Inhibition of Aminopeptidase and Acetylcholinesterase by Puromycin and Puromycin Analogs

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Abstract
Puromycin analogs in which the O-methyl-L-tyrosine moiety was substituted by a number of amino acids were examined as inhibitors of the puromycin-sensitive rat brain aminopeptidase and bovine erythrocyte acetyl-cholinesterase. In the case of the aminopeptidase, the structure and stereochemistry of the amino acid substituent were important factors in determining inhibitor effectiveness. In the case of the acetylcholinesterase reaction, the aminonucleoside of puromycin was nearly as effective an inhibitor as puromycin itself, with little effect dependent on the nature or stereochemistry of the amino acid.