Activation of recombinant proenteropeptidase by duodenase
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 d...
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Veröffentlicht in: | FEBS letters 2000-01, Vol.466 (2), p.295-299 |
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Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | 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. |
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ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/S0014-5793(00)01092-9 |