Expression and characterization of human foamy virus proteinase.
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.
Fenyöfalvi
G
G
Department of Biochemistry and Molecular Biology, University Medical School of Debrecen, Hungary.
Bagossi
P
P
Copeland
T D
TD
Oroszlan
S
S
Boross
P
P
Tözsér
J
J
D018528:ATP-Binding Cassette Transporters; D000595:Amino Acid Sequence; D016282:Aspartic Acid Endopeptidases / Q000096:biosynthesis* / Q000737:chemistry* / Q000302:isolation & purification; D002352:Carrier Proteins / Q000378:metabolism; D003001:Cloning, Molecular; D029968:Escherichia coli Proteins; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D058619:Maltose-Binding Proteins; D008969:Molecular Sequence Data; D009004:Monosaccharide Transport Proteins; D009842:Oligopeptides / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification; D018626:Retroelements; D012190:Retroviridae / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D013997:Time Factors
D018528:ATP-Binding Cassette Transporters; D002352:Carrier Proteins; D029968:Escherichia coli Proteins; D058619:Maltose-Binding Proteins; D009004:Monosaccharide Transport Proteins; D009842:Oligopeptides; D011993:Recombinant Fusion Proteins; D018626:Retroelements; C461599:maltose transport system, E coli; D016282:Aspartic Acid Endopeptidases; C096363:proteinase, foamy virus