title: Arginyl residues: anion recognition sites in enzymes.
abstract: 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.
mesh_terms: D000249:Adenosine Monophosphate / Q000378:metabolism; D000494:Allosteric Regulation; D000838:Anions; D001120:Arginine / Q000378:metabolism*; D001665:Binding Sites; D005075:Biological Evolution; D002238:Carbohydrate Epimerases / Q000378:metabolism*; D002384:Catalysis; D003931:Diacetyl / Q000494:pharmacology; D006597:Fructose-Bisphosphatase / Q000037:antagonists & inhibitors / Q000378:metabolism; D005956:Glucose-6-Phosphate Isomerase / Q000037:antagonists & inhibitors; D006019:Glycolysis / Q000187:drug effects; D006593:Hexokinase / Q000037:antagonists & inhibitors; D010770:Phosphotransferases / Q000378:metabolism*; D013329:Structure-Activity Relationship; D014305:Triose-Phosphate Isomerase / Q000037:antagonists & inhibitors
chemical_list: D000838:Anions; D000249:Adenosine Monophosphate; D001120:Arginine; D010770:Phosphotransferases; D006593:Hexokinase; D006597:Fructose-Bisphosphatase; D002238:Carbohydrate Epimerases; D014305:Triose-Phosphate Isomerase; D005956:Glucose-6-Phosphate Isomerase; D003931:Diacetyl