Escherichia coli S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase. Purification, substrate specificity and mechanism of action.

@article{Ragione1985EscherichiaCS,
  title={Escherichia coli S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase. Purification, substrate specificity and mechanism of action.},
  author={Floriana Della Ragione and Marina Porcelli and Maria Carten{\`i}-Farina and Vincenzo Zappia and Anthony E. Pegg},
  journal={The Biochemical journal},
  year={1985},
  volume={232 2},
  pages={335-41}
}
S-Adenosylhomocysteine/5'-methylthioadenosine nucleosidase (EC 3.2.2.9) was purified to homogeneity from Escherichia coli to a final specific activity of 373 mumol of 5'-methylthioadenosine cleaved/min per mg of protein. Affinity chromatography on S-formycinylhomocysteine-Sepharose is the key step of the purification procedure. The enzyme, responsible for the cleavage of the glycosidic bond of both S-adenosylhomocysteine and 5'-methylthioadenosine, was partially characterized. The apparent Km… CONTINUE READING
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