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PMID: 188137 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Defined dimensional changes in enzyme cofactors: fluorescent "stretched-out" analogs of adenine nucleotides.

Science (New York, N.Y.) ·Vol. 195 ·No. 4275 ·1977-01-21 ·Pages 296-8

Scopes DI, Barrio JR, Leonard NJ

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/metabolism Adenosine Diphosphate/analogs & derivatives Adenosine Triphosphate/analogs & derivatives Animals Binding Sites Catalysis Chemical Phenomena Chemistry Coenzymes/metabolism 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
Chemicals
Adenine Nucleotides Coenzymes Adenosine Diphosphate Adenosine Triphosphate Phosphotransferases Hexokinase Phosphofructokinase-1 Pyruvate Kinase Phosphoglycerate Kinase Polyribonucleotide Nucleotidyltransferase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Scopes D I
Barrio J R
Leonard N J
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1977-01-21
Pages
296-8
Language
English
Region
United States
NLM ID
0404511
Subset
IM
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