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- W2382149420 abstract "An important goal of many biochemists is the identification of amino acids within the active and allosteric sites of enzymes and the elucidation of the role of those amino acids. One approach is to modify chemically 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. This is the strategy termed affinity labeling, which can potentially lead to specific but irreversible attack within purified enzymes, or even of particular enzymes when present in a mixture of proteins. In the case of dehydrogenases and kinases, custom designed purine nucleotide analogues which have reactive functional groups located at key positions of the natural structure can be effective in mapping amino acid residues in different subsites of the nucleotide binding regions (1)." @default.
- W2382149420 created "2016-06-24" @default.
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- W2382149420 date "1987-01-01" @default.
- W2382149420 modified "2023-09-24" @default.
- W2382149420 title "PURINE NUCLEOTIDE SITES IN DEHYDROGENASES" @default.
- W2382149420 hasPublicationYear "1987" @default.
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