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• W1497441623 abstract "Recently, the mechanism of autoprocessing of the protease (PR) of the human immunodeficiency virus type 1 from the model polyprotein, MBP-ΔTF-PR-ΔPol, which contains the protease linked to short native flanking sequences (ΔTF and ΔPol) fused to the maltose binding protein (MBP) of Escherichia coli, was reported (Louis, J. M., Nashed, N. T., Parris, K. D., Kimmel, A. R., and Jerina, D. M.(1994) Proc. Natl. Acad. Sci. U. S. A. 91, 7970-7974). According to this mechanism, intramolecular cleavage of the N-terminal strands of the dimeric MBP-ΔTF-PR-ΔPol protein leads to the formation of the PR-ΔPol intermediate, which is subsequently converted to the mature protease by cleavage of the C-terminal strands. We now report the purification and characterization of the PR-ΔPol intermediate and the kinetics of its processing to the mature protease. Unlike the MBP-ΔTF-PR-ΔPol precursor, PR-ΔPol has proteolytic activity similar to that of the mature enzyme at pH 5.0. The pH rate profile for kcat/Km is similar to that of the mature protease above pH 4.0. Although the PR-ΔPol is more sensitive than the mature protease toward denaturing reagents, both the enzymatic activity and the intrinsic fluorescence of PR-ΔPol are linearly dependent on the protein concentration, indicating that the protein is largely in its dimeric form above 10 nM. In contrast to the first-order kinetics observed for the proteolytic reaction at the N terminus of the protease, the proteolytic reaction at the C terminus of the protease is second order in protein concentration. These results are discussed in terms of a mechanism in which the C-terminally located ΔPol peptide chains are cleaved intermolecularly to release the mature protease. Recently, the mechanism of autoprocessing of the protease (PR) of the human immunodeficiency virus type 1 from the model polyprotein, MBP-ΔTF-PR-ΔPol, which contains the protease linked to short native flanking sequences (ΔTF and ΔPol) fused to the maltose binding protein (MBP) of Escherichia coli, was reported (Louis, J. M., Nashed, N. T., Parris, K. D., Kimmel, A. R., and Jerina, D. M.(1994) Proc. Natl. Acad. Sci. U. S. A. 91, 7970-7974). According to this mechanism, intramolecular cleavage of the N-terminal strands of the dimeric MBP-ΔTF-PR-ΔPol protein leads to the formation of the PR-ΔPol intermediate, which is subsequently converted to the mature protease by cleavage of the C-terminal strands. We now report the purification and characterization of the PR-ΔPol intermediate and the kinetics of its processing to the mature protease. Unlike the MBP-ΔTF-PR-ΔPol precursor, PR-ΔPol has proteolytic activity similar to that of the mature enzyme at pH 5.0. The pH rate profile for kcat/Km is similar to that of the mature protease above pH 4.0. Although the PR-ΔPol is more sensitive than the mature protease toward denaturing reagents, both the enzymatic activity and the intrinsic fluorescence of PR-ΔPol are linearly dependent on the protein concentration, indicating that the protein is largely in its dimeric form above 10 nM. In contrast to the first-order kinetics observed for the proteolytic reaction at the N terminus of the protease, the proteolytic reaction at the C terminus of the protease is second order in protein concentration. These results are discussed in terms of a mechanism in which the C-terminally located ΔPol peptide chains are cleaved intermolecularly to release the mature protease." @default.
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• W1497441623 date "1996-02-01" @default.
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• W1497441623 title "A Transient Precursor of the HIV-1 Protease" @default.
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• W1497441623 doi "https://doi.org/10.1074/jbc.271.8.4477" @default.
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