Triose phosphate isomerase from the blood flukeSchistosoma mansoni: Biochemical characterisation of a potential drug and vaccine target
| Autor: | David J. Timson, David W. Dunne, Edward J. Farnell, Veronika L Zinsser |
|---|---|
| Rok vydání: | 2013 |
| Předmět: |
Models
Molecular Vaccine target Proteolysis 030231 tropical medicine Biophysics Glycolytic enzyme Blood fluke Bilharzia Glyceraldehyde 3-Phosphate Biochemistry Triosephosphate isomerase Epitopes 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Structural Biology Glyceraldehyde Genetics medicine Animals Humans Schistosomiasis Glycolysis Amino Acid Sequence Enzyme kinetics Molecular Biology 030304 developmental biology Dihydroxyacetone phosphate chemistry.chemical_classification 0303 health sciences medicine.diagnostic_test biology Schistosoma mansoni Cell Biology biology.organism_classification Molecular biology 3. Good health Kinetics Enzyme chemistry Dihydroxyacetone Phosphate Antigens Helminth Triose-Phosphate Isomerase |
| Zdroj: | FEBS Letters. 587:3422-3427 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/j.febslet.2013.09.022 |
| Popis: | 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)). |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text