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  • Title: alpha-Allenyl putrescine, an enzyme-activated irreversible inhibitor of bacterial and mammalian ornithine decarboxylases.
    Author: Danzin C, Casara P.
    Journal: FEBS Lett; 1984 Sep 03; 174(2):275-8. PubMed ID: 6381100.
    Abstract:
    alpha-Allenyl putrescine (5,6-heptadiene-1,4-diamine) was designed as a new potential enzyme-activated irreversible inhibitor of ornithine decarboxylase (ODC). This compound, and more specifically its (R)-enantiomer, produced time-dependent inhibitions of E. coli and rat liver ODC. The inhibitions exhibit saturation kinetics and were not relieved by prolonged dialysis of the inactivated enzyme. Selective inactivation of the two types of ODC by the (R)-enantiomer is in agreement with the stereochemistry reported for ornithine decarboxylation by the enzyme. Kinetic constants of E. coli ODC inactivation by alpha-(R)-allenyl putrescine compare favorably with other irreversible inhibitors of this enzyme.
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