Widiatningrum Talitha, Maeda Sorato, Kataoka Kunishige, Sakurai Takeshi
Graduate School of Natural Science and Technology, Kanazawa University, Kakuma, Kanazawa 920-1192, Japan.
Biochem Biophys Rep. 2015 Aug 7;3:144-149. doi: 10.1016/j.bbrep.2015.08.001. eCollection 2015 Sep.
A pirin-like protein from a marine denitrifying bacterium, Zobell has been heterologously expressed in and purified to homogeneity with metal-affinity and gel filtration chromatographies. The recombinant pirin-like protein has exhibited quercetinase activities upon the incorporation of a divalent metal ion, while its biological role remains unclear. In the case of Cu the holo-protein demonstrated the highest activities and spectroscopic properties typical of type II Cu protein. A 3D-structual model constructed using the crystal structure of human pirin as temperate indicated that the metal biding site is constructed with 3His1Glu located in the consensus sequences in the N-terminal domain.
来自海洋反硝化细菌的一种类匹啉蛋白已在佐贝尔（Zobell）中进行了异源表达，并通过金属亲和色谱和凝胶过滤色谱纯化至同质。重组类匹啉蛋白在掺入二价金属离子后表现出槲皮素酶活性，但其生物学作用仍不清楚。就铜而言，全蛋白表现出典型II型铜蛋白的最高活性和光谱特性。使用人匹啉的晶体结构作为模板构建的三维结构模型表明，金属结合位点由位于N端结构域共有序列中的3个组氨酸和1个谷氨酸构成。
