Riordan J F
Mol Cell Biochem. 1979 Jul 31;26(2):71-92. doi: 10.1007/BF00232886.
The functions of a number of amino acid residues in proteins have been studied by chemical modification techniques and much useful information has been obtained. Methods using dicarbonyl compounds for the modification of arginine residues are the most recent to have been developed. Since their introduction about 10 years ago, they have led to the identification of a large number of enzymes and other proteins that contain arginine residues critical to biological function. These reagents are discussed in terms of their chemical reactivity and mechanisms of action and in relation to the unique chemical properties of the guanidinium group. Butanedione, phenylglyoxal and cyclohexanedione are the most commonly employed arginyl reagents, and their relative advantages are examined. A survey of the functional role of arginine residues in enzymes and other proteins is presented in which nearly 100 examples are cited. The prediction that arginine residues would be found to serve a general role as anionic binding sites in protein has obviously been validated. The genetic and physiological implications of the selection of arginine for this important function are discussed.
通过化学修饰技术对蛋白质中一些氨基酸残基的功能进行了研究，并获得了许多有用的信息。使用二羰基化合物修饰精氨酸残基的方法是最近才开发出来的。自从大约10年前引入这些方法以来，它们已促使人们鉴定出大量含有对生物功能至关重要的精氨酸残基的酶和其他蛋白质。从这些试剂的化学反应性和作用机制以及与胍基独特化学性质的关系方面对它们进行了讨论。丁二酮、苯乙二醛和环己二酮是最常用的精氨酰试剂，并对它们的相对优势进行了研究。本文对酶和其他蛋白质中精氨酸残基的功能作用进行了综述，其中引用了近100个例子。关于精氨酸残基在蛋白质中作为阴离子结合位点发挥普遍作用的预测显然已得到验证。讨论了选择精氨酸执行这一重要功能的遗传学和生理学意义。
