Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10871063 | FEBS Letters | 2013 | 6 Pages |
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 sâ1 and kcat for glyceraldehyde 3-phosphate is 6.9 sâ1).
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Authors
Veronika L. Zinsser, Edward Farnell, David W. Dunne, David J. Timson,