HOMEPRODUCTSCOMPANYCONTACTFAQResearchDictionaryPharmaSign Up FREE or Login

Identification of the reactive cysteine residues in oligopeptidase B from Trypanosoma brucei.

Abstract
Oligopeptidase B (OpdB) from Trypanosoma brucei is a candidate therapeutic target in African trypanosomiasis. OpdB is an atypical serine peptidase, since activity is inhibited by thiol-blocking reagents and enhanced by reducing agents. We have identified C256 as the reactive cysteine residue that mediates OpdB inhibition by N-ethylmaleimide and iodoacetic acid. Modeling studies suggest that C256 adducts occlude the P(1) substrate-binding site, preventing substrate binding. We further demonstrate that C559 and C597 are responsible for the thiol-enhancement of OpdB activity. These studies may facilitate the development of specific OpdB inhibitors with therapeutic potential, by exploiting these unique properties of this enzyme.
AuthorsRory E Morty, Angela Y Shih, Vilmos Fülöp, Norma W Andrews
JournalFEBS letters (FEBS Lett) Vol. 579 Issue 10 Pg. 2191-6 (Apr 11 2005) ISSN: 0014-5793 [Print] England
PMID15811340 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • DNA Primers
  • Serine Endopeptidases
  • oligopeptidase B
  • Cysteine
Topics
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cysteine (metabolism)
  • DNA Primers
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Sequence Homology, Amino Acid
  • Serine Endopeptidases (chemistry, genetics, metabolism)
  • Trypanosoma brucei brucei (enzymology)

Join CureHunter, for free Research Interface BASIC access!

Take advantage of free CureHunter research engine access to explore the best drug and treatment options for any disease. Find out why thousands of doctors, pharma researchers and patient activists around the world use CureHunter every day.
Realize the full power of the drug-disease research graph!


Choose Username:
Email:
Password:
Verify Password:
Enter Code Shown: