Nakata P A, Greene T W, Anderson J M, Smith-White B J, Okita T W, Preiss J
Program in Biochemistry and Biophysics, Washington State University, Pullman 99164-6340.
Plant Mol Biol. 1991 Nov;17(5):1089-93. doi: 10.1007/BF00037149.
Near-full-length cDNA clones to the small and large subunit of the heterotetrameric potato tuber ADP-glucose pyrophosphorylase have been isolated and characterized. The missing amino terminal sequence of the small subunit has also been elucidated from its corresponding genomic clone. Primary sequence comparisons revealed that each potato subunit had less identity to each other than to their homologous subunit from other plants. It also appeared that the smaller subunit is more conserved among the different plants and the larger subunit more divergent. Amino acid comparisons of both potato tuber sequences to the Escherichia coli ADP-glucose pyrophosphorylase sequence revealed conserved regions important for both catalytic and allosteric function of the bacterial enzyme.
已分离并鉴定了异源四聚体马铃薯块茎 ADP - 葡萄糖焦磷酸化酶小亚基和大亚基的近全长 cDNA 克隆。小亚基缺失的氨基末端序列也已从其相应的基因组克隆中阐明。一级序列比较显示，与来自其他植物的同源亚基相比，每个马铃薯亚基之间的同源性更低。还发现较小的亚基在不同植物中更保守，而较大的亚基差异更大。将两个马铃薯块茎序列与大肠杆菌 ADP - 葡萄糖焦磷酸化酶序列进行氨基酸比较，揭示了对细菌酶的催化和别构功能都很重要的保守区域。
