Triose phosphate isomerase from the blood fluke Schistosoma mansoni Biochemical characterisation of a potential drug and vaccine target

Veronika L Zinsser, Edward Farnell, David W Dunne, David J Timson

Research output: Contribution to journalArticlepeer-review

17 Citations (Scopus)

Abstract

The glycolytic enzyme triose phosphate isomerase from Schistosoma mansoni is a potential target for drugs and vaccines. Molecular modelling of the enzyme predicted that a Ser-Ala-Asp motif which is believed to be a helminth-specific epitope is exposed. The enzyme is dimeric (as judged by gel filtration and cross-linking), resistant to proteolysis and highly stable to thermal denaturation (melting temperature of 82.0°C). The steady-state kinetic parameters are high (Km for dihydroxyacetone phosphate is 0.51mM; Km for glyceraldehyde 3-phosphate is 1.1mM; kcat for dihydroxyacetone phosphate is 7800s(-1) and kcat for glyceraldehyde 3-phosphate is 6.9s(-1)).
Original languageEnglish
Pages (from-to)3422–3427
JournalFEBS Letters
Volume587
Issue number21
Early online date23 Sep 2013
DOIs
Publication statusPublished - 01 Nov 2013

Bibliographical note

Copyright © 2013. Published by Elsevier B.V.

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

Fingerprint

Dive into the research topics of 'Triose phosphate isomerase from the blood fluke <em>Schistosoma mansoni </em><i>Biochemical characterisation of a potential drug and vaccine target</i>'. Together they form a unique fingerprint.

Cite this