1. Defined dimensional changes in enzyme cofactors: fluorescent "stretched-out" analogs of adenine nucleotides.
- Author
-
Scopes DI, Barrio JR, and Leonard NJ
- Subjects
- Adenosine Diphosphate analogs & derivatives, Adenosine Triphosphate analogs & derivatives, Animals, Binding Sites, Catalysis, Chemical Phenomena, Chemistry, Hexokinase metabolism, In Vitro Techniques, Phosphofructokinase-1 metabolism, Phosphoglycerate Kinase metabolism, Phosphotransferases metabolism, Polyribonucleotide Nucleotidyltransferase metabolism, Protein Binding, Pyruvate Kinase metabolism, Rabbits, Saccharomyces cerevisiae, Spectrometry, Fluorescence, Structure-Activity Relationship, Adenine Nucleotides metabolism, Coenzymes metabolism
- Abstract
A concept is presented for testing the dimensional restrictions of enzyme-active sites by stretching the substrate or cofactor by known magnitude. These restrictions of enzyme-active sites specific for purine cofactors were tested by the synthesis and evaluation of lin-benzoadenosine 5'-triphosphate, 5'-diphosphate, and 3',5'-monophosphate with respect to enzyme binding and activity. These "stretchedout" (by 2.4 angstroms) versions of the adenine ribonucleotides bind strongly, slow the enzymatic rates, and have useful fluorescence properties.
- Published
- 1977
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