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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Danzin C,Casara Pdoi
10.1016/0014-5793(84)81172-2subject
Has Abstractpub_date
1984-09-03 00:00:00pages
275-8issue
2eissn
0014-5793issn
1873-3468pii
0014-5793(84)81172-2journal_volume
174pub_type
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