| Literature DB >> 6144574 |
J G Delcros, A M Roch, G Quash.
Abstract
The transglutaminase-mediated insertion of putrescine into casein was inhibited competitively by alpha-difluoromethylornithine (alpha-DFMO), an enzyme-activated irreversible inhibitor of ornithine decarboxylase. Preincubation of the amine acceptor (casein) or the enzyme itself with the inhibitor did not affect enzyme activity. Alpha-DFMO is a poorer substrate for transglutaminase (Km = 2.10 mM) than putrescine (Km = 0.17 mM). The inhibitory effect was also found with fibronectin as amine acceptor.Entities:
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Year: 1984 PMID： 6144574 DOI： 10.1016/0014-5793(84)80492-5
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124