The cytotoxin α‐sarcin behaves as a cyclizing ribonuclease
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 hydroly...
| Autores: | , , , , , , |
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| Tipo de recurso: | artículo |
| Fecha de publicación: | 1998 |
| País: | España |
| Institución: | Universidad Complutense de Madrid (UCM) |
| Repositorio: | Docta Complutense |
| Idioma: | inglés |
| OAI Identifier: | oai:docta.ucm.es:20.500.14352/103372 |
| Acceso en línea: | https://hdl.handle.net/20.500.14352/103372 |
| Access Level: | acceso abierto |
| Palabra clave: | 577.1 Dinucleotide Ribonucleolytic activity Ribosome-inactivating protein Ribotoxin Bioquímica (Química) 2302 Bioquímica |
| Sumario: | 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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