Brune M, Schumann R, Wittinghofer F
Nucleic Acids Res. 1985 Oct 11;13(19):7139-51. doi: 10.1093/nar/13.19.7139.
Adenylate kinase, the product of the adk locus in Escherichia coli K12, catalyzes the conversion of AMP and ATP to two molecules of ADP. The gene has been cloned by complementation of an adk temperature sensitive mutation. The DNA sequence of the complete coding region and of 5'- and 3'-untranslated regions were determined. The resulting protein sequence was found to contain several regions of high homology with cytosolic adenylate kinase of pig muscle (AK1), whose three-dimensional structure has been determined. The most significant of the amino acid exchanges is the replacement of histidine 36 with glutamine. This residue is believed to play a role in catalysis through metal ion binding. The codon usage pattern and the determination of adenylate kinase molecules per cell shows that the enzyme is one of the more abundant soluble proteins of the bacterial cells.
腺苷酸激酶是大肠杆菌K12中adk基因座的产物，催化AMP和ATP转化为两分子ADP。该基因已通过对adk温度敏感突变体的互补作用进行克隆。测定了完整编码区以及5'和3'非翻译区的DNA序列。结果发现所得蛋白质序列与猪肌肉胞质腺苷酸激酶（AK1）有几个高度同源的区域，其三维结构已确定。最显著的氨基酸交换是组氨酸36被谷氨酰胺取代。据信该残基通过金属离子结合在催化中起作用。密码子使用模式以及每个细胞中腺苷酸激酶分子的测定表明，该酶是细菌细胞中含量较为丰富的可溶性蛋白质之一。
