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  • Title: Oxidation of thymidylate synthase by inorganic compounds.
    Author: Aull JL, Ivery TC, Daron HH.
    Journal: J Inorg Biochem; 1984 Oct; 22(2):119-24. PubMed ID: 6094726.
    Abstract:
    Thymidylate synthase from methotrexate-resistant Lactobacillus casei was rapidly and completely inactivated by low concentrations of permanganate, periodate, or potassium triiodide at 0 degree C. The enzyme was not inactivated to any appreciable extent by iodate, iodide, ferricyanate, iodosobenzoate, or hydrogen peroxide. The inactivation by permanganate was retarded by the substrate 2'-deoxyuridylate and, to a lesser extent, by phosphate. Titration of enzyme activity with permanganate showed that two moles of permanganate were required to completely inactivate one mole of thymidylate synthase.
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