0000000000997115

AUTHOR

Maria Bretner

0000-0002-9643-0843

showing 1 related works from this author

Thymidylate synthases from Hymenolepis diminuta and regenerating rat liver: purification, properties, and inhibition by substrate and cofactor analog…

1995

Comparative studies of thymidylate synthases, isolated from the tapeworm, Hymenolepis diminuta, and regenerating liver of its host, rat, aimed at a possibility of specific inhibition of the helminthic enzyme, are presented. While similar in structure (dimers with monomer molecular masses of 33.7 kDa and 34.9 kDa, respectively) and parameters describing interactions with substrates and products, the tapeworm and rat enzymes differed in the dependences of reaction velocity on temperature (Arrhenius plots biphasic and linear, respectively). The tapeworm, compared with the host, enzyme was less sensitive to the competitive slow-binding inhibition by 5-fluoro-dUMP and its 2-thio congener, but eq…

MaleStereochemistryBiophysicsBiochemistryThymidylate synthaseCofactorchemistry.chemical_compoundmethylenetetrahydrofolate analoguesNon-competitive inhibitionStructural BiologyValineFluorodeoxyuridylateAnimalsRats WistardUMPenzyme inhibitionMolecular BiologyTetrahydrofolatesHelminthic enzymechemistry.chemical_classificationAlaninebiologyTemperatureThymidylate SynthaseHymenolepis diminutabiology.organism_classificationLiver RegenerationRatsMolecular WeightKineticsEnzymechemistryBiochemistryLiverbiology.proteinNorvalineanalogues(H. diminuta)HymenolepisBiochimica et biophysica acta
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