Substrate inhibition of cruzipain is not affected by the C-terminal domain

FEBS Lett. 1998 Jun 12;429(2):129-33. doi: 10.1016/s0014-5793(98)00532-8.


Endogenous and recombinant cruzipain, the major cysteine proteinase from the protozoan parasite Trypanosoma cruzi, exhibit differences in the protein and circular dichroism spectra probably attributed to the absence of the C-terminal domain in the recombinant enzyme. Substrate hydrolysis of both molecules at 25 degrees C and neutral pH obeyed Michaelis-Menten kinetics whereas significant substrate inhibition was observed above neutral pH. The results suggest that substrate inhibition of cruzipain is pH-dependent, and that the C-terminal domain does not play an essential role in this process.

Publication types

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

MeSH terms

  • Animals
  • Binding Sites
  • Circular Dichroism
  • Cysteine Endopeptidases / chemistry
  • Cysteine Endopeptidases / metabolism*
  • Cysteine Proteinase Inhibitors
  • Dose-Response Relationship, Drug
  • Hydrogen-Ion Concentration
  • Hydrolysis
  • Kinetics
  • Oligopeptides / metabolism
  • Protein Conformation
  • Protozoan Proteins
  • Recombinant Fusion Proteins / metabolism
  • Substrate Specificity
  • Trypanosoma cruzi / enzymology*


  • Cysteine Proteinase Inhibitors
  • Oligopeptides
  • Protozoan Proteins
  • Recombinant Fusion Proteins
  • Cysteine Endopeptidases
  • cruzipain