A pathway for the interconversion of hexose and pentose in the parasitic amoeba Entamoeba histolytica
| Autor: | Richard E. Reeves, L G Warren, B M Susskind |
|---|---|
| Rok vydání: | 1982 |
| Předmět: |
Phosphofructokinase-1
Pentoses Transketolase Models Biological Biochemistry chemistry.chemical_compound Entamoeba histolytica Fructose-Bisphosphate Aldolase Animals Molecular Biology Hexoses Dihydroxyacetone phosphate biology Aldolase A Cell Biology biology.organism_classification Kinetics Glucose Sedoheptulose chemistry Erythrose biology.protein RNA Transaldolase Research Article Phosphofructokinase |
| Zdroj: | Biochemical Journal. 204:191-199 |
| ISSN: | 0264-6021 |
| DOI: | 10.1042/bj2040191 |
| Popis: | Isotope studies indicate that hexose-to-pentose interconversion by axenic Entamoeba histolytica conserves the C-1 and C-6 hexose carbon atoms. Transketolase was readily identified in amoebal extracts, and transaldolase could not be demonstrated. However, sedoheptulose 7-phosphate is a substrate for the PPi-dependent amoebal phosphofructokinase, and sedoheptulose 1,7-bisphosphate is cleaved by amoebal aldolase to dihydroxyacetone phosphate and erythrose phosphate. Since these three enzymes catalyse physiologically reversible reactions, a non-oxidative pathway for hexose-pentose interconversion exists in amoebae in the absence of transaldolase. By using known amoebal enzyme, the conversion of ribose into fructose was confirmed in vitro. Some kinetic parameters of amoebal phosphofructokinase, transketolase and aldolase were determined. |
| Databáze: | OpenAIRE |
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