McLennan Alexander G
Structure. 2007 Aug;15(8):891-2. doi: 10.1016/j.str.2007.07.002.
In this issue of Structure, Amzel, Bessman, and colleagues (Gabelli et al., 2007) present the crystal structure of a 17 kDa Nudix hydrolase from Escherichia coli previously characterized as a dATPase and provide evidence that it functions in vivo to remove pyrophosphate from the folate precursor dihydroneopterin triphosphate.
在本期《结构》杂志中，阿姆泽尔、贝斯曼及其同事（加贝利等人，2007年）展示了来自大肠杆菌的一种17 kDa Nudix水解酶的晶体结构，该酶先前被鉴定为dATP酶，并提供证据表明它在体内发挥作用，从叶酸前体二氢新蝶呤三磷酸中去除焦磷酸。
