Inactivation of S-Adenosylhomocysteine hydrolase by 5′-deoxy-5′-methylthioadenosine

Adolph J. Ferro, Arthur A. Vandenbark, Margaret R. MacDonald

Research output: Contribution to journalArticlepeer-review

60 Scopus citations


S-Adenosylhomocysteine hydrolase from human red blood cells is inactivated by the naturally occurring metabolite, 5′-deoxy-5′-methylthioadenosine. Utilizing an 1896-fold purified enzyme preparation, the kinetics of inactivation by 5′-deoxy-5′-methylthioadenosine were examined and a KI value of 36 μM determined. Neither 5-methylthioribose nor adenine, degradation products of 5′-deoxy-5′-methylthioadenosine, inactivated the hydrolase, while both S-adenosylhomocysteine and adenosine protected the enzyme from inactivation by 5′-deoxy-5′-methylthioadenosine. The inactivation of S-adenosylhomocysteine hydrolase by 5′-deoxy-5′-methylthioadenosine may explain the cell growth inhibitory properties of this nucleoside.

Original languageEnglish (US)
Pages (from-to)523-531
Number of pages9
JournalBiochemical and Biophysical Research Communications
Issue number2
StatePublished - May 29 1981

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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