scholarly journals Structural and Immunochemical Homologies between Foxtail Millet Glutelin 60 kDa and Starch Granule-bound Starch Synthase Proteins from Rice, Barley, Corn and Wheat Grains.

2000 ◽  
Vol 46 (2) ◽  
pp. 109-112 ◽  
Author(s):  
Kenji TAKUMI ◽  
Junko UDAKA ◽  
Masumi KIMOTO ◽  
Tetsuzo KOGA ◽  
Hideaki TSUJI
Keyword(s):  
Starch Granule ◽  
Foxtail Millet ◽  
Starch Synthase ◽  
Wheat Grains ◽  
Granule Bound Starch Synthase

scholarly journals Role of Granule-bound Starch Synthase in Determination of Amylopectin Structure and Starch Granule Morphology in Potato

2002 ◽  
Vol 277 (13) ◽  
pp. 10834-10841 ◽  
Author(s):  
Daniel C. Fulton ◽  
Anne Edwards ◽  
Emma Pilling ◽  
Helen L. Robinson ◽  
Brendan Fahy ◽  
...  
Keyword(s):  
Starch Granule ◽  
Starch Synthase ◽  
Granule Morphology ◽  
Amylopectin Structure ◽  
Granule Bound Starch Synthase

scholarly journals Interaction with amylopectin influences the ability of granule-bound starch synthase I to elongate malto-oligosaccharides

1999 ◽  
Vol 342 (3) ◽  
pp. 647-653 ◽  
Author(s):  
Kay DENYER ◽  
Darren WAITE ◽  
Anne EDWARDS ◽  
Cathie MARTIN ◽  
Alison M. SMITH
Keyword(s):  
Starch Granule ◽  
Specific Interaction ◽  
Unique Property ◽  
Starch Synthase ◽  
The Other ◽  
Soluble Form ◽  
The Matrix ◽  
Granule Bound Starch Synthase

This paper examines the properties in soluble form of two isoforms of starch synthase. One of these, granule-bound starch synthase I (GBSSI), is responsible for the synthesis of amylose inside the amylopectin matrix of the starch granule in vivo. The other, starch synthase II (SSII), is involved in amylopectin synthesis. Both isoforms can use amylopectin and malto-oligosaccharide as substrates in vitro. As well as acting as a substrate for GBSSI, amylopectin acts as an effector of this isoform, increasing the rate at which it elongates malto-oligosaccharides and promoting a processive rather than distributive mode of elongation of these compounds. The affinity of GBSSI for amylopectin as an effector is greater than its affinity for amylopectin as a substrate. The rate and mode of elongation of malto-oligosaccharides by SSII are not influenced by amylopectin. These results suggest that specific interaction with amylopectin in the matrix of the starch granule is a unique property of GBSSI and is critical in determining the nature of its products.

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