1H, 13C, 15N backbone resonance assignment of Escherichia coli adenylate kinase.
1H, 13C, 15N backbone resonance assignment of Escherichia coli adenylate kinase.
复制标题
大肠杆菌腺苷酸激酶的 1H、13C、15N 主链共振分配。
DOI：
10.1007/s12104-023-10147-1
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发表时间：
2023
影响因子：
0.9
通讯作者：
Pielak,GaryJ
中科院分区：
文献类型：
--
作者：
Brom,JuliaA;Samsri,Sasiprapa;Petrikis,RutaG;Parnham,Stuart;Pielak,GaryJ
腺苷酸激酶可逆地催化ATP加AMP转化为两个ADP。这种必需的催化剂存在于每一个细胞中，大肠杆菌蛋白常被用作模型酶。我们的目标是使用E。大肠杆菌，以了解干蛋白质的结构和保护。本文报道了其C77S变体的表达、纯化、稳态分析、NMR条件和1H、13C、15N骨架共振NMR归属。这些数据也将帮助其他人利用这种原型酶。
Adenylate kinase reversibly catalyzes the conversion of ATP plus AMP to two ADPs. This essential catalyst is present in every cell, and theEscherichia coliprotein is often employed as a model enzyme. Our aim is to use theE. colienzyme to understand dry protein structure and protection. Here, we report the expression, purification, steady-state assay, NMR conditions and1H,13C,15N backbone resonance NMR assignments of its C77S variant. These data will also help others utilize this prototypical enzyme.