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Granule-bound starch synthase I.

Authors :
Wattebled, Fabrice
Buléon, Alain
Bouchet, Brigitte
Ral, Jean-Philippe
Liénard, Luc
Delvallé, David
Binderup, Kim
Dauvillée, David
Ball, Steven
D'Hulst, Christophe
Source :
European Journal of Biochemistry; Aug2002, Vol. 269 Issue 15, p3810-3820, 11p
Publication Year :
2002

Abstract

Starch defines a semicrystalline polymer made of two different polysaccharide fractions. The A- and B-type crystalline lattices define the distinct structures reported in cereal and tuber starches, respectively. Amylopectin, the major fraction of starch, is thought to be chiefly responsible for this semicrystalline organization while amylose is generally considered as an amorphous polymer with little or no impact on the overall crystalline organization. STA2 represents a Chlamydomonas reinhardtii gene required for both amylose biosynthesis and the presence of significant granule-bound starch synthase I (GBSSI) activity. We show that this locus encodes a 69 kDa starch synthase and report the organization of the corresponding STA2 locus. This enzyme displays a specific activity an order of magnitude higher than those reported for most vascular plants. This property enables us to report a detailed characterization of amylose synthesis both in vivo and invitro . We show that GBSSI is capable of synthesizing a significant number of crystalline structures within starch. Quantifications of amount and type of crystals synthesized under these conditions show that GBSSI induces the formation of B-type crystals either in close association with pre-existing amorphous amylopectin or by crystallization of entirely de novo synthesized material. [ABSTRACT FROM AUTHOR]

Subjects

Subjects :
TRANSFERASES
STARCH

Details

Language :
English
ISSN :
00142956
Volume :
269
Issue :
15
Database :
Complementary Index
Journal :
European Journal of Biochemistry
Publication Type :
Academic Journal
Accession number :
7075046
Full Text :
https://doi.org/10.1046/j.1432-1033.2002.03072.x