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Arginyl residues and anion binding sites in proteins

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Summary

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.

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  1. Biophysics Research Laboratory, Department of Biological Chemistry, Harvard Medical School, USA

    James F. Riordan

  2. Division of Medical Biology, Perer Bent Brigham Hospital Division, Affiliated Hospitals Center, Inc., 02115, Boston, Massachusetts, USA

    James F. Riordan

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This work was supported by Grant-in-Aid GM-15003 from the National Institutes of Health.

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Riordan, J.F. Arginyl residues and anion binding sites in proteins. Mol Cell Biochem 26, 71–92 (1979). https://doi.org/10.1007/BF00232886

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