Purple Acid Phosphatase
Purple Acid Phosphatase
复制标题
DOI：
10.1002/9781119951438.eibc0582
复制
发表时间：
2006-04
期刊：
影响因子：
--
通讯作者：
A. Vogel;F. Spener;B. Krebs
中科院分区：
文献类型：
--
作者：
A. Vogel;F. Spener;B. Krebs
紫色酸性磷酸酶（PAP）水解活化的磷酸酯和酸酐，其共同点是具有负责颜色的酪氨酸-Fe（III）电荷转移跃迁的双金属中心。在来自脾脏、巨噬细胞、破骨细胞和子宫液的哺乳动物酶中，活性位点中的第二金属是Fe（II）;而植物酶菜豆PAP（kbPAP）具有Fe（III）-Zn（II）活性中心。同源二聚体111-kDa kbPAP的结构显示活性位点在两个夹心β-α-β-α-β基序的羧基末端。两个金属离子通过Asp 164单齿桥接。铁进一步由Tyr 167、His 325和Asp 135配位，锌由His 286、His 323和Asn 201配位。活性位点的结构是一致的建议的机制上的磷酸酯水解的亲核攻击的磷酸盐由Fe（III）-协调的氢氧根离子。蛋白质分离，生物学功能，序列，活性，哺乳动物和植物PAP的比较，以及这两种类型的功能方面进行了广泛的讨论。三维结构关键词：紫色酸性磷酸酶;抗酒石酸酸性磷酸酶;子宫铁蛋白;铁蛋白;锌蛋白; X射线结构
Purple acid phosphatases (PAPs) hydrolyzing activated phosphoric acid esters and anhydrides have in common a two-metal center with a tyrosine-Fe(III) charge transfer transition responsible for the color. In the mammalian enzymes from the spleen, macrophages, osteoclasts, and uterine fluids, the second metal in the active site is Fe(II); whereas, the plant enzyme kidney bean PAP (kbPAP) has an Fe(III)–Zn(II) active center. The structure of the homodimeric 111-kDa kbPAP shows the active site at the carboxy end of two sandwiched β–α–β–α–β motifs. The two metal ions are bridged monodentately by Asp164. The iron is further coordinated by Tyr167, His325, and Asp135, and the zinc by His286, His323, and Asn201. The active-site structure is consistent with proposals on the mechanism of phosphate ester hydrolysis by nucleophilic attack on the phosphate by an Fe(III)-coordinated hydroxide ion. Protein isolation, biological functions, sequences, activity, comparison of mammalian and plant PAPs, and the functional aspects of both types are discussed extensively. 3D Structure Keywords: purple acid phosphatase; tartrate-resistant acid phosphatase; uteroferrin; iron protein; zinc protein; X-ray structure