Association and dissociation of the tripeptidyl-peptidase II complex as a way of regulating the enzyme activity

Arch Biochem Biophys. 2000 Apr 15;376(2):275-80. doi: 10.1006/abbi.2000.1713.

Abstract

Tripeptidyl-peptidase II is an unusually large exopeptidase. The subunits (M(r) = 138,000) form an active complex with an M(r) > 10(6). This paper demonstrates that the complex can spontaneously dissociate in vitro into dimers which retain 110th of the original specific activity. The dissociated enzyme can reassociate at elevated temperatures, provided the protein concentration is sufficiently high. This reassociation was accompanied by a reactivation. The rate of reactivation was increased by the presence of competitive peptide inhibitors. It is speculated that association/dissociation may be a way of regulating the enzyme activity in vivo.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aminopeptidases
  • Animals
  • Binding, Competitive
  • Cell Line
  • Dimerization
  • Dipeptidyl-Peptidases and Tripeptidyl-Peptidases
  • Enzyme Activation / drug effects
  • Enzyme Stability
  • Freezing
  • Humans
  • Kinetics
  • Mice
  • Molecular Weight
  • Protein Binding
  • Protein Structure, Quaternary*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Serine Endopeptidases / chemistry*
  • Serine Endopeptidases / genetics
  • Serine Endopeptidases / isolation & purification
  • Serine Endopeptidases / metabolism*
  • Serine Proteinase Inhibitors / metabolism
  • Serine Proteinase Inhibitors / pharmacology
  • Substrate Specificity
  • Temperature

Substances

  • Recombinant Proteins
  • Serine Proteinase Inhibitors
  • Aminopeptidases
  • Dipeptidyl-Peptidases and Tripeptidyl-Peptidases
  • tripeptidyl-peptidase 2
  • Serine Endopeptidases