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Affinity Labeling of Nucleotide Binding Sites of Enzymes and Platelets

  • Roberta F. Colman
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 281)

Abstract

A goal of many biochemists is to identify and then to define the role of particular amino acids within the active and allosteric sites of enzymes. One approach is to chemically modify critical amino acids and to rely on the specificity of the enzyme for its substrate or normal regulatory compound to limit the extent of chemical modification to the region of the active or allosteric sites. In this approach, a reagent is designed which can react irreversibly with amino acid residues of the enzyme, but which is in addition stucturally analogous to the substrate. Such a compound may mimic the substrate in forming a reversible enzyme inhibitor complex at a particular site on the enzyme; the reactive functional group of the reagent may then form a covalent bond within the active site during the existence of this complex. This is the strategy termed affinity labeling, which can potentially lead to specific but irreversible attack within purified enzymes, or even of particular enzymes or receptors when present in a mixture of proteins.

Keywords

Glutamate Dehydrogenase Purine Nucleotide Nucleotide Analogue Allosteric Site cAMP Phosphodiesterase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1990

Authors and Affiliations

  • Roberta F. Colman
    • 1
  1. 1.Department of Chemistry and BiochemistryUniversity of DelawareNewarkUSA

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