The cytotoxin α‐sarcin behaves as a cyclizing ribonuclease

Citation
Lacadena Javier, Martı́nez del Pozo Alvaro, Lacadena Valle, Martı́nez-Ruiz Antonio, Mancheño José M, Oñaderra Mercedes and Gavilanes José G(1998), The cytotoxin α-sarcin behaves as a cyclizing ribonuclease, FEBS Letters, 424, doi: 10.1016/S0014-5793(98)00137-9
Abstract
The hydrolysis of adenylyl(3PC5P)adenosine (ApA) and guanylyl(3PC5P)adenosine (GpA) dinucleotides by the cytotoxic protein K-sarcin has been studied. Quantitative analysis of the reaction has been performed through reversephase chromatographic (HPLC) separation of the resulting products. The hydrolysis of the 3P-5P phosphodiester bond of these substrates yields the 2P-3P cyclic mononucleotide; this intermediate is converted into the corresponding 3P-monophosphate derivative as the final product of the reaction. The values of the apparent Michaelis constant (KM), kcat and kcat/ KM have also been calculated. The obtained results fit into a twostep mechanism for the enzymatic activity of K-sarcin and allow to consider this protein as a cyclizing RNase. z 1998 Federation of European Biochemical Societies.
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