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The FASEB Journal, Vol 11, 217-226, Copyright © 1997 by The Federation of American Societies for Experimental Biology

REVIEWS

Chemical arrows for enzymatic targets

RF Colman
Department of Chemistry and Biochemistry, University of Delaware, Newark 19716, USA.

Reactive analogs of substrates or allosteric regulators can be designed to bind reversibly to particular ligand sites of enzymes. Subsequently, these compounds can react covalently with amino acids accessible from the ligand site, thereby functioning as chemical arrows aimed at specific enzymatic target sites. The approach of affinity labeling can be used to identify amino acid participants in active or regulatory sites, to provide a rational choice of targets for site-directed mutagenesis experiments, or to monitor conformational changes in the region of a particular enzyme site. Illustrations of these approaches include: 1) the use of reactive nucleotide analogs directed to substrate sites in adenylosuccinate synthetase and adenylosuccinate lyase and to regulatory sites of glutamate dehydrogenase, 2) the use of affinity cleavage by Fe2(+)-isocitrate to locate the metal-substrate site of isocitrate dehydrogenase, and 3) the use of reactive peptides and aromatic compounds to target the glutathione and xenobiotic sites of glutathione S-transferases.


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Copyright © 1997 by The Federation of American Societies for Experimental Biology.