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

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 0.51 mM; Km for glyceraldehyde 3-phosphate is 1.1 mM; kcat for dihydroxyacetone phosphate is 7800 s-1 and kcat for glyceraldehyde 3-phosphate is 6.9 s-1).

Original languageEnglish
Pages (from-to)3422-3427
Number of pages6
JournalFebs Letters
Volume587
Issue number21
DOIs
Publication statusPublished - 1 Nov 2013

Keywords

  • Bilharzia
  • Blood fluke
  • Glycolytic enzyme
  • Schistosomiasis
  • Vaccine target

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