Defined dimensional changes in enzyme cofactors: fluorescent "stretched-out" analogs of adenine nucleotides.
Science, 1977/1/21;195(4275):296-8.
Scopes DI, Barrio JR, Leonard NJ
PMID: 188137
Impact factor: 63.714
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.
MeSH terms
Adenine Nucleotides; Adenosine Diphosphate; Adenosine Triphosphate; Animals; Binding Sites; Catalysis; Chemical Phenomena; Chemistry; Coenzymes; Hexokinase; In Vitro Techniques; Phosphofructokinase-1; Phosphoglycerate Kinase; Phosphotransferases; Polyribonucleotide Nucleotidyltransferase; Protein Binding; Pyruvate Kinase; Rabbits; Saccharomyces cerevisiae; Spectrometry, Fluorescence; Structure-Activity Relationship
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