Raffaelli N, Lorenzi T, Mariani P L, Emanuelli M, Amici A, Ruggieri S, Magni G
Istituto di Biochimica, Facoltà di Medicina, Università di Ancona, 60131 Ancona, Italy.
J Bacteriol. 1999 Sep;181(17):5509-11. doi: 10.1128/JB.181.17.5509-5511.1999.
The first identification and characterization of a catalytic activity associated with NadR protein is reported. A computer-aided search for sequence similarity revealed the presence in NadR of a 29-residue region highly conserved among known nicotinamide mononucleotide adenylyltransferases. The Escherichia coli nadR gene was cloned into a T7-based vector and overexpressed. In addition to functionally specific DNA binding properties, the homogeneous recombinant protein catalyzes NAD synthesis from nicotinamide mononucleotide and ATP.
本文报道了与NadR蛋白相关的催化活性的首次鉴定和表征。通过计算机辅助搜索序列相似性发现,NadR中存在一个29个残基的区域,在已知的烟酰胺单核苷酸腺苷酸转移酶中高度保守。将大肠杆菌nadR基因克隆到基于T7的载体中并进行过表达。除了具有功能特异性的DNA结合特性外,该均一的重组蛋白还催化从烟酰胺单核苷酸和ATP合成NAD。