Abstract
AMINO-ACID analogues have proved very useful in numerous investigations involving micro-organisms1. Among these applications is the technique of inhibition analysis whereby one makes a structural comparison of related molecules that competitively inhibit the growth of micro-organisms in order to derive information about the nature of an enzyme-substrate complex2. Thus, the conclusion has been reached that the (β-and ε-carbons must lie in a trans-like conformation when lysine is complexed to the enzyme surface3. The terminal and β-methylene groups of methionine were reported to be cis-like to each other in the enzyme–substrate complex4. The steric and spatial relationships of the ring carbons to the (β-carbon position of the alanine side-chain of certain analogues seemingly determ ine whether the phenylalanine or the leucine enzyme-substrate complex is mimicked5.
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ARONSON, J. Inhibition Analysis and Inhibitor-resistant Enzymes. Nature 198, 992–993 (1963). https://doi.org/10.1038/198992a0
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DOI: https://doi.org/10.1038/198992a0
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