Expression and characterization of human foamy virus proteinase

György Fenyöfalvi, Péter Bagossi, Terry D. Copeland, Stephen Oroszlan, Péter Boross, József Tözsér

Research output: Article

18 Citations (Scopus)


The human foamy virus proteinase was expressed in fusion with maltose binding protein in Escherichia coli and purified. The specific activity of the fusion protein was similar to that of the processed enzyme. The kinetic constants on foamy virus cleavage site substrates were very low but comparable to those obtained with the gag-encoded avian proteinase on its own substrates. The proteinase showed preference for high ionic strength and a pH optimum of 6.6. None of the tested retroviral cleavage site peptides were substrates, however, some peptides representing cleavage sites in retrotransposons were properly processed by the enzyme. Copyright (C) 1999 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)397-401
Number of pages5
JournalFEBS letters
Issue number3
Publication statusPublished - dec. 3 1999

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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