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PMID: 190679 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Arginyl residues: anion recognition sites in enzymes.

Science (New York, N.Y.) ·Vol. 195 ·No. 4281 ·1977-03-04 ·Pages 884-6

Riordan JF, McElvany KD, Borders CL

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
Adenosine Monophosphate/metabolism Allosteric Regulation Anions Arginine/metabolism Binding Sites Biological Evolution Carbohydrate Epimerases/metabolism Catalysis Diacetyl/pharmacology Fructose-Bisphosphatase/antagonists & inhibitors,metabolism Glucose-6-Phosphate Isomerase/antagonists & inhibitors Glycolysis/drug effects Hexokinase/antagonists & inhibitors Phosphotransferases/metabolism Structure-Activity Relationship Triose-Phosphate Isomerase/antagonists & inhibitors
Chemicals
Anions Adenosine Monophosphate Arginine Phosphotransferases Hexokinase Fructose-Bisphosphatase Carbohydrate Epimerases Triose-Phosphate Isomerase Glucose-6-Phosphate Isomerase Diacetyl
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Riordan J F
McElvany K D
Borders C L
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1977-03-04
Pages
884-6
Language
English
Region
United States
NLM ID
0404511
Subset
IM
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