Biochemical characterization of the Chlamydomonas reinhardtii α-1,4 glucanotransferase supports a direct function in amylopectin biosynthesis
Identifieur interne : 006E20 ( PascalFrancis/Curation ); précédent : 006E19; suivant : 006E21Biochemical characterization of the Chlamydomonas reinhardtii α-1,4 glucanotransferase supports a direct function in amylopectin biosynthesis
Auteurs : C. Colleoni [France] ; D. Dauvillee [France] ; G. Mouille [France] ; M. Morell [Australie] ; M. Samuel [Australie] ; M.-C. Slomiany [France] ; L. Lienard [France] ; F. Wattebled [France] ; C. D'Hulst [France] ; S. Ball [France]Source :
- Plant physiology : (Bethesda) [ 0032-0889 ] ; 1999.
Descripteurs français
- Pascal (Inist)
- Wicri :
- topic : Amidon.
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- KwdEn :
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.
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<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>
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<fA61><s0>A</s0>
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<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>
</inist>
</record>
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