Structure and mechanism of ATP-dependent proteases

Curr Opin Chem Biol. 1999 Oct;3(5):584-91. doi: 10.1016/s1367-5931(99)00013-7.

Abstract

A general paradigm for energy-dependent proteases is emerging: ATP may be used to unfold the substrate and translocate it through a narrow channel within the enzyme into a central proteolytic chamber. Different members of the family present intriguing elaborations on this model.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Adenosine Triphosphate*
  • Models, Molecular
  • Molecular Chaperones / metabolism
  • Serine Endopeptidases / chemistry
  • Serine Endopeptidases / metabolism*
  • Structure-Activity Relationship

Substances

  • Molecular Chaperones
  • Adenosine Triphosphate
  • Serine Endopeptidases