Triose phosphate isomerase from the blood fluke Schistosoma mansoni: Biochemical characterisation of a potential drug and vaccine target |
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Authors: | Veronika L Zinsser Edward Farnell David W Dunne David J Timson |
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Institution: | 1. School of Biological Sciences, Queen’s University Belfast, Medical Biology Centre, 97 Lisburn Road, Belfast BT9 7BL, UK;2. Department of Pathology, University of Cambridge, Cambridge CB2 1QP, UK |
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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). |
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Keywords: | Schistosomiasis Bilharzia Blood fluke Vaccine target Glycolytic enzyme |
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