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
Hauptverfasser: Zamolodchikova, Tatyana S., Sokolova, Elena A., Lu, Deshun, Sadler, J.Evan
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.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(00)01092-9