α-二氟甲基鸟氨酸对组织转谷氨酰胺酶的竞争性抑制作用。
The competitive inhibition of tissue transglutaminase by alpha-difluoromethylornithine.
作者信息
Delcros J G, Roch A M, Quash G
出版信息
FEBS Lett. 1984 Jun 11;171(2):221-6. doi: 10.1016/0014-5793(84)80492-5.
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.
α-二氟甲基鸟氨酸（α-DFMO）是鸟氨酸脱羧酶的一种酶激活不可逆抑制剂，它能竞争性抑制转谷氨酰胺酶介导的腐胺插入酪蛋白的过程。将胺受体（酪蛋白）或酶本身与抑制剂预孵育不会影响酶活性。与腐胺（Km = 0.17 mM）相比，α-DFMO是转谷氨酰胺酶较差的底物（Km = 2.10 mM）。以纤连蛋白作为胺受体时也发现了这种抑制作用。
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