The cytotoxin α‐sarcin behaves as a cyclizing ribonuclease
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1998
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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.