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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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Published in: | FEBS letters 1998-03, Vol.424 (1), p.46-48 |
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Main Authors: | , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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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. |
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ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/S0014-5793(98)00137-9 |