Denyer K, Waite D, Edwards A, Martin C, Smith A M
John Innes Centre, Norwich Research Park, Norwich, Norfolk NR4 7UH, U.K.
Biochem J. 1999 Sep 15;342 Pt 3(Pt 3):647-53.
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.
本文研究了淀粉合酶两种同工型的可溶形式的特性。其中一种,颗粒结合淀粉合酶I(GBSSI),在体内负责在淀粉颗粒的支链淀粉基质内合成直链淀粉。另一种,淀粉合酶II(SSII),参与支链淀粉的合成。两种同工型在体外都可以使用支链淀粉和麦芽寡糖作为底物。除了作为GBSSI的底物外,支链淀粉还作为该同工型的效应物,提高其延长麦芽寡糖的速率,并促进这些化合物以连续而非分布的方式延长。GBSSI对作为效应物的支链淀粉的亲和力大于其对作为底物的支链淀粉的亲和力。SSII对麦芽寡糖的延长速率和模式不受支链淀粉的影响。这些结果表明,与淀粉颗粒基质中的支链淀粉的特异性相互作用是GBSSI的独特特性,并且在确定其产物的性质方面至关重要。