Oxidation of thymidylate synthase by inorganic compounds

• Published in: Journal of inorganic biochemistry Vol. 22; no. 2; p. 119
• Main Authors: Aull, J L, Ivery, T C, Daron, H H
• Format: Journal Article
• Language: English
• Published: United States 01-10-1984
• Subjects: Indicators and Reagents; Iodides; Lactobacillus casei - enzymology; Methyltransferases - metabolism; Oxidation-Reduction; Periodic Acid; Potassium Permanganate; Thymidylate Synthase - metabolism
• ISSN: 0162-0134
• DOI: 10.1016/0162-0134(84)80020-3

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.