Expression of sweetpotato ADP-glucose pyrophosphorylase in E. coli BL21(DE3) lacking the glgC gene with a coexpression vector
ADP-glucose pyrophosphorylase (AGPase) plays an important role in the plant starch biosynthesis. Plant AGPase is a heterotetrameric enzyme composed of two a-subunits and two p-subunits encoded by different genes,and several isoforms are known to exist in each subunit. In sweetpotato (cv. Koganesengan),there are two kinds of oc-subunit isoforms,ibAGPal and ibAGPa2,which show an organspecific expression at the tuberous roots and leaves. In order to compare the properties between the two kinds of oc-subunit isoforms of sweetpotato,homotetrameric enzymes composed of each ot-subunit a-lone,and also heterotetrameric enzymes composed of both oc-subunit and β-subunit were expressed using E. coli BL21(DE3) lacking the glgC gene with a coexpression vector. The recombinant AGPase enzymes were characterized. It was found that little difference in the properties was recognized between AGPases having the respective a-subunits. Therefore, the respective a-subunit isoforms of sweetpotato confer the similar effect on the whole AGPase property,suggesting that the βsubunit isoforms would primarily affect the properties of the organspecific AGPases.
sweetpotato starch synthesis ADP-glucose pyrophosphorylase coexpression system
Kanefumi Kitahara Shunsuke Matsuo Kiyotaka Fujita Toshihiko Suganuma
Department of Biochemical Science and Technology,Faculty of Agriculture,Kagoshima University, 1-21-24 Korimoto, Kagoshima 890-0065,Japan
国际会议
徐州
英文
199-202
2010-11-27（万方平台首次上网日期，不代表论文的发表时间）