Glucokinase and fructokinase of Trichomonas vaginalis and Tritrichomonas foetus
Autor: | Emmanuel Mertens, Miklø Müller |
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Rok vydání: | 1990 |
Předmět: |
chemistry.chemical_classification
Hexokinase Glucokinase Nucleotides Fructose Biology biology.organism_classification Fructokinase Fructokinases chemistry.chemical_compound Kinetics Enzyme chemistry Biochemistry Trichomonas Trichomonas vaginalis Animals Carbohydrate Metabolism Parasitology Glycolysis Hexose Tritrichomonas foetus Phosphorylation |
Zdroj: | The Journal of protozoology. 37(5) |
ISSN: | 0022-3921 |
Popis: | Trichomonas vaginalis and Tritrichomonas foetus contain glucokinase and not a hexokinase of broad hexose specificity. Tritrichomonas foetus also contains a specific fructokinase which could be resolved from glucokinase by anion exchange chromatography. Native T. vaginalis glucokinase had a Mr of 76,000, and SDS-PAG electrophoresis showed two equally stained bands corresponding to Mr 40,000 and 38,000. Glucose and ATP were by far the best substrates for both trichomonad glucokinases, with Km values as low as 33-35 microM and 75-83 microM, respectively. Substrate saturation curves for these enzymes were all hyperbolic. Tritrichomonas foetus fructokinase required fructose and ATP, with Km values of 200 microM and 81 microM. None of the activities was affected by a number of potential regulatory metabolites, including glucose-6-phosphate. The only exception was AMP which in supraphysiological concentrations had an inhibitory effect on T. foetus fructokinase. In conclusion, the absence of regulation at the hexose phosphorylation step described here, as well as the presence of an easily reversible PPi: fructose-6-phosphate 1-phosphotransferase described previously (Mertens, E., Van Schaftingen, E. & Muller, M. 1989. Mol. Biochem. Parasitol., 37:183-190), suggest that the rate of the 1st part of glycolysis in trichomonads is controlled only by the intracellular availability of hexoses. |
Databáze: | OpenAIRE |
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