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- W7855339 abstract "This chapter describes the structural chemistry and the biological aspects of Bovine Leukemia Virus (BLV) retropepsin. BLV retropepsin is also named as BLV endopeptidase, BLV protease or BLV proteinase. It contains the Asp-Thr-Gly sequence typical of the aspartic proteases and is inhibited by pepstatin A, an inhibitor of this class of enzyme. BLV retropepsin is a dimeric enzyme of about 28 kDa composed of two identical subunits of 126 residues (14 kDa) devoid of cysteine and histidine residues, and having a pI of 10.2. BLV retropepsin is able to hydrolyze its own N- and C-terminals and to process its precursor Gag into structural proteins of the matrix (MA), capsid (CA) and nucleocapsid (NC). BLV retropepsin processes the BLV precursors Gag and Gag-Pro into mature structural proteins and functional protease enabling formation of new infectious virions. BLV retropepsin is of interest because it can be used as a model for the study of the Human T-cell Leukemia Virus type I (HTLV-I) retropepsin." @default.
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- W7855339 date "2004-01-01" @default.
- W7855339 modified "2023-09-23" @default.
- W7855339 title "Bovine leukemia virus retropepsin" @default.
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- W7855339 doi "https://doi.org/10.1016/b978-0-12-079611-3.50055-0" @default.
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