Riordan J F, McElvany K D, Borders C L
Science. 1977 Mar 4;195(4281):884-6. doi: 10.1126/science.190679.
Chemical modification with 2,3-butanedione in borate buffer indicates that nine of ten glycolytic enzymes studied contain arginyl residues at their active sites. Fructose-1,6-diphosphatase also has arginines at its binding site for the allosteric inhibitor, adenosine monophosphate. These and other data suggest that, as a general rule, enzymes acting on anionic substrates or cofactors will probably contain arginyl residues as components of their ligand binding sites. This could account in part for the relatively infrequent occurrence of arginine in proteins.
在硼酸盐缓冲液中用2,3 - 丁二酮进行化学修饰表明，所研究的十种糖酵解酶中有九种在其活性位点含有精氨酰残基。果糖 - 1,6 - 二磷酸酶在其变构抑制剂单磷酸腺苷的结合位点也有精氨酸。这些以及其他数据表明，一般来说，作用于阴离子底物或辅因子的酶可能会含有精氨酰残基作为其配体结合位点的组成部分。这可能部分解释了精氨酸在蛋白质中相对较少出现的原因。
