Durmus A, Eicken C, Spener F, Krebs B
Anorganisch-Chemisches Institut, Universität Münster, Wilhelm-Klemm-Strasse 8, 48149, Münster, Germany.
Biochim Biophys Acta. 1999 Sep 14;1434(1):202-9. doi: 10.1016/s0167-4838(99)00176-4.
The sequence of cDNA fragments of two isozymes of the purple acid phosphatase from sweet potato (spPAP1 and spPAP2) has been determined by 5' and 3' rapid amplification of cDNA ends protocols using oligonucleotide primers based on amino acid information. The encoded amino acid sequences of these two isozymes show an equidistance of 72-77% not only to each other, but also to the primary structure of the purple acid phosphatase from red kidney bean (kbPAP). A three-dimensional model of the active site has been constructed for spPAP2 on the basis of the kbPAP crystallographic structure that helps to explain the reported differences in the visible and EPR spectra of spPAP2 and kbPAP.
利用基于氨基酸信息的寡核苷酸引物，通过5'和3' cDNA末端快速扩增方案，测定了甘薯紫色酸性磷酸酶两种同工酶（spPAP1和spPAP2）的cDNA片段序列。这两种同工酶的编码氨基酸序列不仅彼此之间显示出72 - 77%的等距离，而且与红芸豆紫色酸性磷酸酶（kbPAP）的一级结构也显示出72 - 77%的等距离。基于kbPAP晶体结构构建了spPAP2活性位点的三维模型，这有助于解释报道的spPAP2和kbPAP在可见光谱和电子顺磁共振光谱方面的差异。
