Expression and characterization of human foamy virus proteinase

György Fenyöfalvi, P. Bagossi, Terry D. Copeland, Stephen Oroszlan, Péter Boross, J. Tőzsér

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

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
Volume462
Issue number3
DOIs
Publication statusPublished - Dec 3 1999

Fingerprint

Simian foamy virus
Peptide Hydrolases
Spumavirus
Maltose-Binding Proteins
Retroelements
Peptides
Substrates
Enzymes
Fusion reactions
Osmolar Concentration
Escherichia coli
Ionic strength
Viruses
Proteins
Kinetics
foamy virus proteinase

Keywords

  • Enzyme kinetics
  • Human foamy virus
  • Proteinase
  • Substrate specificity

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Expression and characterization of human foamy virus proteinase. / Fenyöfalvi, György; Bagossi, P.; Copeland, Terry D.; Oroszlan, Stephen; Boross, Péter; Tőzsér, J.

In: FEBS Letters, Vol. 462, No. 3, 03.12.1999, p. 397-401.

Research output: Contribution to journalArticle

Fenyöfalvi, György ; Bagossi, P. ; Copeland, Terry D. ; Oroszlan, Stephen ; Boross, Péter ; Tőzsér, J. / Expression and characterization of human foamy virus proteinase. In: FEBS Letters. 1999 ; Vol. 462, No. 3. pp. 397-401.
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