| Literature DB >> 190679 |
J F Riordan, K D McElvany, C L Borders.
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.Entities:
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Year: 1977 PMID: 190679 DOI: 10.1126/science.190679
Source DB: PubMed Journal: Science ISSN: 0036-8075 Impact factor: 47.728