.hfd -nk 006234 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Wicri/Asie
   |area=    AustralieFrV1
   |flux=    PascalFrancis
   |étape=   Corpus
   |type=    RBID
   |clé=     Pascal:99-0458902
   |texte=   Biochemical characterization of the Chlamydomonas reinhardtii α-1,4 glucanotransferase supports a direct function in amylopectin biosynthesis
}}

This area was generated with Dilib version V0.6.33.
Data generation: Tue Dec 5 10:43:12 2017. Site generation: Tue Mar 5 14:07:20 2024

	Serveur d'exploration sur les relations entre la France et l'Australie
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.

Serveur d'exploration sur les relations entre la France et l'Australie

Biochemical characterization of the Chlamydomonas reinhardtii α-1,4 glucanotransferase supports a direct function in amylopectin biosynthesis

Biochemical characterization of the Chlamydomonas reinhardtii α-1,4 glucanotransferase supports a direct function in amylopectin biosynthesis

Source :

Descripteurs français

English descriptors

Abstract

Notice en format standard (ISO 2709)

Format Inist (serveur)

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