- Triose phosphate isomerase from the blood fluke Schistosoma mansoni: biochemical characterisation of a potential drug and vaccine target.
Triose phosphate isomerase from the blood fluke Schistosoma mansoni: biochemical characterisation of a potential drug and vaccine target.
FEBS letters (2013-09-28)
Veronika L Zinsser, Edward Farnell, David W Dunne, David J Timson
PMID24070897
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 6.9s(-1)).
MATERIALS
Product Number
Brand
Product Description
Sigma-Aldrich
Triosephosphate Isomerase from rabbit muscle, Type X, lyophilized powder, ≥3,500 units/mg protein
Sigma-Aldrich
Triosephosphate Isomerase from rabbit muscle, Type III-S, ammonium sulfate suspension, ≥4,000 units/mg protein
Sigma-Aldrich
Triosephosphate Isomerase from baker′s yeast (S. cerevisiae), Type I, ammonium sulfate suspension, ~10,000 units/mg protein