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The cytotoxin α-sarcin behaves as a cyclizing ribonuclease

The hydrolysis of adenylyl(3′→5′)adenosine (ApA) and guanylyl(3′→5′)adenosine (GpA) dinucleotides by the cytotoxic protein α-sarcin has been studied. Quantitative analysis of the reaction has been performed through reverse-phase chromatographic (HPLC) separation of the resulting products. The hydrol...

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Bibliographic Details
Published in:FEBS letters 1998-03, Vol.424 (1), p.46-48
Main Authors: Lacadena, Javier, Martı́nez del Pozo, Alvaro, Lacadena, Valle, Martı́nez-Ruiz, Antonio, Mancheño, José M, Oñaderra, Mercedes, Gavilanes, José G
Format: Article
Language:English
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Summary:The hydrolysis of adenylyl(3′→5′)adenosine (ApA) and guanylyl(3′→5′)adenosine (GpA) dinucleotides by the cytotoxic protein α-sarcin has been studied. Quantitative analysis of the reaction has been performed through reverse-phase chromatographic (HPLC) separation of the resulting products. The hydrolysis of the 3′-5′ phosphodiester bond of these substrates yields the 2′-3′ cyclic mononucleotide; this intermediate is converted into the corresponding 3′-monophosphate derivative as the final product of the reaction. The values of the apparent Michaelis constant ( K M), k cat and k cat/ K M have also been calculated. The obtained results fit into a two-step mechanism for the enzymatic activity of α-sarcin and allow to consider this protein as a cyclizing RNase.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(98)00137-9