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, 466 (2-3), 295-9

Activation of Recombinant Proenteropeptidase by Duodenase

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Activation of Recombinant Proenteropeptidase by Duodenase

T S Zamolodchikova et al. FEBS Lett.

Abstract

Duodenase, a serine proteinase from bovine Brunner's (duodenal) glands that was predicted to be a natural activator of enteropeptidase zymogen, cleaves and activates recombinant single-chain bovine proenteropeptidase (kcat/Km = 2700 M(-1) s(-1)). The measured rate of proenteropeptidase cleavage by duodenase was about 70-fold lower compared with the rate of trypsin-mediated cleavage of the zymogen. The role of duodenase is supposed to be the primary activator of proenteropeptidase maintaining a certain level of active enteropeptidase in the duodenum. A new scheme of proteolytic activation cascade of digestive proteases is discussed.

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