Activation of recombinant proenteropeptidase by duodenase

FEBS Lett. 2000 Jan 28;466(2-3):295-9. doi: 10.1016/s0014-5793(00)01092-9.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cattle
  • Electrophoresis, Polyacrylamide Gel
  • Enteropeptidase / chemistry
  • Enteropeptidase / metabolism*
  • Enzyme Activation
  • Enzyme Precursors / chemistry
  • Enzyme Precursors / metabolism*
  • Molecular Sequence Data
  • Recombinant Proteins / metabolism
  • Serine Endopeptidases / metabolism*

Substances

  • Enzyme Precursors
  • Recombinant Proteins
  • Serine Endopeptidases
  • duodenase
  • Enteropeptidase