Activation of recombinant proenteropeptidase by duodenase

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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 (k cat/K m=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.