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Science 4 March 1977:
Vol. 195. no. 4281, pp. 884 - 886
DOI: 10.1126/science.190679
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Articles

Science, Vol 195, Issue 4281, 884-886
Copyright © 1977 by American Association for the Advancement of Science

articles

Arginyl residues: anion recognition sites in enzymes

JF Riordan, KD McElvany, and CL Borders Jr

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.


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