title: Expression of virus-encoded proteinases: functional and structural similarities with cellular enzymes.
abstract: Many viruses express their genome, or part of their genome, initially as a polyprotein precursor that undergoes proteolytic processing. Molecular genetic analyses of viral gene expression have revealed that many of these processing events are mediated by virus-encoded proteinases. Biochemical activity studies and structural analyses of these viral enzymes reveal that they have remarkable similarities to cellular proteinases. However, the viral proteinases have evolved unique features that permit them to function in a cellular environment. In this article, the current status of plant and animal virus proteinases is described along with their role in the viral replication cycle. The reactions catalyzed by viral proteinases are not simple enzyme-substrate interactions; rather, the processing steps are highly regulated, are coordinated with other viral processes, and frequently involve the participation of other factors.
authors.affiliation: Department of Microbiology, Oregon State University, Corvallis 97331-3804.
authors.forename: W G
authors.initials: WG
authors.lastname: Dougherty
authors.forename: B L
authors.initials: BL
authors.lastname: Semler
mesh_terms: D000595:Amino Acid Sequence; D016282:Aspartic Acid Endopeptidases / Q000378:metabolism; D003546:Cysteine Endopeptidases / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism*; D008969:Molecular Sequence Data; D010942:Plant Viruses / Q000201:enzymology; D011499:Protein Processing, Post-Translational; D012697:Serine Endopeptidases / Q000378:metabolism; D014780:Viruses / Q000201:enzymology*
chemical_list: D010450:Endopeptidases; D012697:Serine Endopeptidases; D003546:Cysteine Endopeptidases; D016282:Aspartic Acid Endopeptidases