Crystal structure of glutamine amidotransferase from Pyrococcus horikoshii OT3
Crystal structure of glutamine amidotransferase from Pyrococcus horikoshii OT3
复制标题
DOI：
10.2183/pjab.81.459
复制
发表时间：
2005-12-01
影响因子：
3.1
通讯作者：
Tanokura, M
中科院分区：
文献类型：
--
作者：
Maruoka, S;Lee, WC;Tanokura, M
谷氨酰胺酰胺转移酶（GATases）水解谷氨酰胺并产生氨。谷氨酰胺酰胺氮用于多种分子的生物合成，例如氨基酸、辅酶、抗生素、嘌呤和嘧啶核苷酸以及葡糖胺。在这里，我们确定了超嗜热古菌Pyrococcus horikoshii OT 3的GAT酶（PH 1346）的晶体结构，分辨率为1.89（A）。它的整体结构和活性部位与E. coli鸟苷5 '-单磷酸（GMP）合酶和硫磺硫化叶菌邻氨基苯甲酸合酶。
Glutamine amidotransferases (GATases) hydrolyze glutamine and generate ammonia. The glutamine amide nitrogen is utilized for the biosynthesis of a variety of molecules such as amino acids, coenzymes, antibiotics, purine and pyrimidine nucleotides, and glucosamine. Here, we determined the crystal structure of a GATase (PH1346) from the hyperthermophilic archaeon Pyrococcus horikoshii OT3 at 1.89 (A) over circle resolution. Its overall structure and active site are the most similar to those of E. coli guanosine 5'-monophosphate (GMP) synthase and Sulfolobus solfataricus anthranilate synthase, respectively.